ID   TTHY_HUMAN              Reviewed;         147 AA.
AC   P02766; Q549C7; Q6IB96; Q9UBZ6; Q9UCM9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   27-MAR-2024, entry version 266.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=ATTR;
DE   AltName: Full=Prealbumin;
DE   AltName: Full=TBPA;
DE   Flags: Precursor;
GN   Name=TTR; Synonyms=PALB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=6093805; DOI=10.1016/0006-291x(84)91590-0;
RA   Mita S., Maeda S., Shimada K., Araki S.;
RT   "Cloning and sequence analysis of cDNA for human prealbumin.";
RL   Biochem. Biophys. Res. Commun. 124:558-564(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2990465; DOI=10.1016/0006-291x(85)91956-4;
RA   Wallace M.R., Naylor S.L., Kluve-Beckerman B., Long G.L., McDonald L.,
RA   Shows T.B., Benson M.D.;
RT   "Localization of the human prealbumin gene to chromosome 18.";
RL   Biochem. Biophys. Res. Commun. 129:753-758(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4054629; DOI=10.1016/0378-1119(85)90272-0;
RA   Sasaki H., Yoshioka N., Takagi Y., Sakaki Y.;
RT   "Structure of the chromosomal gene for human serum prealbumin.";
RL   Gene 37:191-197(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2995367; DOI=10.1016/s0021-9258(17)39013-0;
RA   Tsuzuki T., Mita S., Maeda S., Araki S., Shimada K.;
RT   "Structure of the human prealbumin gene.";
RL   J. Biol. Chem. 260:12224-12227(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AMYL-TTR MET-50.
RX   PubMed=3818577; DOI=10.1093/oxfordjournals.jbchem.a121826;
RA   Mita S., Maeda S., Shimada K., Araki S.;
RT   "Analyses of prealbumin mRNAs in individuals with familial amyloidotic
RT   polyneuropathy.";
RL   J. Biochem. 100:1215-1222(1986).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT AMYL-TTR MET-50.
RC   TISSUE=Liver;
RX   PubMed=3022108;
RA   Maeda S., Mita S., Araki S., Shimada K.;
RT   "Structure and expression of the mutant prealbumin gene associated with
RT   familial amyloidotic polyneuropathy.";
RL   Mol. Biol. Med. 3:329-338(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-28.
RC   TISSUE=Liver;
RX   PubMed=2015890; DOI=10.1016/0014-5793(91)80387-i;
RA   Christmanson L., Betsholtz C., Gustavsson A., Johansson B., Sletten K.,
RA   Westermark P.;
RT   "The transthyretin cDNA sequence is normal in transthyretin-derived senile
RT   systemic amyloidosis.";
RL   FEBS Lett. 281:177-180(1991).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1666289;
RA   Gu J.R., Jiang H.Q., He L.P., Li D.Z., Zhou X.M., Dai W.L., Qian L.F.,
RA   Chen Y.Q., Schweinfest C., Papas T.;
RT   "Transthyretin (prealbumin) gene in human primary hepatic cancer.";
RL   Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 34:1312-1318(1991).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Retina;
RX   PubMed=10328977; DOI=10.1006/exer.1998.0646;
RA   Getz R.K., Kennedy B.G., Mangini N.J.;
RT   "Transthyretin localization in cultured and native human retinal pigment
RT   epithelium.";
RL   Exp. Eye Res. 68:629-636(1999).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Corpus callosum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [15]
RP   PROTEIN SEQUENCE OF 21-147.
RX   PubMed=4607556; DOI=10.1016/s0021-9258(19)42128-5;
RA   Kanda Y., Goodman D.S., Canfield R.E., Morgan F.J.;
RT   "The amino acid sequence of human plasma prealbumin.";
RL   J. Biol. Chem. 249:6796-6805(1974).
RN   [16]
RP   PRELIMINARY PROTEIN SEQUENCE OF 21-147, AND VARIANT SER-26.
RX   PubMed=6300852; DOI=10.1073/pnas.80.2.539;
RA   Pras M., Prelli F., Franklin E.C., Frangione B.;
RT   "Primary structure of an amyloid prealbumin variant in familial
RT   polyneuropathy of Jewish origin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:539-542(1983).
RN   [17]
RP   PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX   PubMed=6651852; DOI=10.1016/s0006-291x(83)80224-1;
RA   Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S.;
RT   "Identification of amyloid prealbumin variant in familial amyloidotic
RT   polyneuropathy (Japanese type).";
RL   Biochem. Biophys. Res. Commun. 116:880-888(1983).
RN   [18]
RP   PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX   PubMed=6583672; DOI=10.1073/pnas.81.3.694;
RA   Dwulet F.E., Benson M.D.;
RT   "Primary structure of an amyloid prealbumin and its plasma precursor in a
RT   heredofamilial polyneuropathy of Swedish origin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:694-698(1984).
RN   [19]
RP   PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR ILE-142.
RX   PubMed=3135807; DOI=10.1016/0006-291x(88)90188-x;
RA   Cornwell G.G. III, Sletten K., Johansson B., Westermark P.;
RT   "Evidence that the amyloid fibril protein in senile systemic amyloidosis is
RT   derived from normal prealbumin.";
RL   Biochem. Biophys. Res. Commun. 154:648-653(1988).
RN   [20]
RP   PROTEIN SEQUENCE OF 21-147, AND VARIANT AMYL-TTR MET-50.
RX   PubMed=1517749; DOI=10.1016/0022-510x(92)90048-p;
RA   Kametani F., Ikeda S., Yanagisawa N., Ishi T., Hanyu N.;
RT   "Characterization of a transthyretin-related amyloid fibril protein from
RT   cerebral amyloid angiopathy in type I familial amyloid polyneuropathy.";
RL   J. Neurol. Sci. 108:178-183(1992).
RN   [21]
RP   PROTEIN SEQUENCE OF 21-41.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [22]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, AND VARIANT AMYL-TTR LEU-53.
RX   PubMed=1932142; DOI=10.1016/0925-4439(91)90033-6;
RA   Harding J., Skare J., Skinner M.;
RT   "A second transthyretin mutation at position 33 (Leu/Phe) associated with
RT   familial amyloidotic polyneuropathy.";
RL   Biochim. Biophys. Acta 1097:183-186(1991).
RN   [23]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR GLY-62, AND
RP   VARIANT ASN-110.
RX   PubMed=7923855; DOI=10.1111/j.1399-0004.1994.tb04030.x;
RA   Skare J.C., Jones L.A., Myles N., Kane K., Milunsky A., Cohen A.S.,
RA   Skinner M.;
RT   "Two transthyretin mutations (Glu42Gly, His90Asn) in an Italian family with
RT   amyloidosis.";
RL   Clin. Genet. 45:281-284(1994).
RN   [24]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
RX   PubMed=4044580; DOI=10.1016/s0021-9258(17)39100-7;
RA   Soprano D.R., Herbert J., Soprano K.J., Schon E.A., Goodman D.S.;
RT   "Demonstration of transthyretin mRNA in the brain and other extrahepatic
RT   tissues in the rat.";
RL   J. Biol. Chem. 260:11793-11798(1985).
RN   [25]
RP   PROTEIN SEQUENCE OF 42-68; 101-123 AND 125-146, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [26]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, AND VARIANT DTTRH THR-129.
RX   PubMed=1979335; DOI=10.1172/jci114938;
RA   Moses A.C., Rosen H.N., Moller D.E., Tsuzaki S., Haddow J.E., Lawlor J.,
RA   Liepnieks J.J., Nichols W.C., Benson M.D.;
RT   "A point mutation in transthyretin increases affinity for thyroxine and
RT   produces euthyroid hyperthyroxinemia.";
RL   J. Clin. Invest. 86:2025-2033(1990).
RN   [27]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7474944;
RA   Gustavsson A., Jahr H., Tobiassen R., Jacobson D.R., Sletten K.,
RA   Westermark P.;
RT   "Amyloid fibril composition and transthyretin gene structure in senile
RT   systemic amyloidosis.";
RL   Lab. Invest. 73:703-708(1995).
RN   [28]
RP   BINDING SITES FOR THYROID HORMONES.
RX   PubMed=201845; DOI=10.1038/268115a0;
RA   Blake C.C.F., Oatley S.J.;
RT   "Protein-DNA and protein-hormone interactions in prealbumin: a model of the
RT   thyroid hormone nuclear receptor?";
RL   Nature 268:115-120(1977).
RN   [29]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=3714052; DOI=10.1212/wnl.36.7.900;
RA   Herbert J., Wilcox J.N., Pham K.T., Fremeau R.T. Jr., Zeviani M., Dwork A.,
RA   Soprano D.R., Makover A., Goodman D.S., Zimmerman E.A., Roberts J.L.,
RA   Schon E.A.;
RT   "Transthyretin: a choroid plexus-specific transport protein in human brain.
RT   The 1986 S. Weir Mitchell award.";
RL   Neurology 36:900-911(1986).
RN   [30]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [31]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [32]
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-62, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=18221012; DOI=10.2174/092986608783330297;
RA   Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T.;
RT   "Detection of a gamma-carboxy-glutamate as novel post-translational
RT   modification of human transthyretin.";
RL   Protein Pept. Lett. 15:43-46(2008).
RN   [33]
RP   GLYCOSYLATION AT ASN-118, AND CHARACTERIZATION OF VARIANT AMYL-TTR GLY-38.
RX   PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
RA   Ruiz-Canada C., Kelleher D.J., Gilmore R.;
RT   "Cotranslational and posttranslational N-glycosylation of polypeptides by
RT   distinct mammalian OST isoforms.";
RL   Cell 136:272-283(2009).
RN   [34]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=4216640; DOI=10.1016/0022-2836(74)90291-5;
RA   Blake C.C.F., Geisow M.J., Swan I.D.A., Rerat C., Rerat B.;
RT   "Structure of human plasma prealbumin at 2.5-A resolution. A preliminary
RT   report on the polypeptide chain conformation, quaternary structure and
RT   thyroxine binding.";
RL   J. Mol. Biol. 88:1-12(1974).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=671542; DOI=10.1016/0022-2836(78)90368-6;
RA   Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C.;
RT   "Structure of prealbumin: secondary, tertiary and quaternary interactions
RT   determined by Fourier refinement at 1.8 A.";
RL   J. Mol. Biol. 121:339-356(1978).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
RX   PubMed=8382610; DOI=10.1002/j.1460-2075.1993.tb05707.x;
RA   Terry C.J., Damas A.M., Oliveira P., Saraiva M.J.M., Alves I.L.,
RA   Costa P.P., Matias P.M., Sakaki Y., Blake C.C.F.;
RT   "Structure of Met30 variant of transthyretin and its amyloidogenic
RT   implications.";
RL   EMBO J. 12:735-741(1993).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
RX   PubMed=8428915; DOI=10.1016/s0021-9258(18)53792-3;
RA   Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D.,
RA   Holmgren G., Sandgren O., Steen L.;
RT   "The X-ray crystal structure refinements of normal human transthyretin and
RT   the amyloidogenic Val-30-->Met variant to 1.7-A resolution.";
RL   J. Biol. Chem. 268:2416-2424(1993).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
RX   PubMed=7754382; DOI=10.1126/science.7754382;
RA   Monaco H.L., Rizzi M., Coda A.;
RT   "Structure of a complex of two plasma proteins: transthyretin and retinol-
RT   binding protein.";
RL   Science 268:1039-1041(1995).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
RX   PubMed=9818054; DOI=10.3109/13506129809003843;
RA   Schormann N., Murrell J.R., Benson M.D.;
RT   "Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin
RT   variants: new model for amyloid fibril formation.";
RL   Amyloid 5:175-187(1998).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PRO-75.
RX   PubMed=9733771; DOI=10.1074/jbc.273.38.24715;
RA   Sebastiao M.P., Saraiva M.J., Damas A.M.;
RT   "The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant
RT   reveals a possible pathway for transthyretin polymerization into amyloid
RT   fibrils.";
RL   J. Biol. Chem. 273:24715-24722(1998).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=9789022; DOI=10.1073/pnas.95.22.12956;
RA   Peterson S.A., Klabunde T., Lashuel H.A., Purkey H., Sacchettini J.C.,
RA   Kelly J.W.;
RT   "Inhibiting transthyretin conformational changes that lead to amyloid
RT   fibril formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12956-12960(1998).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP4, AND SUBUNIT.
RX   PubMed=10052934; DOI=10.1021/bi982291i;
RA   Naylor H.M., Newcomer M.E.;
RT   "The structure of human retinol-binding protein (RBP) with its carrier
RT   protein transthyretin reveals an interaction with the carboxy terminus of
RT   RBP.";
RL   Biochemistry 38:2647-2653(1999).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147.
RX   PubMed=10986125; DOI=10.1006/jmbi.2000.4078;
RA   Hoernberg A., Eneqvist T., Olofsson A., Lundgren E., Sauer-Eriksson A.E.;
RT   "A comparative analysis of 23 structures of the amyloidogenic protein
RT   transthyretin.";
RL   J. Mol. Biol. 302:649-669(2000).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10742177; DOI=10.1038/74082;
RA   Klabunde T., Petrassi H.M., Oza V.B., Raman P., Kelly J.W.,
RA   Sacchettini J.C.;
RT   "Rational design of potent human transthyretin amyloid disease
RT   inhibitors.";
RL   Nat. Struct. Biol. 7:312-321(2000).
RN   [46] {ECO:0007744|PDB:1ICT}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP   L-THYROXINE.
RX   PubMed=11418763; DOI=10.1107/s0907444901006047;
RA   Wojtczak A., Neumann P., Cody V.;
RT   "Structure of a new polymorphic monoclinic form of human transthyretin at 3
RT   A resolution reveals a mixed complex between unliganded and T4-bound
RT   tetramers of TTR.";
RL   Acta Crystallogr. D 57:957-967(2001).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-147, MUTAGENESIS OF PHE-107 AND
RP   LEU-130, IDENTIFICATION BY MASS SPECTROMETRY, FORMATION OF AMYLOID FIBERS
RP   AT ACIDIC PH, AND SUBUNIT.
RX   PubMed=11560492; DOI=10.1021/bi011194d;
RA   Jiang X., Smith C.S., Petrassi H.M., Hammarstroem P., White J.T.,
RA   Sacchettini J.C., Kelly J.W.;
RT   "An engineered transthyretin monomer that is nonamyloidogenic, unless it is
RT   partially denatured.";
RL   Biochemistry 40:11442-11452(2001).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 30-144 OF VARIANT AMYL-TTR MET-50
RP   AND VARIANT CHICAGO MET-139 IN COMPLEX WITH L-THYROXINE, AND SUBUNIT.
RX   PubMed=11243784; DOI=10.1006/jmbi.2000.4415;
RA   Sebastiao M.P., Lamzin V., Saraiva M.J., Damas A.M.;
RT   "Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis
RT   at atomic resolution.";
RL   J. Mol. Biol. 306:733-744(2001).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
RP   CYS-134.
RX   PubMed=12403615; DOI=10.1021/bi025800w;
RA   Eneqvist T., Olofsson A., Ando Y., Miyakawa T., Katsuragi S., Jass J.,
RA   Lundgren E., Sauer-Eriksson A.E.;
RT   "Disulfide-bond formation in the transthyretin mutant Y114C prevents
RT   amyloid fibril formation in vivo and in vitro.";
RL   Biochemistry 41:13143-13151(2002).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147IN COMPLEX WITH
RP   AMYLOIDOGENESIS INHIBITORS.
RX   PubMed=12820260; DOI=10.1002/anie.200351179;
RA   Razavi H., Palaninathan S.K., Powers E.T., Wiseman R.L., Purkey H.E.,
RA   Mohamedmohaideen N.N., Deechongkit S., Chiang K.P., Dendle M.T.A.,
RA   Sacchettini J.C., Kelly J.W.;
RT   "Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis,
RT   evaluation, and mechanism of action.";
RL   Angew. Chem. Int. Ed. 42:2758-2761(2003).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP   AMYLOIDOGENESIS INHIBITORS, AND FIBRIL FORMATION.
RX   PubMed=14583036; DOI=10.1021/ja030294z;
RA   Green N.S., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
RT   "Synthesis and characterization of potent bivalent amyloidosis inhibitors
RT   that bind prior to transthyretin tetramerization.";
RL   J. Am. Chem. Soc. 125:13404-13414(2003).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147 IN COMPLEX WITH DIFLUNISAL
RP   ANALOGS, AND INHIBITION OF AMYLOID FORMATION.
RX   PubMed=14711308; DOI=10.1021/jm030347n;
RA   Adamski-Werner S.L., Palaninathan S.K., Sacchettini J.C., Kelly J.W.;
RT   "Diflunisal analogues stabilize the native state of transthyretin. Potent
RT   inhibition of amyloidogenesis.";
RL   J. Med. Chem. 47:355-374(2004).
RN   [53]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PHE-98
RP   AND VARIANT HIS-124, AND SUBUNIT.
RX   PubMed=15735344; DOI=10.1107/s0907444904034316;
RA   Neto-Silva R.M., Macedo-Ribeiro S., Pereira P.J.B., Coll M., Saraiva M.J.,
RA   Damas A.M.;
RT   "X-ray crystallographic studies of two transthyretin variants: further
RT   insights into amyloidogenesis.";
RL   Acta Crystallogr. D 61:333-339(2005).
RN   [54]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEXES WITH CHLORIDE
RP   AND IODIDE IONS.
RX   PubMed=15981995; DOI=10.1021/bi050249z;
RA   Hoernberg A., Hultdin U.W., Olofsson A., Sauer-Eriksson A.E.;
RT   "The effect of iodide and chloride on transthyretin structure and
RT   stability.";
RL   Biochemistry 44:9290-9299(2005).
RN   [55]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR
RP   CYS-134.
RX   PubMed=16185074; DOI=10.1021/bi050795s;
RA   Karlsson A., Olofsson A., Eneqvist T., Sauer-Eriksson A.E.;
RT   "Cys114-linked dimers of transthyretin are compatible with amyloid
RT   formation.";
RL   Biochemistry 44:13063-13070(2005).
RN   [56]
RP   X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-147 IN COMPLEX WITH THYROID
RP   HORMONE ANALOG, AND SUBUNIT.
RX   PubMed=15826192; DOI=10.1021/ja042929f;
RA   Wiseman R.L., Johnson S.M., Kelker M.S., Foss T., Wilson I.A., Kelly J.W.;
RT   "Kinetic stabilization of an oligomeric protein by a single ligand binding
RT   event.";
RL   J. Am. Chem. Soc. 127:5540-5551(2005).
RN   [57]
RP   X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 31-147, AND SUBUNIT.
RX   PubMed=15769474; DOI=10.1016/j.jmb.2005.01.050;
RA   Foss T.R., Kelker M.S., Wiseman R.L., Wilson I.A., Kelly J.W.;
RT   "Kinetic stabilization of the native state by protein engineering:
RT   implications for inhibition of transthyretin amyloidogenesis.";
RL   J. Mol. Biol. 347:841-854(2005).
RN   [58]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND VARIANTS
RP   AMYL-TTR PRO-75 AND PHE-98.
RX   PubMed=16627944; DOI=10.1107/s0907444906006962;
RA   Morais-de-Sa E., Neto-Silva R.M., Pereira P.J.B., Saraiva M.J., Damas A.M.;
RT   "The binding of 2,4-dinitrophenol to wild-type and amyloidogenic
RT   transthyretin.";
RL   Acta Crystallogr. D 62:512-519(2006).
RN   [59] {ECO:0007744|PDB:2H4E}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-147, AND SULFATION AT CYS-30.
RX   PubMed=17175208; DOI=10.1016/j.bbapap.2006.10.015;
RA   Gales L., Saraiva M.J., Damas A.M.;
RT   "Structural basis for the protective role of sulfite against transthyretin
RT   amyloid formation.";
RL   Biochim. Biophys. Acta 1774:59-64(2007).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147.
RX   PubMed=17196219; DOI=10.1016/j.jmb.2006.11.076;
RA   Pasquato N., Berni R., Folli C., Alfieri B., Cendron L., Zanotti G.;
RT   "Acidic pH-induced conformational changes in amyloidogenic mutant
RT   transthyretin.";
RL   J. Mol. Biol. 366:711-719(2007).
RN   [61]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP   3,5-DIIODOSALICYLIC ACID, AND THYROXINE BINDING.
RX   PubMed=18155178; DOI=10.1016/j.bbapap.2007.11.014;
RA   Gales L., Almeida M.R., Arsequell G., Valencia G., Saraiva M.J.,
RA   Damas A.M.;
RT   "Iodination of salicylic acid improves its binding to transthyretin.";
RL   Biochim. Biophys. Acta 1784:512-517(2008).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 21-147 IN COMPLEX WITH RBP4.
RX   PubMed=19021760; DOI=10.1111/j.1742-4658.2008.06705.x;
RA   Zanotti G., Folli C., Cendron L., Alfieri B., Nishida S.K., Gliubich F.,
RA   Pasquato N., Negro A., Berni R.;
RT   "Structural and mutational analyses of protein-protein interactions between
RT   transthyretin and retinol-binding protein.";
RL   FEBS J. 275:5841-5854(2008).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147 IN COMPLEX WITH
RP   2-ARYLBENZOXAZOLE-BASED TRANSTHYRETIN AMYLOIDOGENESIS INHIBITORS.
RX   PubMed=18095641; DOI=10.1021/jm0708735;
RA   Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
RT   "Biochemical and structural evaluation of highly selective 2-
RT   arylbenzoxazole-based transthyretin amyloidogenesis inhibitors.";
RL   J. Med. Chem. 51:260-270(2008).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-147 IN COMPLEX WITH BISARYL
RP   AMYLOIDOGENESIS INHIBITORS.
RX   PubMed=18811132; DOI=10.1021/jm800435s;
RA   Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.;
RT   "Toward optimization of the linker substructure common to transthyretin
RT   amyloidogenesis inhibitors using biochemical and structural studies.";
RL   J. Med. Chem. 51:6348-6358(2008).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 21-147 AT PH 3.5 AND 4.5.
RX   PubMed=18662699; DOI=10.1016/j.jmb.2008.07.029;
RA   Palaninathan S.K., Mohamedmohaideen N.N., Snee W.C., Kelly J.W.,
RA   Sacchettini J.C.;
RT   "Structural insight into pH-induced conformational changes within the
RT   native human transthyretin tetramer.";
RL   J. Mol. Biol. 382:1157-1167(2008).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-147.
RG   Mycobacterium tuberculosis structural genomics consortium (TB);
RT   "Crystal structure of the F87M/L110M mutant of human transthyretin at pH
RT   4.6 soaked.";
RL   Submitted (JUL-2008) to the PDB data bank.
RN   [67]
RP   REVIEW ON VARIANTS.
RX   PubMed=7599630; DOI=10.1002/humu.1380050302;
RA   Saraiva M.J.M.;
RT   "Transthyretin mutations in health and disease.";
RL   Hum. Mutat. 5:191-196(1995).
RN   [68]
RP   VARIANT AMYL-TTR ILE-53.
RX   PubMed=6487335; DOI=10.1016/s0006-291x(84)80222-3;
RA   Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S.;
RT   "Revised analysis of amino acid replacement in a prealbumin variant (SKO-
RT   III) associated with familial amyloidotic polyneuropathy of Jewish
RT   origin.";
RL   Biochem. Biophys. Res. Commun. 123:921-928(1984).
RN   [69]
RP   VARIANT AMYL-TTR SER-104.
RX   PubMed=3722385; DOI=10.1172/jci112573;
RA   Wallace M.R., Dwulet F.E., Conneally P.M., Benson M.D.;
RT   "Biochemical and molecular genetic characterization of a new variant
RT   prealbumin associated with hereditary amyloidosis.";
RL   J. Clin. Invest. 78:6-12(1986).
RN   [70]
RP   VARIANT VAL-136.
RX   PubMed=3675594; DOI=10.1016/0006-291x(87)91135-1;
RA   Strahler J.R., Rosenblum B.B., Hanash S.M.;
RT   "Identification and characterization of a human transthyretin variant.";
RL   Biochem. Biophys. Res. Commun. 148:471-477(1987).
RN   [71]
RP   VARIANT AMYL-TTR TYR-97.
RX   PubMed=2891727; DOI=10.1172/jci113293;
RA   Wallace M.R., Dwulet F.E., Williams E.C., Conneally P.M., Benson M.D.;
RT   "Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77,
RT   and detection of the gene by DNA analysis.";
RL   J. Clin. Invest. 81:189-193(1988).
RN   [72]
RP   VARIANT AMYL-TTR CYS-134.
RX   PubMed=2161654; DOI=10.1016/0006-291x(90)91445-x;
RA   Ueno S., Uemichi T., Yorifuji S., Tarui S.;
RT   "A novel variant of transthyretin (Tyr114 to Cys) deduced from the
RT   nucleotide sequences of gene fragments from familial amyloidotic
RT   polyneuropathy in Japanese sibling cases.";
RL   Biochem. Biophys. Res. Commun. 169:143-147(1990).
RN   [73]
RP   VARIANTS AMYL-TTR GLY-62 AND ARG-70.
RX   PubMed=2363717; DOI=10.1016/0006-291x(90)92011-n;
RA   Ueno S., Uemichi T., Takahashi N., Soga F., Yorifuji S., Tarui S.;
RT   "Two novel variants of transthyretin identified in Japanese cases with
RT   familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and
RT   transthyretin (Ser50 to Arg).";
RL   Biochem. Biophys. Res. Commun. 169:1117-1121(1990).
RN   [74]
RP   VARIANT CHICAGO MET-139.
RX   PubMed=1877623; DOI=10.1002/ajmg.1320390415;
RA   Harrison H.H., Gordon E.D., Nichols W.C., Benson M.D.;
RT   "Biochemical and clinical characterization of prealbuminCHICAGO: an
RT   apparently benign variant of serum prealbumin (transthyretin) discovered
RT   with high-resolution two-dimensional electrophoresis.";
RL   Am. J. Med. Genet. 39:442-452(1991).
RN   [75]
RP   VARIANT AMYL-TTR ARG-78.
RX   PubMed=1656975; DOI=10.1016/s0006-291x(05)81304-x;
RA   Saeki Y., Ueno S., Yorifuji S., Sugiyama Y., Ide Y., Matsuzawa Y.;
RT   "New mutant gene (transthyretin Arg 58) in cases with hereditary
RT   polyneuropathy detected by non-isotope method of single-strand conformation
RT   polymorphism analysis.";
RL   Biochem. Biophys. Res. Commun. 180:380-385(1991).
RN   [76]
RP   VARIANT ASN-110.
RX   PubMed=1997217; DOI=10.1111/j.1399-0004.1991.tb02979.x;
RA   Skare J.C., Milunsky J.M., Milunsky A., Skare I.B., Cohen A.S., Skinner M.;
RT   "A new transthyretin variant from a patient with familial amyloidotic
RT   polyneuropathy has asparagine substituted for histidine at position 90.";
RL   Clin. Genet. 39:6-12(1991).
RN   [77]
RP   VARIANTS AMYL-TTR LEU-53 AND LEU-84.
RX   PubMed=2046936; DOI=10.1212/wnl.41.6.893;
RA   Li S., Minnerath S., Li K., Dyck P.J., Sommer S.S.;
RT   "Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two
RT   novel point mutations.";
RL   Neurology 41:893-898(1991).
RN   [78]
RP   VARIANT AMYL-TTR THR-65.
RX   PubMed=1570831;
RA   Saraiva M.J.M., Almeida M.R., Sherman W., Gawinowicz M., Costa P.,
RA   Costa P.P., Goodman D.S.;
RT   "A new transthyretin mutation associated with amyloid cardiomyopathy.";
RL   Am. J. Hum. Genet. 50:1027-1030(1992).
RN   [79]
RP   VARIANT AMYL-TTR ARG-67.
RX   PubMed=1734866; DOI=10.1016/0006-291x(92)91763-g;
RA   Murakami T., Maeda S., Yi S., Ikegawa S., Kawashima E., Onodera S.,
RA   Shimada K., Araki S.;
RT   "A novel transthyretin mutation associated with familial amyloidotic
RT   polyneuropathy.";
RL   Biochem. Biophys. Res. Commun. 182:520-526(1992).
RN   [80]
RP   VARIANT AMYL-TTR LEU-50.
RX   PubMed=1520326; DOI=10.1016/s0006-291x(05)81506-2;
RA   Murakami T., Atsumi T., Maeda S., Tanase S., Ishikawa K., Mita S.,
RA   Kumamoto T., Araki S., Ando M.;
RT   "A novel transthyretin mutation at position 30 (Leu for Val) associated
RT   with familial amyloidotic polyneuropathy.";
RL   Biochem. Biophys. Res. Commun. 187:397-403(1992).
RN   [81]
RP   VARIANT AMYL-TTR ILE-70.
RX   PubMed=1520336; DOI=10.1016/s0006-291x(05)81516-5;
RA   Nishi H., Kimura A., Harada H., Hayashi Y., Nakamura M., Sasazuki T.;
RT   "Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac
RT   amyloidosis.";
RL   Biochem. Biophys. Res. Commun. 187:460-466(1992).
RN   [82]
RP   VARIANT AMYL-TTR ALA-50.
RX   PubMed=1544214; DOI=10.1111/j.1399-0004.1992.tb03635.x;
RA   Jones L.A., Skare J.C., Cohen A.S., Harding J.A., Milunsky A., Skinner M.;
RT   "Familial amyloidotic polyneuropathy: a new transthyretin position 30
RT   mutation (alanine for valine) in a family of German descent.";
RL   Clin. Genet. 41:70-73(1992).
RN   [83]
RP   VARIANT AMYL-TTR PRO-75.
RX   PubMed=1351039; DOI=10.1007/bf00220559;
RA   Jacobson D.R., McFarlin D.E., Kane I., Buxbaum J.N.;
RT   "Transthyretin Pro55, a variant associated with early-onset, aggressive,
RT   diffuse amyloidosis with cardiac and neurologic involvement.";
RL   Hum. Genet. 89:353-356(1992).
RN   [84]
RP   VARIANTS AMYL-TTR ALA-69 AND GLN-109.
RX   PubMed=1301926; DOI=10.1002/humu.1380010306;
RA   Almeida M.R., Ferlini A., Forabosco A., Gawinowicz M.A., Costa P.P.,
RA   Salvi F., Plasmati R., Tassinari C.A., Altland K., Saraiva M.J.;
RT   "Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian
RT   kindreds with hereditary amyloidosis.";
RL   Hum. Mutat. 1:211-215(1992).
RN   [85]
RP   VARIANT AMYL-TTR ARG-30.
RX   PubMed=1362222; DOI=10.1136/jmg.29.12.888;
RA   Uemichi T., Murrel J.R., Zeldenrust S., Benson M.D.;
RT   "A new mutant transthyretin (Arg 10) associated with familial amyloid
RT   polyneuropathy.";
RL   J. Med. Genet. 29:888-891(1992).
RN   [86]
RP   VARIANT AMYL-TTR ASN-90.
RX   PubMed=1436517; DOI=10.1212/wnl.42.11.2094;
RA   Izumoto S., Younger D., Hays A.P., Martone R.L., Smith R.T., Herbert J.;
RT   "Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome
RT   and a new transthyretin mutation, asparagine 70.";
RL   Neurology 42:2094-2102(1992).
RN   [87]
RP   VARIANT AMYL-TTR LYS-81.
RX   PubMed=8352764; DOI=10.1006/bbrc.1993.1933;
RA   Shiomi K., Nakazato M., Matsukura S., Ohnishi A., Hatanaka H., Tsuji S.,
RA   Murai Y., Kojima M., Kangawa K., Matsuo H.;
RT   "A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic
RT   polyneuropathy: protein and DNA sequencing and PCR-induced mutation
RT   restriction analysis.";
RL   Biochem. Biophys. Res. Commun. 194:1090-1096(1993).
RN   [88]
RP   VARIANT AMYL-TTR LEU-88.
RX   PubMed=8038017; DOI=10.1136/hrt.70.2.111;
RA   Hesse A., Altland K., Linke R.P., Almeida M.R., Saraiva M.J.M.,
RA   Steinmetz A., Maisch B.;
RT   "Cardiac amyloidosis: a review and report of a new transthyretin
RT   (prealbumin) variant.";
RL   Br. Heart J. 70:111-115(1993).
RN   [89]
RP   VARIANT AMYL-TTR ALA-91.
RX   PubMed=8257997; DOI=10.1002/humu.1380020516;
RA   Almeida M.R., Lopez-Andreu F., Munar-Ques M., Costa P.P., Saraiva M.J.;
RT   "Transthyretin Ala-71: a new transthyretin variant in a Spanish family with
RT   familial amyloidotic polyneuropathy.";
RL   Hum. Mutat. 2:420-421(1993).
RN   [90]
RP   VARIANT AMYL-TTR ALA-91.
RX   PubMed=8095302; DOI=10.1136/jmg.30.2.120;
RA   Benson M.D. II, Turpin J.C., Lucotte G., Zeldenrust S., Lechevalier B.,
RA   Benson M.D.;
RT   "A transthyretin variant (alanine 71) associated with familial amyloidotic
RT   polyneuropathy in a French family.";
RL   J. Med. Genet. 30:120-122(1993).
RN   [91]
RP   VARIANT AMYL-TTR ALA-67.
RA   Ferlini A., Salvi F., Patrosso C., Fini S., Vezzoni P., Forbasco A.;
RT   "Gly47Ala: a new transthyretin gene mutation in hereditary amyloidosis TTR-
RT   related.";
RL   J. Rheumatol. 20:187-187(1993).
RN   [92]
RP   VARIANT SER-26, AND VARIANT AMYL-TTR ILE-53.
RX   PubMed=8019560; DOI=10.1002/humu.1380030313;
RA   Jacobson D.R., Buxbaum J.N.;
RT   "A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli
RT   patient 'SKO' with familial amyloidotic polyneuropathy.";
RL   Hum. Mutat. 3:254-260(1994).
RN   [93]
RP   VARIANT AMYL-TTR VAL-127.
RX   PubMed=8081397; DOI=10.1002/humu.1380030414;
RA   Jacobson D., Gertz M.A., Buxbaum J.N.;
RT   "Transthyretin VAL107, a new variant associated with familial cardiac and
RT   neuropathic amyloidosis.";
RL   Hum. Mutat. 3:399-401(1994).
RN   [94]
RP   VARIANT SER-104, AND RBP BINDING STUDIES.
RX   PubMed=8089102; DOI=10.1016/s0021-9258(17)31527-2;
RA   Berni R., Malpeli G., Folli C., Murrell J.R., Liepnieks J.J., Benson M.D.;
RT   "The Ile-84-->Ser amino acid substitution in transthyretin interferes with
RT   the interaction with plasma retinol-binding protein.";
RL   J. Biol. Chem. 269:23395-23398(1994).
RN   [95]
RP   VARIANT AMYL-TTR VAL-127.
RX   PubMed=7914929; DOI=10.1136/jmg.31.5.416;
RA   Uemichi T., Gertz M.A., Benson M.D.;
RT   "Amyloid polyneuropathy in two German-American families: a new
RT   transthyretin variant (Val 107).";
RL   J. Med. Genet. 31:416-417(1994).
RN   [96]
RP   VARIANT AMYL-TTR GLY-117.
RX   PubMed=8133316; DOI=10.1016/0022-510x(94)90162-7;
RA   Yasuda T., Sobue G., Doyu M., Nakazato M., Shiomi K., Yanagi T.,
RA   Mitsuma T.;
RT   "Familial amyloidotic polyneuropathy with late-onset and well-preserved
RT   autonomic function: a Japanese kindred with novel mutant transthyretin
RT   (Ala97 to Gly).";
RL   J. Neurol. Sci. 121:97-102(1994).
RN   [97]
RP   VARIANT AMYL-TTR PRO-75.
RX   PubMed=7910950; DOI=10.1002/mus.880170611;
RA   Yamamoto K., Hsu S.P., Yoshida K., Ikeda S., Nakazato M., Shiomi K.,
RA   Cheng S.Y., Furihata K., Ueno I., Yanagisawa N.;
RT   "Familial amyloid polyneuropathy in Taiwan: identification of transthyretin
RT   variant (Leu55-->Pro).";
RL   Muscle Nerve 17:637-641(1994).
RN   [98]
RP   VARIANT CTS1 HIS-134.
RX   PubMed=8309582; DOI=10.1212/wnl.44.2.315;
RA   Murakami T., Tachibana S., Endo Y., Kawai R., Hara M., Tanase S., Ando M.;
RT   "Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114
RT   variant.";
RL   Neurology 44:315-318(1994).
RN   [99]
RP   VARIANTS AMYL-TTR MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND
RP   GLN-109.
RX   PubMed=7655883; DOI=10.1093/brain/118.4.849;
RA   Reilly M.M., Adams D., Booth D.R., Davis M.B., Said G.,
RA   Laubriat-Bianchin M., Pepys M.B., Thomas P.K., Harding A.E.;
RT   "Transthyretin gene analysis in European patients with suspected familial
RT   amyloid polyneuropathy.";
RL   Brain 118:849-856(1995).
RN   [100]
RP   VARIANT AMYL-TTR LYS-79.
RX   PubMed=7850982; DOI=10.1161/01.cir.91.4.962;
RA   Booth D.R., Tan S.Y., Hawkins P.N., Pepys M.B., Frustaci A.;
RT   "A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal
RT   dominant cardiac amyloidosis in an Italian family.";
RL   Circulation 91:962-967(1995).
RN   [101]
RP   VARIANT AMYL-TTR GLY-38.
RX   PubMed=8579098;
RA   Vidal R., Garzuly F., Budka H., Lalowski M., Linke R.P., Brittig F.,
RA   Frangione B., Wisniewski T.;
RT   "Meningocerebrovascular amyloidosis associated with a novel transthyretin
RT   mis-sense mutation at codon 18 (TTRD 18G).";
RL   Am. J. Pathol. 148:361-366(1996).
RN   [102]
RP   VARIANT AMYL-TTR GLY-50.
RX   PubMed=9066351; DOI=10.1002/ana.410410305;
RA   Petersen R.B., Goren H., Cohen M., Richardson S.L., Tresser N., Lynn A.,
RA   Gali M., Estes M., Gambetti P.;
RT   "Transthyretin amyloidosis: a new mutation associated with dementia.";
RL   Ann. Neurol. 41:307-313(1997).
RN   [103]
RP   VARIANT AMYL-TTR ILE-40.
RX   PubMed=8990019;
RX   DOI=10.1002/(sici)1098-1004(1997)9:1<83::aid-humu19>3.0.co;2-l;
RA   Jacobson D.R., Pan T., Kyle R.A., Buxbaum J.N.;
RT   "Transthyretin ILE20, a new variant associated with late-onset cardiac
RT   amyloidosis.";
RL   Hum. Mutat. 9:83-85(1997).
RN   [104]
RP   VARIANT AMYL-TTR THR-54.
RX   PubMed=9605286;
RX   DOI=10.1002/(sici)1096-8628(19980501)77:2<135::aid-ajmg5>3.0.co;2-r;
RA   Patrosso M.C., Salvi F., De Grandis D., Vezzoni P., Jacobson D.R.,
RA   Ferlini A.;
RT   "Novel transthyretin missense mutation (Thr34) in an Italian family with
RT   hereditary amyloidosis.";
RL   Am. J. Med. Genet. 77:135-138(1998).
RN   [105]
RP   VARIANT AMYL-TTR ASP-62.
RX   PubMed=10036587; DOI=10.3109/13506129809007302;
RA   Dupuy O., Bletry O., Blanc A.S., Droz D., Viemont M., Delpech M.,
RA   Grateau G.;
RT   "A novel variant of transthyretin (Glu42Asp) associated with sporadic late-
RT   onset cardiac amyloidosis.";
RL   Amyloid 5:285-287(1998).
RN   [106]
RP   VARIANTS AMYL-TTR SER-111 AND SER-136.
RX   PubMed=10627135;
RX   DOI=10.1002/(sici)1098-1004(1998)12:1<71::aid-humu15>3.0.co;2-7;
RA   Misrahi A.M., Plante V., Lalu T., Serre I., Adams D., Lacroix D.C.,
RA   Said G.;
RT   "New transthyretin variants Ser 91 and Ser 116 associated with familial
RT   amyloidotic polyneuropathy.";
RL   Hum. Mutat. 12:71-71(1998).
RN   [107]
RP   VARIANT AMYL-TTR VAL-93.
RX   PubMed=10694917;
RX   DOI=10.1002/(sici)1098-1004(1998)12:2<135::aid-humu10>3.0.co;2-6;
RA   Booth D.R., Gillmore J.D., Persey M.R., Booth S.E., Cafferty K.D.,
RA   Tennent G.A., Madhoo S., Cochrane S.W., Whitehead T.C., Pasvol G.,
RA   Hawkins P.N.;
RT   "Transthyretin Ile73Val is associated with familial amyloidotic
RT   polyneuropathy in a Bangladeshi family.";
RL   Hum. Mutat. 12:135-135(1998).
RN   [108]
RP   VARIANT SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10671063;
RA   Kishikawa M., Nakanishi T., Miyazaki A., Hatanaka M., Shimizu A.,
RA   Tamoto S., Ohsawa N., Hayashi H., Kanai M.;
RT   "A new nonamyloid transthyretin variant, G101S, detected by electrospray
RT   ionization/mass spectrometry.";
RL   Hum. Mutat. 12:363-363(1998).
RN   [109]
RP   VARIANT SER-64.
RX   PubMed=9818883; DOI=10.1212/wnl.51.5.1462;
RA   Klein C.J., Nakumura M., Jacobson D.R., Lacy M.Q., Benson M.D.,
RA   Petersen R.C.;
RT   "Transthyretin amyloidosis (serine 44) with headache, hearing loss, and
RT   peripheral neuropathy.";
RL   Neurology 51:1462-1464(1998).
RN   [110]
RP   VARIANT AMYL-TTR ALA-142, VARIANT SER-26, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=10211412; DOI=10.3109/13506129908993288;
RA   Theberge R., Connors L., Skare J., Skinner M., Falk R.H., Costello C.E.;
RT   "A new amyloidogenic transthyretin variant (Val122Ala) found in a compound
RT   heterozygous patient.";
RL   Amyloid 6:54-58(1999).
RN   [111]
RP   VARIANT AMYL-TTR ASN-43, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10439117; DOI=10.3109/13506129909007311;
RA   Connors L.H., Theberge R., Skare J., Costello C.E., Falk R.H., Skinner M.;
RT   "A new transthyretin variant (Ser23Asn) associated with familial
RT   amyloidosis in a Portuguese patient.";
RL   Amyloid 6:114-118(1999).
RN   [112]
RP   VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10611950; DOI=10.3109/13506129909007341;
RA   Tachibana N., Tokuda T., Yoshida K., Taketomi T., Nakazato M., Li Y.F.,
RA   Masuda Y., Ikeda S.;
RT   "Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum
RT   variant transthyretin in the diagnosis of familial amyloid
RT   polyneuropathy.";
RL   Amyloid 6:282-288(1999).
RN   [113]
RP   VARIANT HIS-124, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10529370; DOI=10.1006/bbrc.1999.1514;
RA   Terazaki H., Ando Y., Misumi S., Nakamura M., Ando E., Matsunaga N.,
RA   Shoji S., Okuyama M., Ideta H., Nakagawa K., Ishizaki T., Ando M.,
RA   Saraiva M.J.;
RT   "A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with high
RT   serum transthyretin (TTR) and retinol binding protein (RBP) levels.";
RL   Biochem. Biophys. Res. Commun. 264:365-370(1999).
RN   [114]
RP   VARIANT AMYL-TTR PRO-32.
RX   PubMed=10071047; DOI=10.1093/brain/122.2.183;
RA   Brett M., Persey M.R., Reilly M.M., Revesz T., Booth D.R., Booth S.E.,
RA   Hawkins P.N., Pepys M.B., Morgan-Hughes J.A.;
RT   "Transthyretin Leu12Pro is associated with systemic, neuropathic and
RT   leptomeningeal amyloidosis.";
RL   Brain 122:183-190(1999).
RN   [115]
RP   VARIANT AMYL-TTR ILE-69, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10436378; DOI=10.1159/000022872;
RA   Nakamura M., Yamashita T., Ando Y., Hamidi Asl K., Tashima K., Ohlsson P.,
RA   Kususe Y., Benson M.D.;
RT   "Identification of a new transthyretin variant (Ile49) in familial
RT   amyloidotic polyneuropathy using electrospray ionization mass spectrometry
RT   and nonisotopic RNase cleavage assay.";
RL   Hum. Hered. 49:186-189(1999).
RN   [116]
RP   VARIANT AMYL-TTR LYS-109.
RX   PubMed=10842705; DOI=10.3109/13506120009146824;
RA   Nakamura M., Hamidi Asl K., Benson M.D.;
RT   "A novel variant of transthyretin (Glu89Lys) associated with familial
RT   amyloidotic polyneuropathy.";
RL   Amyloid 7:46-50(2000).
RN   [117]
RP   VARIANT AMYL-TTR SER-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10842718; DOI=10.3109/13506120009146252;
RA   Janunger T., Anan I., Holmgren G., Lovheim O., Ohlsson P.I., Suhr O.B.,
RA   Tashima K.;
RT   "Heart failure caused by a novel amyloidogenic mutation of the
RT   transthyretin gene: ATTR Ala45Ser.";
RL   Amyloid 7:137-140(2000).
RN   [118]
RP   VARIANT AMYL-TTR MET-48.
RX   PubMed=10882995;
RX   DOI=10.1002/1097-4598(200007)23:7<1016::aid-mus3>3.0.co;2-w;
RA   de Carvalho M., Moreira P., Evangelista T., Ducla-Soares J.L., Bento M.,
RA   Fernandes R., Saraiva M.J.;
RT   "New transthyretin mutation V28M in a Portuguese kindred with amyloid
RT   polyneuropathy.";
RL   Muscle Nerve 23:1016-1021(2000).
RN   [119]
RP   VARIANT AMYL-TTR GLU-73.
RX   PubMed=11445644; DOI=10.1212/wnl.57.1.135;
RA   Ellie E., Camou F., Vital A., Rummens C., Grateau G., Delpech M.,
RA   Valleix S.;
RT   "Recurrent subarachnoid hemorrhage associated with a new transthyretin
RT   variant (Gly53Glu).";
RL   Neurology 57:135-137(2001).
RN   [120]
RP   VARIANT AMYL-TTR GLN-75.
RX   PubMed=12557757; DOI=10.3109/13506120209114105;
RA   Yazaki M., Varga J., Dyck P.J., Benson M.D.;
RT   "A new transthyretin variant Leu55Gln in a patient with systemic
RT   amyloidosis.";
RL   Amyloid 9:268-271(2002).
RN   [121]
RP   VARIANTS SER-26 AND MET-139, VARIANTS AMYL-TTR ALA-58; LEU-61; SER-64 AND
RP   LEU-84, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11866053; DOI=10.1021/ac010780+;
RA   Lim A., Prokaeva T., McComb M.E., O'Connor P.B., Theberge R., Connors L.H.,
RA   Skinner M., Costello C.E.;
RT   "Characterization of transthyretin variants in familial transthyretin
RT   amyloidosis by mass spectrometric peptide mapping and DNA sequence
RT   analysis.";
RL   Anal. Chem. 74:741-751(2002).
RN   [122]
RP   VARIANTS AMYL-TTR MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140
RP   AND ILE-142.
RX   PubMed=12050338; DOI=10.1056/nejmoa013354;
RA   Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A.,
RA   Gillmore J.D., Pepys M.B., Hawkins P.N.;
RT   "Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.";
RL   N. Engl. J. Med. 346:1786-1791(2002).
RN   [123]
RP   VARIANT AMYL-TTR HIS-89.
RX   PubMed=12771253; DOI=10.1212/01.wnl.0000065901.18353.ab;
RA   Blevins G., Macaulay R., Harder S., Fladeland D., Yamashita T., Yazaki M.,
RA   Hamidi Asl K., Benson M.D., Donat J.R.;
RT   "Oculoleptomeningeal amyloidosis in a large kindred with a new
RT   transthyretin variant Tyr69His.";
RL   Neurology 60:1625-1630(2003).
RN   [124]
RP   VARIANT CYS-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12876326; DOI=10.1110/ps.0349703;
RA   Lim A., Prokaeva T., McComb M.E., Connors L.H., Skinner M., Costello C.E.;
RT   "Identification of S-sulfonation and S-thiolation of a novel transthyretin
RT   Phe33Cys variant from a patient diagnosed with familial transthyretin
RT   amyloidosis.";
RL   Protein Sci. 12:1775-1785(2003).
RN   [125]
RP   VARIANT AMYL-TTR LYS-74.
RX   PubMed=15214015; DOI=10.1002/ajmg.a.30007;
RA   Busse A., Sanchez M.A., Monterroso V., Alvarado M.V., Leon P.;
RT   "A severe form of amyloidotic polyneuropathy in a Costa Rican family with a
RT   rare transthyretin mutation (Glu54Lys).";
RL   Am. J. Med. Genet. A 128:190-194(2004).
RN   [126]
RP   VARIANT AMYL-TTR VAL-53.
RX   PubMed=15478468; DOI=10.1080/13506120410001727767;
RA   Frigerio R., Fabrizi G.M., Ferrarini M., Cavallaro T., Brighina L.,
RA   Santoro P., Agostoni E., Cavaletti G., Rizzuto N., Ferrarese C.;
RT   "An unusual transthyretin gene missense mutation (TTR Phe33Val) linked to
RT   familial amyloidotic polyneuropathy.";
RL   Amyloid 11:121-124(2004).
RN   [127]
RP   VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL-TTR GLU-67; HIS-78;
RP   ALA-80 AND TYR-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15217993; DOI=10.1373/clinchem.2004.033266;
RA   Bergen H.R. III, Zeldenrust S.R., Butz M.L., Snow D.S., Dyck P.J.,
RA   Dyck P.J.B., Klein C.J., O'Brien J.F., Thibodeau S.N., Muddiman D.C.;
RT   "Identification of transthyretin variants by sequential proteomic and
RT   genomic analysis.";
RL   Clin. Chem. 50:1544-1552(2004).
RN   [128]
RP   VARIANT AMYL-TTR GLY-81.
RX   PubMed=17453626; DOI=10.1080/13506120601116625;
RA   Rosenzweig M., Skinner M., Prokaeva T., Theberge R., Costello C.,
RA   Drachman B.M., Connors L.H.;
RT   "A new transthyretin variant (Glu61Gly) associated with cardiomyopathy.";
RL   Amyloid 14:65-71(2007).
RN   [129]
RP   VARIANT AMYL-TTR SER-144.
RX   PubMed=17577687; DOI=10.1080/13506120701259895;
RA   Bergstroem J., Patrosso M.C., Colussi G., Salvadore M., Penco S., Lando G.,
RA   Marocchi A., Ueda A., Nakamura M., Ando Y.;
RT   "A novel type of familial transthyretin amyloidosis, ATTR Asn124Ser, with
RT   co-localization of kappa light chains.";
RL   Amyloid 14:141-145(2007).
RN   [130]
RP   VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53; VAL-53;
RP   PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84; LEU-88; ALA-91;
RP   TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114; GLY-117; ASN-126;
RP   MET-127; VAL-127; MET-131 AND ILE-142, VARIANTS ILE-33; SER-121 AND
RP   THR-129, AND VARIANT CHICAGO MET-139.
RX   PubMed=17503405; DOI=10.1002/elps.200600840;
RA   Altland K., Benson M.D., Costello C.E., Ferlini A., Hazenberg B.P.C.,
RA   Hund E., Kristen A.V., Linke R.P., Merlini G., Salvi F., Saraiva M.J.,
RA   Singer R., Skinner M., Winter P.;
RT   "Genetic microheterogeneity of human transthyretin detected by IEF.";
RL   Electrophoresis 28:2053-2064(2007).
RN   [131]
RP   VARIANT AMYL-TTR VAL-58.
RX   PubMed=17635579; DOI=10.1111/j.1365-2362.2007.01836.x;
RA   Augustin S., Llige D., Andreu A., Gonzalez A., Genesca J.;
RT   "Familial amyloidosis in a large Spanish kindred resulting from a D38V
RT   mutation in the transthyretin gene.";
RL   Eur. J. Clin. Invest. 37:673-678(2007).
RN   [132]
RP   VARIANT AMYL-TTR ARG-70.
RX   PubMed=23317988; DOI=10.1016/j.jaad.2012.07.026;
RA   Dekmezian M.S., Tschen J.A., Cho-Vega J.H.;
RT   "Delayed diagnosis of transthyretin amyloidosis with a novel mutation
RT   (c.210T>A) in the transthyretin gene.";
RL   J. Am. Acad. Dermatol. 68:E49-E51(2013).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain.
CC       {ECO:0000269|PubMed:3714052}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC       assemble around a central channel that can accommodate two ligand
CC       molecules. Interacts with RBP4. {ECO:0000269|PubMed:10052934,
CC       ECO:0000269|PubMed:11243784, ECO:0000269|PubMed:11560492,
CC       ECO:0000269|PubMed:12820260, ECO:0000269|PubMed:14583036,
CC       ECO:0000269|PubMed:14711308, ECO:0000269|PubMed:15735344,
CC       ECO:0000269|PubMed:15769474, ECO:0000269|PubMed:15826192,
CC       ECO:0000269|PubMed:18095641, ECO:0000269|PubMed:18155178,
CC       ECO:0000269|PubMed:18811132, ECO:0000269|PubMed:19021760}.
CC   -!- INTERACTION:
CC       P02766; Q15109: AGER; NbExp=2; IntAct=EBI-711909, EBI-1646426;
CC       P02766; P05067: APP; NbExp=3; IntAct=EBI-711909, EBI-77613;
CC       P02766; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-711909, EBI-821758;
CC       P02766; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-711909, EBI-2875816;
CC       P02766; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-711909, EBI-14199987;
CC       P02766; P18848: ATF4; NbExp=3; IntAct=EBI-711909, EBI-492498;
CC       P02766; Q9Y2D1: ATF5; NbExp=3; IntAct=EBI-711909, EBI-492509;
CC       P02766; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-711909, EBI-2891281;
CC       P02766; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-711909, EBI-741210;
CC       P02766; Q8N163: CCAR2; NbExp=3; IntAct=EBI-711909, EBI-355410;
CC       P02766; Q01850: CDR2; NbExp=3; IntAct=EBI-711909, EBI-1181367;
CC       P02766; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-711909, EBI-11953200;
CC       P02766; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-711909, EBI-744045;
CC       P02766; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-711909, EBI-3957044;
CC       P02766; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-711909, EBI-25836090;
CC       P02766; Q96MW5: COG8; NbExp=3; IntAct=EBI-711909, EBI-720875;
CC       P02766; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-711909, EBI-350590;
CC       P02766; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-711909, EBI-10213520;
CC       P02766; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-711909, EBI-25835236;
CC       P02766; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-711909, EBI-396453;
CC       P02766; Q7Z602: GPR141; NbExp=3; IntAct=EBI-711909, EBI-21649723;
CC       P02766; P68431: H3C12; NbExp=3; IntAct=EBI-711909, EBI-79722;
CC       P02766; Q86U28: ISCA2; NbExp=3; IntAct=EBI-711909, EBI-10258659;
CC       P02766; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-711909, EBI-12382297;
CC       P02766; Q06136: KDSR; NbExp=3; IntAct=EBI-711909, EBI-3909166;
CC       P02766; Q12756: KIF1A; NbExp=3; IntAct=EBI-711909, EBI-2679809;
CC       P02766; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-711909, EBI-714379;
CC       P02766; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-711909, EBI-8487781;
CC       P02766; P41218: MNDA; NbExp=3; IntAct=EBI-711909, EBI-2829677;
CC       P02766; P25713: MT3; NbExp=3; IntAct=EBI-711909, EBI-8084264;
CC       P02766; Q16718: NDUFA5; NbExp=3; IntAct=EBI-711909, EBI-746417;
CC       P02766; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-711909, EBI-10172876;
CC       P02766; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-711909, EBI-1059321;
CC       P02766; Q96FW1: OTUB1; NbExp=4; IntAct=EBI-711909, EBI-1058491;
CC       P02766; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-711909, EBI-25830200;
CC       P02766; O75781-2: PALM; NbExp=3; IntAct=EBI-711909, EBI-16399860;
CC       P02766; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-711909, EBI-2513978;
CC       P02766; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-711909, EBI-9090282;
CC       P02766; P11908: PRPS2; NbExp=3; IntAct=EBI-711909, EBI-4290895;
CC       P02766; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-711909, EBI-743880;
CC       P02766; P02753: RBP4; NbExp=4; IntAct=EBI-711909, EBI-2116134;
CC       P02766; Q96D59: RNF183; NbExp=3; IntAct=EBI-711909, EBI-743938;
CC       P02766; Q9C004: SPRY4; NbExp=3; IntAct=EBI-711909, EBI-354861;
CC       P02766; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-711909, EBI-18616594;
CC       P02766; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-711909, EBI-723091;
CC       P02766; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-711909, EBI-21575846;
CC       P02766; Q13569: TDG; NbExp=3; IntAct=EBI-711909, EBI-348333;
CC       P02766; P21980-2: TGM2; NbExp=3; IntAct=EBI-711909, EBI-25842075;
CC       P02766; A0AVI4-2: TMEM129; NbExp=3; IntAct=EBI-711909, EBI-25871541;
CC       P02766; P02766: TTR; NbExp=11; IntAct=EBI-711909, EBI-711909;
CC       P02766; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-711909, EBI-348496;
CC       P02766; O95164: UBL3; NbExp=3; IntAct=EBI-711909, EBI-12876508;
CC       P02766; Q8IWV7: UBR1; NbExp=3; IntAct=EBI-711909, EBI-711736;
CC       P02766; P45880: VDAC2; NbExp=3; IntAct=EBI-711909, EBI-354022;
CC       P02766; P58304: VSX2; NbExp=3; IntAct=EBI-711909, EBI-6427899;
CC       P02766; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-711909, EBI-7705033;
CC       P02766; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-711909, EBI-1538838;
CC       P02766; Q86V28; NbExp=3; IntAct=EBI-711909, EBI-10259496;
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Detected in serum and cerebrospinal fluid (at
CC       protein level). Highly expressed in choroid plexus epithelial cells.
CC       Detected in retina pigment epithelium and liver.
CC       {ECO:0000269|PubMed:10328977, ECO:0000269|PubMed:3714052}.
CC   -!- DOMAIN: Each monomer has two 4-stranded beta sheets and the shape of a
CC       prolate ellipsoid. Antiparallel beta-sheet interactions link monomers
CC       into dimers. A short loop from each monomer forms the main dimer-dimer
CC       interaction. These two pairs of loops separate the opposed, convex
CC       beta-sheets of the dimers to form an internal channel.
CC   -!- PTM: Not glycosylated under normal conditions. Following unfolding,
CC       caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118
CC       site is exposed and glycosylated by STT3B-containing OST complex,
CC       leading to its degradation by the ER-associated degradation (ERAD)
CC       pathway. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:19167329}.
CC   -!- PTM: Sulfonation of the reactive cysteine Cys-30 enhances the stability
CC       of the native conformation of TTR, avoiding misassembly of the protein
CC       leading to amyloid formation. {ECO:0000305|PubMed:17175208}.
CC   -!- DISEASE: Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: A
CC       hereditary generalized amyloidosis due to transthyretin amyloid
CC       deposition. Protein fibrils can form in different tissues leading to
CC       amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel
CC       syndrome, systemic senile amyloidosis. The disease includes
CC       leptomeningeal amyloidosis that is characterized by primary involvement
CC       of the central nervous system. Neuropathologic examination shows
CC       amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and
CC       subpial deposits. Some patients also develop vitreous amyloid
CC       deposition that leads to visual impairment (oculoleptomeningeal
CC       amyloidosis). Clinical features include seizures, stroke-like episodes,
CC       dementia, psychomotor deterioration, variable amyloid deposition in the
CC       vitreous humor. {ECO:0000269|PubMed:10036587,
CC       ECO:0000269|PubMed:10071047, ECO:0000269|PubMed:10211412,
CC       ECO:0000269|PubMed:10436378, ECO:0000269|PubMed:10439117,
CC       ECO:0000269|PubMed:10611950, ECO:0000269|PubMed:10627135,
CC       ECO:0000269|PubMed:10694917, ECO:0000269|PubMed:10842705,
CC       ECO:0000269|PubMed:10842718, ECO:0000269|PubMed:10882995,
CC       ECO:0000269|PubMed:11243784, ECO:0000269|PubMed:11445644,
CC       ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:12050338,
CC       ECO:0000269|PubMed:12403615, ECO:0000269|PubMed:12557757,
CC       ECO:0000269|PubMed:12771253, ECO:0000269|PubMed:1301926,
CC       ECO:0000269|PubMed:1351039, ECO:0000269|PubMed:1362222,
CC       ECO:0000269|PubMed:1436517, ECO:0000269|PubMed:1517749,
CC       ECO:0000269|PubMed:1520326, ECO:0000269|PubMed:1520336,
CC       ECO:0000269|PubMed:15214015, ECO:0000269|PubMed:15217993,
CC       ECO:0000269|PubMed:1544214, ECO:0000269|PubMed:15478468,
CC       ECO:0000269|PubMed:1570831, ECO:0000269|PubMed:15735344,
CC       ECO:0000269|PubMed:16185074, ECO:0000269|PubMed:1656975,
CC       ECO:0000269|PubMed:16627944, ECO:0000269|PubMed:1734866,
CC       ECO:0000269|PubMed:17453626, ECO:0000269|PubMed:17503405,
CC       ECO:0000269|PubMed:17577687, ECO:0000269|PubMed:17635579,
CC       ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:1932142,
CC       ECO:0000269|PubMed:2046936, ECO:0000269|PubMed:2161654,
CC       ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717,
CC       ECO:0000269|PubMed:2891727, ECO:0000269|PubMed:3022108,
CC       ECO:0000269|PubMed:3135807, ECO:0000269|PubMed:3722385,
CC       ECO:0000269|PubMed:3818577, ECO:0000269|PubMed:6487335,
CC       ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852,
CC       ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:7850982,
CC       ECO:0000269|PubMed:7910950, ECO:0000269|PubMed:7914929,
CC       ECO:0000269|PubMed:7923855, ECO:0000269|PubMed:8019560,
CC       ECO:0000269|PubMed:8038017, ECO:0000269|PubMed:8081397,
CC       ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8133316,
CC       ECO:0000269|PubMed:8257997, ECO:0000269|PubMed:8352764,
CC       ECO:0000269|PubMed:8382610, ECO:0000269|PubMed:8428915,
CC       ECO:0000269|PubMed:8579098, ECO:0000269|PubMed:8990019,
CC       ECO:0000269|PubMed:9066351, ECO:0000269|PubMed:9605286,
CC       ECO:0000269|PubMed:9733771, ECO:0000269|Ref.91}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Hyperthyroxinemia, dystransthyretinemic (DTTRH) [MIM:145680]:
CC       A condition characterized by elevation of total and free thyroxine in
CC       healthy, euthyroid persons without detectable binding protein
CC       abnormalities. {ECO:0000269|PubMed:1979335}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition
CC       characterized by entrapment of the median nerve within the carpal
CC       tunnel. Symptoms include burning pain and paresthesias involving the
CC       ventral surface of the hand and fingers which may radiate proximally.
CC       Impairment of sensation in the distribution of the median nerve and
CC       thenar muscle atrophy may occur. This condition may be associated with
CC       repetitive occupational trauma, wrist injuries, amyloid neuropathies,
CC       rheumatoid arthritis. {ECO:0000269|PubMed:8309582}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Tetramer dissociation and partial unfolding leads to the
CC       formation of aggregates and amyloid fibrils. Small molecules that
CC       occupy at least one of the thyroid hormone binding sites stabilize the
CC       tetramer, and thereby stabilize the native state and protect against
CC       misfolding and the formation of amyloid fibrils.
CC   -!- MISCELLANEOUS: Two binding sites for thyroxine are located in the
CC       channel. Less than 1% of plasma prealbumin molecules are normally
CC       involved in thyroxine transport. L-thyroxine binds to the transthyretin
CC       by an order of magnitude stronger than does the triiodo-L-thyronine.
CC       Thyroxine-binding globulin is the major carrier protein for thyroid
CC       hormones in man.
CC   -!- MISCELLANEOUS: About 40% of plasma transthyretin circulates in a tight
CC       protein-protein complex with the plasma retinol-binding protein (RBP).
CC       The formation of the complex with RBP stabilizes the binding of retinol
CC       to RBP and decreases the glomerular filtration and renal catabolism of
CC       the relatively small RBP molecule. There is evidence for 2 binding
CC       sites for RBP, one possibly being a region that includes Ile-104,
CC       located on the outer surface of the transthyretin molecule.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Transthyretin entry;
CC       URL="https://en.wikipedia.org/wiki/Transthyretin";
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DR   EMBL; K02091; AAA60011.1; -; mRNA.
DR   EMBL; M10605; AAA60012.1; -; mRNA.
DR   EMBL; M11518; AAA98771.1; -; Genomic_DNA.
DR   EMBL; M11844; AAA60013.1; -; Genomic_DNA.
DR   EMBL; X59498; CAA42087.1; -; mRNA.
DR   EMBL; D00096; BAA00059.1; -; mRNA.
DR   EMBL; M15517; AAA60018.1; -; Genomic_DNA.
DR   EMBL; M15515; AAA60018.1; JOINED; Genomic_DNA.
DR   EMBL; M15516; AAA60018.1; JOINED; Genomic_DNA.
DR   EMBL; U19780; AAA73473.1; -; mRNA.
DR   EMBL; AF162690; AAD45014.1; -; mRNA.
DR   EMBL; AK312051; BAG34987.1; -; mRNA.
DR   EMBL; BT007189; AAP35853.1; -; mRNA.
DR   EMBL; CR456908; CAG33189.1; -; mRNA.
DR   EMBL; CH471088; EAX01264.1; -; Genomic_DNA.
DR   EMBL; BC005310; AAH05310.1; -; mRNA.
DR   EMBL; BC020791; AAH20791.1; -; mRNA.
DR   EMBL; S63185; AAD14937.2; -; Genomic_DNA.
DR   EMBL; S72385; AAD14098.1; -; Genomic_DNA.
DR   EMBL; M11714; AAA61181.1; -; mRNA.
DR   EMBL; M63285; AAA36784.1; -; Genomic_DNA.
DR   CCDS; CCDS11899.1; -.
DR   PIR; A91532; VBHU.
DR   RefSeq; NP_000362.1; NM_000371.3.
DR   PDB; 1BM7; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1BMZ; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1BZ8; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1BZD; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 1BZE; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1DVQ; X-ray; 2.00 A; A/B=21-144.
DR   PDB; 1DVS; X-ray; 2.00 A; A/B=21-144.
DR   PDB; 1DVT; X-ray; 1.90 A; A/B=21-144.
DR   PDB; 1DVU; X-ray; 1.90 A; A/B=21-144.
DR   PDB; 1DVX; X-ray; 2.00 A; A/B=21-144.
DR   PDB; 1DVY; X-ray; 1.90 A; A/B=21-144.
DR   PDB; 1DVZ; X-ray; 1.90 A; A/B=21-144.
DR   PDB; 1E3F; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 1E4H; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1E5A; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1ETA; X-ray; 1.70 A; 1/2=21-147.
DR   PDB; 1ETB; X-ray; 1.70 A; 1/2=21-147.
DR   PDB; 1F41; X-ray; 1.30 A; A/B=21-147.
DR   PDB; 1F86; X-ray; 1.10 A; A/B=30-144.
DR   PDB; 1FH2; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1FHN; X-ray; 1.75 A; A/B=21-147.
DR   PDB; 1G1O; X-ray; 2.30 A; A/B/C/D=21-147.
DR   PDB; 1GKO; X-ray; 2.10 A; A/B/C/D=21-147.
DR   PDB; 1ICT; X-ray; 3.00 A; A/B/C/D/E/F/G/H=21-147.
DR   PDB; 1III; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1IIK; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1IJN; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1QAB; X-ray; 3.20 A; A/B/C/D=21-147.
DR   PDB; 1QWH; X-ray; 1.36 A; A/B=31-147.
DR   PDB; 1RLB; X-ray; 3.10 A; A/B/C/D=21-147.
DR   PDB; 1SOK; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 1SOQ; X-ray; 2.10 A; A/B/C/D=21-147.
DR   PDB; 1THA; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 1THC; X-ray; 2.30 A; A/B=21-147.
DR   PDB; 1TLM; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 1TSH; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1TT6; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1TTA; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1TTB; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1TTC; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1TTR; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 1TYR; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1TZ8; X-ray; 1.85 A; A/B/C/D=21-147.
DR   PDB; 1U21; X-ray; 1.69 A; A/B=21-147.
DR   PDB; 1X7S; X-ray; 1.55 A; A/B=21-147.
DR   PDB; 1X7T; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 1Y1D; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 1Z7J; X-ray; 2.20 A; A/B=21-147.
DR   PDB; 1ZCR; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 1ZD6; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 2B14; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 2B15; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 2B16; X-ray; 1.75 A; A/B=21-147.
DR   PDB; 2B77; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 2B9A; X-ray; 1.54 A; A/B=21-147.
DR   PDB; 2F7I; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 2F8I; X-ray; 1.54 A; A/B=21-147.
DR   PDB; 2FBR; X-ray; 1.46 A; A/B=21-147.
DR   PDB; 2FLM; X-ray; 1.65 A; A/B=21-147.
DR   PDB; 2G3X; X-ray; 1.58 A; A/B=21-147.
DR   PDB; 2G3Z; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 2G4E; X-ray; 2.17 A; A/B=21-147.
DR   PDB; 2G4G; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 2G5U; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 2G9K; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 2GAB; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 2H4E; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 2M5N; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=125-135.
DR   PDB; 2NBO; NMR; -; A=21-147.
DR   PDB; 2NBP; NMR; -; A=21-147.
DR   PDB; 2NOY; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 2PAB; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 2QEL; X-ray; 2.29 A; A/B/C/D=21-147.
DR   PDB; 2QGB; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 2QGC; X-ray; 1.30 A; A/B=21-147.
DR   PDB; 2QGD; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 2QGE; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 2ROX; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 2ROY; X-ray; 2.20 A; A/B=21-147.
DR   PDB; 2TRH; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 2TRY; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 2WQA; X-ray; 2.85 A; A/B/C/D=21-147.
DR   PDB; 3A4D; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 3A4E; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 3A4F; X-ray; 1.99 A; A/B=21-147.
DR   PDB; 3B56; X-ray; 1.55 A; A/B=21-147.
DR   PDB; 3BSZ; X-ray; 3.38 A; A/B/C/D=21-147.
DR   PDB; 3BT0; X-ray; 1.59 A; A/B=21-147.
DR   PDB; 3CBR; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 3CFM; X-ray; 1.60 A; A/B=30-147.
DR   PDB; 3CFN; X-ray; 1.87 A; A/B=30-147.
DR   PDB; 3CFQ; X-ray; 2.09 A; A/B=30-147.
DR   PDB; 3CFT; X-ray; 1.87 A; A/B=30-147.
DR   PDB; 3CN0; X-ray; 1.52 A; A/B=21-147.
DR   PDB; 3CN1; X-ray; 1.52 A; A/B=21-147.
DR   PDB; 3CN2; X-ray; 1.52 A; A/B=21-147.
DR   PDB; 3CN3; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 3CN4; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 3CXF; X-ray; 2.30 A; A/B=21-147.
DR   PDB; 3D2T; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 3D7P; X-ray; 1.72 A; A/B=21-147.
DR   PDB; 3DGD; X-ray; 1.38 A; A/B/C/D=21-147.
DR   PDB; 3DID; X-ray; 1.78 A; A/B/C/D=21-147.
DR   PDB; 3DJR; X-ray; 2.02 A; A/B=21-147.
DR   PDB; 3DJS; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 3DJT; X-ray; 2.30 A; A/B=21-147.
DR   PDB; 3DJZ; X-ray; 1.82 A; A/B=21-147.
DR   PDB; 3DK0; X-ray; 1.87 A; A/B=21-147.
DR   PDB; 3DK2; X-ray; 2.35 A; A/B=21-147.
DR   PDB; 3DO4; X-ray; 2.40 A; A/B/C/D/E/F/G/H=21-147.
DR   PDB; 3ESN; X-ray; 1.35 A; A/B=21-147.
DR   PDB; 3ESO; X-ray; 1.31 A; A/B=21-147.
DR   PDB; 3ESP; X-ray; 1.31 A; A/B=21-147.
DR   PDB; 3FC8; X-ray; 1.85 A; A/B=21-144.
DR   PDB; 3FCB; X-ray; 1.80 A; A/B=21-144.
DR   PDB; 3GLZ; X-ray; 1.78 A; A/B=21-147.
DR   PDB; 3GPS; X-ray; 1.78 A; A/B/C/D=21-147.
DR   PDB; 3GRB; X-ray; 1.75 A; A/B/C/D=21-147.
DR   PDB; 3GRG; X-ray; 1.90 A; A/B/C/D=21-147.
DR   PDB; 3GS0; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 3GS4; X-ray; 1.78 A; A/B=21-147.
DR   PDB; 3GS7; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 3HJ0; X-ray; 1.34 A; A/B=21-147.
DR   PDB; 3I9A; X-ray; 1.65 A; A/B=21-147.
DR   PDB; 3I9I; X-ray; 1.80 A; A/B=30-145.
DR   PDB; 3I9P; X-ray; 1.90 A; A/B=30-145.
DR   PDB; 3IMR; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 3IMS; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 3IMT; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 3IMU; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 3IMV; X-ray; 1.47 A; A/B=21-147.
DR   PDB; 3IMW; X-ray; 1.31 A; A/B=21-147.
DR   PDB; 3IPB; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 3IPE; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 3KGS; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 3KGT; X-ray; 1.95 A; A/B=21-147.
DR   PDB; 3KGU; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 3M1O; X-ray; 1.20 A; A/B=21-147.
DR   PDB; 3NEE; X-ray; 1.55 A; A/B=30-145.
DR   PDB; 3NEO; X-ray; 2.00 A; A/B=30-145.
DR   PDB; 3NES; X-ray; 1.75 A; A/B=30-145.
DR   PDB; 3NEX; X-ray; 1.70 A; A/B=30-145.
DR   PDB; 3NG5; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 3OZK; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 3OZL; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 3P3R; X-ray; 1.25 A; A/B=21-147.
DR   PDB; 3P3S; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 3P3T; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 3P3U; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 3SSG; X-ray; 2.00 A; A=21-147.
DR   PDB; 3TCT; X-ray; 1.30 A; A/B=21-147.
DR   PDB; 3TFB; X-ray; 2.03 A; A/B=30-145.
DR   PDB; 3U2I; X-ray; 1.70 A; A/B=32-147.
DR   PDB; 3U2J; Neutron; 2.00 A; A/B=32-147.
DR   PDB; 3W3B; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 4ABQ; X-ray; 1.70 A; A/B=21-144.
DR   PDB; 4ABU; X-ray; 1.86 A; A/B=21-144.
DR   PDB; 4ABV; X-ray; 1.80 A; A/B=21-144.
DR   PDB; 4ABW; X-ray; 1.70 A; A/B=21-144.
DR   PDB; 4AC2; X-ray; 1.81 A; A/B=21-144.
DR   PDB; 4AC4; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 4ACT; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 4ANK; X-ray; 1.70 A; A/B=1-147.
DR   PDB; 4D7B; X-ray; 1.15 A; A/B=21-147.
DR   PDB; 4DER; X-ray; 1.90 A; A/B=30-145.
DR   PDB; 4DES; X-ray; 1.75 A; A/B=30-145.
DR   PDB; 4DET; X-ray; 2.05 A; A/B=30-145.
DR   PDB; 4DEU; X-ray; 1.60 A; A/B=30-145.
DR   PDB; 4DEW; X-ray; 1.90 A; A/B=1-147.
DR   PDB; 4FI6; X-ray; 1.46 A; A/B=21-147.
DR   PDB; 4FI7; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 4FI8; X-ray; 1.22 A; A/B=21-147.
DR   PDB; 4HIQ; X-ray; 1.18 A; A/B=21-147.
DR   PDB; 4HIS; X-ray; 1.20 A; A/B=21-147.
DR   PDB; 4HJS; X-ray; 1.22 A; A/B=30-145.
DR   PDB; 4HJT; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 4HJU; X-ray; 1.35 A; A/B=21-147.
DR   PDB; 4I85; X-ray; 1.67 A; A/B=21-147.
DR   PDB; 4I87; X-ray; 1.69 A; A/B=21-147.
DR   PDB; 4I89; X-ray; 1.69 A; A/B=21-147.
DR   PDB; 4IIZ; X-ray; 2.10 A; A/B=21-147.
DR   PDB; 4IK6; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 4IK7; X-ray; 2.10 A; A/B=21-147.
DR   PDB; 4IKI; X-ray; 2.00 A; A/B=21-147.
DR   PDB; 4IKJ; X-ray; 2.10 A; A/B=21-147.
DR   PDB; 4IKK; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 4IKL; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 4KY2; X-ray; 1.13 A; A/B=21-147.
DR   PDB; 4L1S; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 4L1T; X-ray; 1.16 A; A/B=21-147.
DR   PDB; 4MAS; X-ray; 1.22 A; A/B=21-147.
DR   PDB; 4MRB; X-ray; 1.27 A; A/B=21-147.
DR   PDB; 4MRC; X-ray; 1.54 A; A/B=22-147.
DR   PDB; 4N85; X-ray; 1.60 A; A/B=1-147.
DR   PDB; 4N86; X-ray; 2.00 A; A/B=1-147.
DR   PDB; 4N87; X-ray; 1.79 A; A/B=1-147.
DR   PDB; 4PM1; X-ray; 1.23 A; A/B=21-147.
DR   PDB; 4PME; X-ray; 1.26 A; A/B=29-146.
DR   PDB; 4PMF; X-ray; 1.35 A; A/B=29-145.
DR   PDB; 4PVL; X-ray; 1.85 A; A/B=21-147.
DR   PDB; 4PVM; Other; 2.00 A; A/B=21-147.
DR   PDB; 4PVN; Other; 2.30 A; A/B=21-147.
DR   PDB; 4PWE; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 4PWF; X-ray; 1.60 A; A/B=1-147.
DR   PDB; 4PWG; X-ray; 1.80 A; A/B=1-147.
DR   PDB; 4PWH; X-ray; 1.80 A; A/B=1-147.
DR   PDB; 4PWI; X-ray; 1.49 A; A/B=1-147.
DR   PDB; 4PWJ; X-ray; 1.55 A; A/B=1-147.
DR   PDB; 4PWK; X-ray; 1.59 A; A/B=1-147.
DR   PDB; 4QRF; X-ray; 1.80 A; A/B=1-147.
DR   PDB; 4QXV; X-ray; 1.12 A; A/B=21-147.
DR   PDB; 4QYA; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 4TKW; X-ray; 1.80 A; A/B=29-147.
DR   PDB; 4TL4; X-ray; 1.75 A; A/B=29-147.
DR   PDB; 4TL5; X-ray; 1.44 A; A/B=29-147.
DR   PDB; 4TLK; X-ray; 1.44 A; A/B=29-147.
DR   PDB; 4TLS; X-ray; 1.35 A; A/B=29-147.
DR   PDB; 4TLT; X-ray; 1.70 A; A/B=29-147.
DR   PDB; 4TLU; X-ray; 1.75 A; A/B=29-147.
DR   PDB; 4TM9; X-ray; 1.70 A; A/B=29-147.
DR   PDB; 4TNE; X-ray; 1.55 A; A/B=29-147.
DR   PDB; 4TNF; X-ray; 1.60 A; A/B=29-147.
DR   PDB; 4TNG; X-ray; 1.60 A; A/B=29-147.
DR   PDB; 4TQ8; X-ray; 1.52 A; A/B=21-147.
DR   PDB; 4TQH; X-ray; 1.51 A; A/B=21-147.
DR   PDB; 4TQI; X-ray; 1.25 A; A/B=21-147.
DR   PDB; 4TQP; X-ray; 1.58 A; A/B=21-147.
DR   PDB; 4WNJ; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 4WNS; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 4WO0; X-ray; 1.34 A; A/B=21-147.
DR   PDB; 4Y9B; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 4Y9C; X-ray; 1.49 A; A/B=1-147.
DR   PDB; 4Y9E; X-ray; 1.49 A; A/B=1-147.
DR   PDB; 4Y9F; X-ray; 1.50 A; A/B=1-147.
DR   PDB; 4Y9G; X-ray; 1.89 A; A/B=1-147.
DR   PDB; 4YDM; X-ray; 1.25 A; A/B=21-147.
DR   PDB; 4YDN; X-ray; 1.35 A; A/B=21-147.
DR   PDB; 5A6I; X-ray; 1.86 A; A=21-147.
DR   PDB; 5AKS; X-ray; 1.25 A; A/B=21-147.
DR   PDB; 5AKT; X-ray; 1.35 A; A/B=21-147.
DR   PDB; 5AKV; X-ray; 1.52 A; A/B=21-147.
DR   PDB; 5AL0; X-ray; 1.39 A; A/B=21-147.
DR   PDB; 5AL8; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 5AYT; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 5BOJ; X-ray; 1.75 A; A/B=21-147.
DR   PDB; 5CLX; X-ray; 1.28 A; A/B=21-147.
DR   PDB; 5CLY; X-ray; 1.23 A; A/B=21-147.
DR   PDB; 5CLZ; X-ray; 1.22 A; A/B=21-147.
DR   PDB; 5CM1; X-ray; 1.22 A; A/B=21-147.
DR   PDB; 5CN3; X-ray; 1.30 A; A/B=21-147.
DR   PDB; 5CNH; X-ray; 1.42 A; A/B=21-147.
DR   PDB; 5CR1; X-ray; 1.54 A; A/B=30-145.
DR   PDB; 5DEJ; X-ray; 1.37 A; A/B=30-145.
DR   PDB; 5DWP; X-ray; 1.20 A; A/B=30-145.
DR   PDB; 5E23; X-ray; 1.41 A; A/B=21-147.
DR   PDB; 5E4A; X-ray; 1.33 A; A/B=10-146.
DR   PDB; 5E4O; X-ray; 1.50 A; A/B=30-146.
DR   PDB; 5EN3; X-ray; 1.25 A; A/B=21-147.
DR   PDB; 5EZP; X-ray; 2.50 A; A/B/C/D/E/F/G/H=26-147.
DR   PDB; 5FO2; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 5FW6; X-ray; 1.30 A; A/B=21-147.
DR   PDB; 5FW7; X-ray; 1.20 A; A/B=21-147.
DR   PDB; 5FW8; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 5H0V; X-ray; 1.58 A; A/B/C/D=31-147.
DR   PDB; 5H0W; X-ray; 1.90 A; A=31-147.
DR   PDB; 5H0X; X-ray; 1.57 A; A/B=31-147.
DR   PDB; 5H0Y; X-ray; 1.80 A; A=31-147.
DR   PDB; 5H0Z; X-ray; 1.74 A; A=31-147.
DR   PDB; 5HJG; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 5IHH; X-ray; 1.35 A; A/B=21-147.
DR   PDB; 5JID; X-ray; 1.20 A; A/B=21-147.
DR   PDB; 5JIM; X-ray; 1.26 A; A/B=21-147.
DR   PDB; 5JIQ; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 5K1J; X-ray; 1.69 A; A/B=30-145.
DR   PDB; 5K1N; X-ray; 1.81 A; A/B=30-147.
DR   PDB; 5L4F; X-ray; 1.48 A; A/B=21-147.
DR   PDB; 5L4I; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 5L4J; X-ray; 1.62 A; A/B=21-147.
DR   PDB; 5L4M; X-ray; 1.58 A; A/B=21-147.
DR   PDB; 5LLL; X-ray; 1.42 A; A/B=21-147.
DR   PDB; 5LLV; X-ray; 1.70 A; A/B/C/D=21-147.
DR   PDB; 5N5Q; X-ray; 2.53 A; A/B=30-145.
DR   PDB; 5N62; X-ray; 1.80 A; A/B=30-146.
DR   PDB; 5N7C; X-ray; 2.45 A; A/B=30-145.
DR   PDB; 5NFE; Other; 1.85 A; A/B=21-147.
DR   PDB; 5NFW; Other; 1.80 A; A/B=21-147.
DR   PDB; 5OQ0; X-ray; 1.94 A; A=21-147.
DR   PDB; 5TTR; X-ray; 2.70 A; A/B/C/D/E/F/G/H=21-147.
DR   PDB; 5TZL; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 5U48; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 5U49; X-ray; 2.22 A; A=21-147.
DR   PDB; 5U4A; X-ray; 1.90 A; A/B=21-147.
DR   PDB; 5U4B; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 5U4C; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 5U4D; X-ray; 1.55 A; A/B=21-147.
DR   PDB; 5U4E; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 5U4F; X-ray; 1.50 A; A/B=21-147.
DR   PDB; 5U4G; X-ray; 1.80 A; A/B=21-147.
DR   PDB; 6D0W; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 6E6Z; X-ray; 1.75 A; A/B=30-144.
DR   PDB; 6E70; X-ray; 1.99 A; A/B=30-144.
DR   PDB; 6E71; X-ray; 1.50 A; A/B=30-144.
DR   PDB; 6E72; X-ray; 1.45 A; A/B=30-144.
DR   PDB; 6E73; X-ray; 1.80 A; A/B=30-144.
DR   PDB; 6E74; X-ray; 1.60 A; A/B=30-144.
DR   PDB; 6E75; X-ray; 1.50 A; A/B=30-144.
DR   PDB; 6E76; X-ray; 1.60 A; A/B=30-144.
DR   PDB; 6E77; X-ray; 1.60 A; A/B=30-144.
DR   PDB; 6E78; X-ray; 1.50 A; A/B=30-144.
DR   PDB; 6EOY; X-ray; 1.38 A; A/B=30-144.
DR   PDB; 6EP1; X-ray; 1.30 A; A/B=30-144.
DR   PDB; 6FFT; Other; 2.00 A; A/B=21-147.
DR   PDB; 6FWD; X-ray; 1.58 A; A/B=21-147.
DR   PDB; 6FXU; X-ray; 1.36 A; A/B=21-147.
DR   PDB; 6FZL; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 6GR7; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 6GRP; X-ray; 1.60 A; A/B=21-147.
DR   PDB; 6IMX; X-ray; 1.60 A; A/B=1-147.
DR   PDB; 6IMY; X-ray; 1.50 A; A/B=1-147.
DR   PDB; 6KGB; X-ray; 1.30 A; A/B=1-146.
DR   PDB; 6R66; X-ray; 1.30 A; A/B=1-147.
DR   PDB; 6R67; X-ray; 1.30 A; A/B=1-147.
DR   PDB; 6R68; X-ray; 1.45 A; A/B=1-147.
DR   PDB; 6R6I; X-ray; 1.47 A; A/B=1-147.
DR   PDB; 6SDZ; EM; 2.97 A; A/B/C/D/E/F/G/H/I/J/K=21-147.
DR   PDB; 6SUG; X-ray; 1.21 A; A/B=1-147.
DR   PDB; 6SUH; X-ray; 1.26 A; A/B=1-147.
DR   PDB; 6TI9; X-ray; 1.45 A; A/B=21-147.
DR   PDB; 6TJN; X-ray; 1.70 A; A/B=21-147.
DR   PDB; 6TXV; X-ray; 1.60 A; A/B=30-145.
DR   PDB; 6TXW; X-ray; 1.15 A; A/B=30-145.
DR   PDB; 6U0Q; X-ray; 1.75 A; A/B=21-147.
DR   PDB; 6XTK; X-ray; 1.70 A; A/B=30-145.
DR   PDB; 7ACU; X-ray; 1.54 A; A/B=30-144.
DR   PDB; 7DT3; X-ray; 1.20 A; A/B=1-147.
DR   PDB; 7DT5; X-ray; 1.25 A; A/B=1-147.
DR   PDB; 7DT6; X-ray; 1.30 A; A/B=1-147.
DR   PDB; 7DT8; X-ray; 1.25 A; A/B=1-147.
DR   PDB; 7EJQ; X-ray; 1.15 A; A/B=1-146.
DR   PDB; 7EJR; X-ray; 1.45 A; A/B=1-146.
DR   PDB; 7ERH; X-ray; 1.55 A; A/B=1-147.
DR   PDB; 7ERI; X-ray; 1.81 A; A/B=1-147.
DR   PDB; 7ERJ; X-ray; 1.89 A; A/B=1-147.
DR   PDB; 7ERK; X-ray; 1.70 A; A/B=1-147.
DR   PDB; 7OB4; EM; 3.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=21-147.
DR   PDB; 7Q3I; X-ray; 1.55 A; AAA/BBB=21-147.
DR   PDB; 7Q9L; X-ray; 1.45 A; A/B=29-147.
DR   PDB; 7Q9N; X-ray; 1.45 A; A/B=29-147.
DR   PDB; 7Q9O; X-ray; 1.35 A; A/B=29-147.
DR   PDB; 7QC5; X-ray; 1.20 A; A/B=21-147.
DR   PDB; 7THA; X-ray; 1.75 A; A/B=21-147.
DR   PDB; 7W9Q; X-ray; 1.60 A; A/B=1-147.
DR   PDB; 7W9R; X-ray; 2.00 A; A/B=1-147.
DR   PDB; 7WL6; X-ray; 1.42 A; A/B=21-147.
DR   PDB; 7Y1I; X-ray; 2.79 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR   PDB; 7Y6J; X-ray; 1.38 A; A/B=21-147.
DR   PDB; 7YBR; X-ray; 1.71 A; A/B=21-147.
DR   PDB; 7YCQ; X-ray; 1.99 A; A/B=21-147.
DR   PDB; 7Z60; X-ray; 1.40 A; A/B=21-147.
DR   PDB; 8ADE; EM; 2.78 A; A/B/C/D/E/F/G=21-147.
DR   PDB; 8AWI; X-ray; 1.15 A; A/B=29-147.
DR   PDB; 8AWW; X-ray; 1.60 A; A/B=30-145.
DR   PDB; 8E7D; EM; 3.31 A; A/B/C/D/E=1-147.
DR   PDB; 8E7E; EM; 3.61 A; A/B/C/D/E=1-147.
DR   PDB; 8E7H; EM; 3.70 A; A/B/C/D/E=1-147.
DR   PDB; 8E7I; EM; 3.65 A; A/B/C/D/E=1-147.
DR   PDB; 8E7J; EM; 3.10 A; A/B/C/D/E=1-147.
DR   PDB; 8HEJ; X-ray; 1.54 A; A/B=31-144.
DR   PDB; 8HY4; X-ray; 1.53 A; A/B=21-147.
DR   PDB; 8IG1; X-ray; 1.45 A; A/B=1-147.
DR   PDB; 8II1; X-ray; 1.91 A; A/B=1-147.
DR   PDB; 8II2; X-ray; 1.80 A; A/B=1-147.
DR   PDB; 8II3; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 8II4; X-ray; 1.50 A; A/B=1-147.
DR   PDB; 8PKE; EM; 3.39 A; A/B/C/D/E/F=21-147.
DR   PDB; 8PKF; EM; 2.37 A; A/B/C/D/E/F=21-147.
DR   PDB; 8PKG; EM; 2.99 A; A/B/C/D/E/F=21-147.
DR   PDB; 8W42; X-ray; 1.45 A; A/B=1-147.
DR   PDB; 8W43; X-ray; 1.30 A; A/B=1-147.
DR   PDB; 8W44; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 8W45; X-ray; 1.10 A; A/B=1-147.
DR   PDB; 8W46; X-ray; 1.35 A; A/B=1-147.
DR   PDB; 8W47; X-ray; 1.40 A; A/B=1-147.
DR   PDB; 8W48; Other; 1.19 A; A/B=1-147.
DR   PDBsum; 1BM7; -.
DR   PDBsum; 1BMZ; -.
DR   PDBsum; 1BZ8; -.
DR   PDBsum; 1BZD; -.
DR   PDBsum; 1BZE; -.
DR   PDBsum; 1DVQ; -.
DR   PDBsum; 1DVS; -.
DR   PDBsum; 1DVT; -.
DR   PDBsum; 1DVU; -.
DR   PDBsum; 1DVX; -.
DR   PDBsum; 1DVY; -.
DR   PDBsum; 1DVZ; -.
DR   PDBsum; 1E3F; -.
DR   PDBsum; 1E4H; -.
DR   PDBsum; 1E5A; -.
DR   PDBsum; 1ETA; -.
DR   PDBsum; 1ETB; -.
DR   PDBsum; 1F41; -.
DR   PDBsum; 1F86; -.
DR   PDBsum; 1FH2; -.
DR   PDBsum; 1FHN; -.
DR   PDBsum; 1G1O; -.
DR   PDBsum; 1GKO; -.
DR   PDBsum; 1ICT; -.
DR   PDBsum; 1III; -.
DR   PDBsum; 1IIK; -.
DR   PDBsum; 1IJN; -.
DR   PDBsum; 1QAB; -.
DR   PDBsum; 1QWH; -.
DR   PDBsum; 1RLB; -.
DR   PDBsum; 1SOK; -.
DR   PDBsum; 1SOQ; -.
DR   PDBsum; 1THA; -.
DR   PDBsum; 1THC; -.
DR   PDBsum; 1TLM; -.
DR   PDBsum; 1TSH; -.
DR   PDBsum; 1TT6; -.
DR   PDBsum; 1TTA; -.
DR   PDBsum; 1TTB; -.
DR   PDBsum; 1TTC; -.
DR   PDBsum; 1TTR; -.
DR   PDBsum; 1TYR; -.
DR   PDBsum; 1TZ8; -.
DR   PDBsum; 1U21; -.
DR   PDBsum; 1X7S; -.
DR   PDBsum; 1X7T; -.
DR   PDBsum; 1Y1D; -.
DR   PDBsum; 1Z7J; -.
DR   PDBsum; 1ZCR; -.
DR   PDBsum; 1ZD6; -.
DR   PDBsum; 2B14; -.
DR   PDBsum; 2B15; -.
DR   PDBsum; 2B16; -.
DR   PDBsum; 2B77; -.
DR   PDBsum; 2B9A; -.
DR   PDBsum; 2F7I; -.
DR   PDBsum; 2F8I; -.
DR   PDBsum; 2FBR; -.
DR   PDBsum; 2FLM; -.
DR   PDBsum; 2G3X; -.
DR   PDBsum; 2G3Z; -.
DR   PDBsum; 2G4E; -.
DR   PDBsum; 2G4G; -.
DR   PDBsum; 2G5U; -.
DR   PDBsum; 2G9K; -.
DR   PDBsum; 2GAB; -.
DR   PDBsum; 2H4E; -.
DR   PDBsum; 2M5N; -.
DR   PDBsum; 2NBO; -.
DR   PDBsum; 2NBP; -.
DR   PDBsum; 2NOY; -.
DR   PDBsum; 2PAB; -.
DR   PDBsum; 2QEL; -.
DR   PDBsum; 2QGB; -.
DR   PDBsum; 2QGC; -.
DR   PDBsum; 2QGD; -.
DR   PDBsum; 2QGE; -.
DR   PDBsum; 2ROX; -.
DR   PDBsum; 2ROY; -.
DR   PDBsum; 2TRH; -.
DR   PDBsum; 2TRY; -.
DR   PDBsum; 2WQA; -.
DR   PDBsum; 3A4D; -.
DR   PDBsum; 3A4E; -.
DR   PDBsum; 3A4F; -.
DR   PDBsum; 3B56; -.
DR   PDBsum; 3BSZ; -.
DR   PDBsum; 3BT0; -.
DR   PDBsum; 3CBR; -.
DR   PDBsum; 3CFM; -.
DR   PDBsum; 3CFN; -.
DR   PDBsum; 3CFQ; -.
DR   PDBsum; 3CFT; -.
DR   PDBsum; 3CN0; -.
DR   PDBsum; 3CN1; -.
DR   PDBsum; 3CN2; -.
DR   PDBsum; 3CN3; -.
DR   PDBsum; 3CN4; -.
DR   PDBsum; 3CXF; -.
DR   PDBsum; 3D2T; -.
DR   PDBsum; 3D7P; -.
DR   PDBsum; 3DGD; -.
DR   PDBsum; 3DID; -.
DR   PDBsum; 3DJR; -.
DR   PDBsum; 3DJS; -.
DR   PDBsum; 3DJT; -.
DR   PDBsum; 3DJZ; -.
DR   PDBsum; 3DK0; -.
DR   PDBsum; 3DK2; -.
DR   PDBsum; 3DO4; -.
DR   PDBsum; 3ESN; -.
DR   PDBsum; 3ESO; -.
DR   PDBsum; 3ESP; -.
DR   PDBsum; 3FC8; -.
DR   PDBsum; 3FCB; -.
DR   PDBsum; 3GLZ; -.
DR   PDBsum; 3GPS; -.
DR   PDBsum; 3GRB; -.
DR   PDBsum; 3GRG; -.
DR   PDBsum; 3GS0; -.
DR   PDBsum; 3GS4; -.
DR   PDBsum; 3GS7; -.
DR   PDBsum; 3HJ0; -.
DR   PDBsum; 3I9A; -.
DR   PDBsum; 3I9I; -.
DR   PDBsum; 3I9P; -.
DR   PDBsum; 3IMR; -.
DR   PDBsum; 3IMS; -.
DR   PDBsum; 3IMT; -.
DR   PDBsum; 3IMU; -.
DR   PDBsum; 3IMV; -.
DR   PDBsum; 3IMW; -.
DR   PDBsum; 3IPB; -.
DR   PDBsum; 3IPE; -.
DR   PDBsum; 3KGS; -.
DR   PDBsum; 3KGT; -.
DR   PDBsum; 3KGU; -.
DR   PDBsum; 3M1O; -.
DR   PDBsum; 3NEE; -.
DR   PDBsum; 3NEO; -.
DR   PDBsum; 3NES; -.
DR   PDBsum; 3NEX; -.
DR   PDBsum; 3NG5; -.
DR   PDBsum; 3OZK; -.
DR   PDBsum; 3OZL; -.
DR   PDBsum; 3P3R; -.
DR   PDBsum; 3P3S; -.
DR   PDBsum; 3P3T; -.
DR   PDBsum; 3P3U; -.
DR   PDBsum; 3SSG; -.
DR   PDBsum; 3TCT; -.
DR   PDBsum; 3TFB; -.
DR   PDBsum; 3U2I; -.
DR   PDBsum; 3U2J; -.
DR   PDBsum; 3W3B; -.
DR   PDBsum; 4ABQ; -.
DR   PDBsum; 4ABU; -.
DR   PDBsum; 4ABV; -.
DR   PDBsum; 4ABW; -.
DR   PDBsum; 4AC2; -.
DR   PDBsum; 4AC4; -.
DR   PDBsum; 4ACT; -.
DR   PDBsum; 4ANK; -.
DR   PDBsum; 4D7B; -.
DR   PDBsum; 4DER; -.
DR   PDBsum; 4DES; -.
DR   PDBsum; 4DET; -.
DR   PDBsum; 4DEU; -.
DR   PDBsum; 4DEW; -.
DR   PDBsum; 4FI6; -.
DR   PDBsum; 4FI7; -.
DR   PDBsum; 4FI8; -.
DR   PDBsum; 4HIQ; -.
DR   PDBsum; 4HIS; -.
DR   PDBsum; 4HJS; -.
DR   PDBsum; 4HJT; -.
DR   PDBsum; 4HJU; -.
DR   PDBsum; 4I85; -.
DR   PDBsum; 4I87; -.
DR   PDBsum; 4I89; -.
DR   PDBsum; 4IIZ; -.
DR   PDBsum; 4IK6; -.
DR   PDBsum; 4IK7; -.
DR   PDBsum; 4IKI; -.
DR   PDBsum; 4IKJ; -.
DR   PDBsum; 4IKK; -.
DR   PDBsum; 4IKL; -.
DR   PDBsum; 4KY2; -.
DR   PDBsum; 4L1S; -.
DR   PDBsum; 4L1T; -.
DR   PDBsum; 4MAS; -.
DR   PDBsum; 4MRB; -.
DR   PDBsum; 4MRC; -.
DR   PDBsum; 4N85; -.
DR   PDBsum; 4N86; -.
DR   PDBsum; 4N87; -.
DR   PDBsum; 4PM1; -.
DR   PDBsum; 4PME; -.
DR   PDBsum; 4PMF; -.
DR   PDBsum; 4PVL; -.
DR   PDBsum; 4PVM; -.
DR   PDBsum; 4PVN; -.
DR   PDBsum; 4PWE; -.
DR   PDBsum; 4PWF; -.
DR   PDBsum; 4PWG; -.
DR   PDBsum; 4PWH; -.
DR   PDBsum; 4PWI; -.
DR   PDBsum; 4PWJ; -.
DR   PDBsum; 4PWK; -.
DR   PDBsum; 4QRF; -.
DR   PDBsum; 4QXV; -.
DR   PDBsum; 4QYA; -.
DR   PDBsum; 4TKW; -.
DR   PDBsum; 4TL4; -.
DR   PDBsum; 4TL5; -.
DR   PDBsum; 4TLK; -.
DR   PDBsum; 4TLS; -.
DR   PDBsum; 4TLT; -.
DR   PDBsum; 4TLU; -.
DR   PDBsum; 4TM9; -.
DR   PDBsum; 4TNE; -.
DR   PDBsum; 4TNF; -.
DR   PDBsum; 4TNG; -.
DR   PDBsum; 4TQ8; -.
DR   PDBsum; 4TQH; -.
DR   PDBsum; 4TQI; -.
DR   PDBsum; 4TQP; -.
DR   PDBsum; 4WNJ; -.
DR   PDBsum; 4WNS; -.
DR   PDBsum; 4WO0; -.
DR   PDBsum; 4Y9B; -.
DR   PDBsum; 4Y9C; -.
DR   PDBsum; 4Y9E; -.
DR   PDBsum; 4Y9F; -.
DR   PDBsum; 4Y9G; -.
DR   PDBsum; 4YDM; -.
DR   PDBsum; 4YDN; -.
DR   PDBsum; 5A6I; -.
DR   PDBsum; 5AKS; -.
DR   PDBsum; 5AKT; -.
DR   PDBsum; 5AKV; -.
DR   PDBsum; 5AL0; -.
DR   PDBsum; 5AL8; -.
DR   PDBsum; 5AYT; -.
DR   PDBsum; 5BOJ; -.
DR   PDBsum; 5CLX; -.
DR   PDBsum; 5CLY; -.
DR   PDBsum; 5CLZ; -.
DR   PDBsum; 5CM1; -.
DR   PDBsum; 5CN3; -.
DR   PDBsum; 5CNH; -.
DR   PDBsum; 5CR1; -.
DR   PDBsum; 5DEJ; -.
DR   PDBsum; 5DWP; -.
DR   PDBsum; 5E23; -.
DR   PDBsum; 5E4A; -.
DR   PDBsum; 5E4O; -.
DR   PDBsum; 5EN3; -.
DR   PDBsum; 5EZP; -.
DR   PDBsum; 5FO2; -.
DR   PDBsum; 5FW6; -.
DR   PDBsum; 5FW7; -.
DR   PDBsum; 5FW8; -.
DR   PDBsum; 5H0V; -.
DR   PDBsum; 5H0W; -.
DR   PDBsum; 5H0X; -.
DR   PDBsum; 5H0Y; -.
DR   PDBsum; 5H0Z; -.
DR   PDBsum; 5HJG; -.
DR   PDBsum; 5IHH; -.
DR   PDBsum; 5JID; -.
DR   PDBsum; 5JIM; -.
DR   PDBsum; 5JIQ; -.
DR   PDBsum; 5K1J; -.
DR   PDBsum; 5K1N; -.
DR   PDBsum; 5L4F; -.
DR   PDBsum; 5L4I; -.
DR   PDBsum; 5L4J; -.
DR   PDBsum; 5L4M; -.
DR   PDBsum; 5LLL; -.
DR   PDBsum; 5LLV; -.
DR   PDBsum; 5N5Q; -.
DR   PDBsum; 5N62; -.
DR   PDBsum; 5N7C; -.
DR   PDBsum; 5NFE; -.
DR   PDBsum; 5NFW; -.
DR   PDBsum; 5OQ0; -.
DR   PDBsum; 5TTR; -.
DR   PDBsum; 5TZL; -.
DR   PDBsum; 5U48; -.
DR   PDBsum; 5U49; -.
DR   PDBsum; 5U4A; -.
DR   PDBsum; 5U4B; -.
DR   PDBsum; 5U4C; -.
DR   PDBsum; 5U4D; -.
DR   PDBsum; 5U4E; -.
DR   PDBsum; 5U4F; -.
DR   PDBsum; 5U4G; -.
DR   PDBsum; 6D0W; -.
DR   PDBsum; 6E6Z; -.
DR   PDBsum; 6E70; -.
DR   PDBsum; 6E71; -.
DR   PDBsum; 6E72; -.
DR   PDBsum; 6E73; -.
DR   PDBsum; 6E74; -.
DR   PDBsum; 6E75; -.
DR   PDBsum; 6E76; -.
DR   PDBsum; 6E77; -.
DR   PDBsum; 6E78; -.
DR   PDBsum; 6EOY; -.
DR   PDBsum; 6EP1; -.
DR   PDBsum; 6FFT; -.
DR   PDBsum; 6FWD; -.
DR   PDBsum; 6FXU; -.
DR   PDBsum; 6FZL; -.
DR   PDBsum; 6GR7; -.
DR   PDBsum; 6GRP; -.
DR   PDBsum; 6IMX; -.
DR   PDBsum; 6IMY; -.
DR   PDBsum; 6KGB; -.
DR   PDBsum; 6R66; -.
DR   PDBsum; 6R67; -.
DR   PDBsum; 6R68; -.
DR   PDBsum; 6R6I; -.
DR   PDBsum; 6SDZ; -.
DR   PDBsum; 6SUG; -.
DR   PDBsum; 6SUH; -.
DR   PDBsum; 6TI9; -.
DR   PDBsum; 6TJN; -.
DR   PDBsum; 6TXV; -.
DR   PDBsum; 6TXW; -.
DR   PDBsum; 6U0Q; -.
DR   PDBsum; 6XTK; -.
DR   PDBsum; 7ACU; -.
DR   PDBsum; 7DT3; -.
DR   PDBsum; 7DT5; -.
DR   PDBsum; 7DT6; -.
DR   PDBsum; 7DT8; -.
DR   PDBsum; 7EJQ; -.
DR   PDBsum; 7EJR; -.
DR   PDBsum; 7ERH; -.
DR   PDBsum; 7ERI; -.
DR   PDBsum; 7ERJ; -.
DR   PDBsum; 7ERK; -.
DR   PDBsum; 7OB4; -.
DR   PDBsum; 7Q3I; -.
DR   PDBsum; 7Q9L; -.
DR   PDBsum; 7Q9N; -.
DR   PDBsum; 7Q9O; -.
DR   PDBsum; 7QC5; -.
DR   PDBsum; 7THA; -.
DR   PDBsum; 7W9Q; -.
DR   PDBsum; 7W9R; -.
DR   PDBsum; 7WL6; -.
DR   PDBsum; 7Y1I; -.
DR   PDBsum; 7Y6J; -.
DR   PDBsum; 7YBR; -.
DR   PDBsum; 7YCQ; -.
DR   PDBsum; 7Z60; -.
DR   PDBsum; 8ADE; -.
DR   PDBsum; 8AWI; -.
DR   PDBsum; 8AWW; -.
DR   PDBsum; 8E7D; -.
DR   PDBsum; 8E7E; -.
DR   PDBsum; 8E7H; -.
DR   PDBsum; 8E7I; -.
DR   PDBsum; 8E7J; -.
DR   PDBsum; 8HEJ; -.
DR   PDBsum; 8HY4; -.
DR   PDBsum; 8IG1; -.
DR   PDBsum; 8II1; -.
DR   PDBsum; 8II2; -.
DR   PDBsum; 8II3; -.
DR   PDBsum; 8II4; -.
DR   PDBsum; 8PKE; -.
DR   PDBsum; 8PKF; -.
DR   PDBsum; 8PKG; -.
DR   PDBsum; 8W42; -.
DR   PDBsum; 8W43; -.
DR   PDBsum; 8W44; -.
DR   PDBsum; 8W45; -.
DR   PDBsum; 8W46; -.
DR   PDBsum; 8W47; -.
DR   PDBsum; 8W48; -.
DR   AlphaFoldDB; P02766; -.
DR   BMRB; P02766; -.
DR   EMDB; EMD-10150; -.
DR   EMDB; EMD-12794; -.
DR   EMDB; EMD-15361; -.
DR   EMDB; EMD-26685; -.
DR   EMDB; EMD-26691; -.
DR   EMDB; EMD-26692; -.
DR   EMDB; EMD-27323; -.
DR   PCDDB; P02766; -.
DR   SMR; P02766; -.
DR   BioGRID; 113127; 105.
DR   CORUM; P02766; -.
DR   DIP; DIP-1083N; -.
DR   IntAct; P02766; 104.
DR   MINT; P02766; -.
DR   STRING; 9606.ENSP00000237014; -.
DR   BindingDB; P02766; -.
DR   ChEMBL; CHEMBL3194; -.
DR   DrugBank; DB07201; (2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid.
DR   DrugBank; DB07176; 1-Naphthylamine-5-sulfonic acid.
DR   DrugBank; DB07047; 2',4'-DICHLORO-4-HYDROXY-1,1'-BIPHENYL-3-CARBOXYLIC ACID.
DR   DrugBank; DB06935; 2',6'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID.
DR   DrugBank; DB02417; 2,4,6-Tribromophenol.
DR   DrugBank; DB07694; 2,5-dichloro-N-(3,5-dibromo-4-hydroxyphenyl)benzamide.
DR   DrugBank; DB08101; 2,6-dibromo-4-[(E)-2-phenylethenyl]phenol.
DR   DrugBank; DB08103; 2,6-dibromo-4-phenoxyphenol.
DR   DrugBank; DB08100; 2,6-dimethyl-4-[(E)-2-phenylethenyl]phenol.
DR   DrugBank; DB06907; 2-(2,6-DICHLOROPHENYL)-1,3-BENZOXAZOLE-6-CARBOXYLIC ACID.
DR   DrugBank; DB08207; 2-(3,5-DIMETHYLPHENYL)-1,3-BENZOXAZOLE.
DR   DrugBank; DB04756; 2-[(3,5-Dichloro-4-trioxidanylphenyl)amino]benzoic acid.
DR   DrugBank; DB04674; 2-HYDROXY-3,5-DIIODOBENZOIC ACID.
DR   DrugBank; DB07775; 3',5'-DIBROMO-2',4,4',6'-TETRAHYDROXY AURONE.
DR   DrugBank; DB07753; 3',5'-DIFLUOROBIPHENYL-4-CARBOXYLIC ACID.
DR   DrugBank; DB03239; 3',5'-Dinitro-N-Acetyl-L-Thyronine.
DR   DrugBank; DB03346; 3,3',5,5'-tetrachlorobiphenyl-4,4'-diol.
DR   DrugBank; DB08102; 3,5-dibromobiphenyl-4-ol.
DR   DrugBank; DB07282; 3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid.
DR   DrugBank; DB07240; 3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid.
DR   DrugBank; DB06885; 3-[({(1E)-[2-(trifluoromethyl)phenyl]methylidene}amino)oxy]propanoic acid.
DR   DrugBank; DB08206; 4-(1,3-BENZOXAZOL-2-YL)-2,6-DIBROMOPHENOL.
DR   DrugBank; DB08205; 4-(1,3-BENZOXAZOL-2-YL)-2,6-DIMETHYLPHENOL.
DR   DrugBank; DB01838; 6,4'-Dihydroxy-3-Methyl-3',5'-Dibromoflavone.
DR   DrugBank; DB04474; 8-anilinonaphthalene-1-sulfonic acid.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB03682; Dibenzofuran-4,6-Dicarboxylic Acid.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB00255; Diethylstilbestrol.
DR   DrugBank; DB00861; Diflunisal.
DR   DrugBank; DB01093; Dimethyl sulfoxide.
DR   DrugBank; DB02266; Flufenamic acid.
DR   DrugBank; DB05352; Fx-1006A.
DR   DrugBank; DB01645; Genistein.
DR   DrugBank; DB00451; Levothyroxine.
DR   DrugBank; DB00279; Liothyronine.
DR   DrugBank; DB01583; Liotrix.
DR   DrugBank; DB07962; METHYL N-[(2',4'-DIFLUORO-4-HYDROXY-5-IODOBIPHENYL-3-YL)CARBONYL]-BETA-ALANINATE.
DR   DrugBank; DB07693; N-(3,5-dibromo-4-hydroxyphenyl)-2,6-dimethylbenzamide.
DR   DrugBank; DB07695; N-(3,5-dibromo-4-hydroxyphenyl)-4-hydroxy-3,5-dimethylbenzamide.
DR   DrugBank; DB08104; N-(3,5-dibromo-4-hydroxyphenyl)benzamide.
DR   DrugBank; DB02698; N-(M-Trifluoromethylphenyl) Phenoxazine-4,6-Dicarboxylic Acid.
DR   DrugBank; DB07963; N-[(2',4'-DIFLUORO-4-HYDROXY-5-IODOBIPHENYL-3-YL)CARBONYL]-BETA-ALANINE.
DR   DrugBank; DB05235; NRP409.
DR   DrugBank; DB02179; O-Trifluoromethylphenyl Anthranilic Acid.
DR   DrugBank; DB03167; Pentabromophenol.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB16309; Revusiran.
DR   DrugBank; DB11644; Tafamidis.
DR   DrugBank; DB01751; Tetraiodothyroacetic acid.
DR   DrugBank; DB09100; Thyroid, porcine.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   DrugCentral; P02766; -.
DR   GuidetoPHARMACOLOGY; 2851; -.
DR   CarbonylDB; P02766; -.
DR   GlyCosmos; P02766; 1 site, No reported glycans.
DR   GlyGen; P02766; 1 site.
DR   iPTMnet; P02766; -.
DR   PhosphoSitePlus; P02766; -.
DR   BioMuta; TTR; -.
DR   DMDM; 136464; -.
DR   DOSAC-COBS-2DPAGE; P02766; -.
DR   REPRODUCTION-2DPAGE; P02766; -.
DR   CPTAC; non-CPTAC-1165; -.
DR   EPD; P02766; -.
DR   jPOST; P02766; -.
DR   MassIVE; P02766; -.
DR   MaxQB; P02766; -.
DR   PaxDb; 9606-ENSP00000237014; -.
DR   PeptideAtlas; P02766; -.
DR   PRIDE; P02766; -.
DR   ProteomicsDB; 51586; -.
DR   TopDownProteomics; P02766; -.
DR   Antibodypedia; 650; 1558 antibodies from 45 providers.
DR   CPTC; P02766; 1 antibody.
DR   DNASU; 7276; -.
DR   Ensembl; ENST00000237014.8; ENSP00000237014.4; ENSG00000118271.12.
DR   Ensembl; ENST00000649620.1; ENSP00000497927.1; ENSG00000118271.12.
DR   GeneID; 7276; -.
DR   KEGG; hsa:7276; -.
DR   MANE-Select; ENST00000237014.8; ENSP00000237014.4; NM_000371.4; NP_000362.1.
DR   UCSC; uc002kwx.5; human.
DR   AGR; HGNC:12405; -.
DR   CTD; 7276; -.
DR   DisGeNET; 7276; -.
DR   GeneCards; TTR; -.
DR   GeneReviews; TTR; -.
DR   HGNC; HGNC:12405; TTR.
DR   HPA; ENSG00000118271; Tissue enriched (choroid).
DR   MalaCards; TTR; -.
DR   MIM; 105210; phenotype.
DR   MIM; 115430; phenotype.
DR   MIM; 145680; phenotype.
DR   MIM; 176300; gene.
DR   neXtProt; NX_P02766; -.
DR   OpenTargets; ENSG00000118271; -.
DR   Orphanet; 85451; ATTRV122I amyloidosis.
DR   Orphanet; 85447; ATTRV30M amyloidosis.
DR   Orphanet; 597939; Euthyroid dysprealbuminemic hyperthyroxinemia.
DR   PharmGKB; PA37069; -.
DR   VEuPathDB; HostDB:ENSG00000118271; -.
DR   eggNOG; KOG3006; Eukaryota.
DR   GeneTree; ENSGT00940000153229; -.
DR   HOGENOM; CLU_115536_2_0_1; -.
DR   InParanoid; P02766; -.
DR   OMA; TWEPFAT; -.
DR   OrthoDB; 5352684at2759; -.
DR   PhylomeDB; P02766; -.
DR   TreeFam; TF300210; -.
DR   PathwayCommons; P02766; -.
DR   Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR   Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P02766; -.
DR   BioGRID-ORCS; 7276; 10 hits in 1147 CRISPR screens.
DR   ChiTaRS; TTR; human.
DR   EvolutionaryTrace; P02766; -.
DR   GeneWiki; Transthyretin; -.
DR   GenomeRNAi; 7276; -.
DR   Pharos; P02766; Tclin.
DR   PRO; PR:P02766; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P02766; Protein.
DR   Bgee; ENSG00000118271; Expressed in choroid plexus epithelium and 143 other cell types or tissues.
DR   ExpressionAtlas; P02766; baseline and differential.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR   CDD; cd05821; TLP_Transthyretin; 1.
DR   Gene3D; 2.60.40.180; Transthyretin/hydroxyisourate hydrolase domain; 1.
DR   InterPro; IPR023418; Thyroxine_BS.
DR   InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR   InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR   InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR   InterPro; IPR023419; Transthyretin_CS.
DR   PANTHER; PTHR10395:SF12; TRANSTHYRETIN; 1.
DR   PANTHER; PTHR10395; URICASE AND TRANSTHYRETIN-RELATED; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SMART; SM00095; TR_THY; 1.
DR   SUPFAM; SSF49472; Transthyretin (synonym: prealbumin); 1.
DR   PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
DR   SWISS-2DPAGE; P02766; -.
DR   UCD-2DPAGE; P02766; -.
DR   Genevisible; P02766; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Amyloid; Amyloidosis; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Gamma-carboxyglutamic acid; Glycoprotein; Hormone;
KW   Neuropathy; Phosphoprotein; Reference proteome; Secreted; Signal;
KW   Sulfation; Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:1517749, ECO:0000269|PubMed:3135807,
FT                   ECO:0000269|PubMed:4607556, ECO:0000269|PubMed:6583672,
FT                   ECO:0000269|PubMed:6651852"
FT   CHAIN           21..147
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035755"
FT   BINDING         35
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000269|PubMed:11418763,
FT                   ECO:0007744|PDB:1ICT"
FT   BINDING         74
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000269|PubMed:11418763,
FT                   ECO:0007744|PDB:1ICT"
FT   BINDING         137
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000269|PubMed:11418763,
FT                   ECO:0007744|PDB:1ICT"
FT   MOD_RES         30
FT                   /note="Sulfocysteine"
FT                   /evidence="ECO:0000269|PubMed:17175208,
FT                   ECO:0007744|PDB:2H4E"
FT   MOD_RES         62
FT                   /note="4-carboxyglutamate; in a patient with Moyamoya
FT                   disease"
FT                   /evidence="ECO:0000269|PubMed:18221012"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02767"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19167329"
FT   VARIANT         26
FT                   /note="G -> S (in dbSNP:rs1800458)"
FT                   /evidence="ECO:0000269|PubMed:10211412,
FT                   ECO:0000269|PubMed:11866053, ECO:0000269|PubMed:15217993,
FT                   ECO:0000269|PubMed:6300852, ECO:0000269|PubMed:8019560"
FT                   /id="VAR_007546"
FT   VARIANT         30
FT                   /note="C -> R (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918083)"
FT                   /evidence="ECO:0000269|PubMed:1362222"
FT                   /id="VAR_007547"
FT   VARIANT         32
FT                   /note="L -> P (in AMYL-TTR; dbSNP:rs121918094)"
FT                   /evidence="ECO:0000269|PubMed:10071047,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038959"
FT   VARIANT         33
FT                   /note="M -> I"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038960"
FT   VARIANT         38
FT                   /note="D -> E (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /id="VAR_007548"
FT   VARIANT         38
FT                   /note="D -> G (in AMYL-TTR; leptomeningeal amyloidosis;
FT                   leads to unfolding and exposure of N-118 to glycosylation
FT                   by STT3B and subsequent degradation by the ERAD pathway;
FT                   dbSNP:rs121918098)"
FT                   /evidence="ECO:0000269|PubMed:19167329,
FT                   ECO:0000269|PubMed:8579098"
FT                   /id="VAR_007549"
FT   VARIANT         40
FT                   /note="V -> I (in AMYL-TTR; late-onset amyloid
FT                   polyneuropathy with carpal tunnel syndrome;
FT                   dbSNP:rs121918093)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:8990019"
FT                   /id="VAR_007550"
FT   VARIANT         43
FT                   /note="S -> N (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:10439117"
FT                   /id="VAR_038961"
FT   VARIANT         44
FT                   /note="P -> S (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs11541790)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007551"
FT   VARIANT         48
FT                   /note="V -> M (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:10882995"
FT                   /id="VAR_010658"
FT   VARIANT         50
FT                   /note="V -> A (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs79977247)"
FT                   /evidence="ECO:0000269|PubMed:1544214,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007552"
FT   VARIANT         50
FT                   /note="V -> G (in AMYL-TTR; dbSNP:rs79977247)"
FT                   /evidence="ECO:0000269|PubMed:9066351"
FT                   /id="VAR_038962"
FT   VARIANT         50
FT                   /note="V -> L (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs28933979)"
FT                   /evidence="ECO:0000269|PubMed:10611950,
FT                   ECO:0000269|PubMed:1520326"
FT                   /id="VAR_007553"
FT   VARIANT         50
FT                   /note="V -> M (in AMYL-TTR; amyloid polyneuropathy; by far
FT                   the most frequent mutation; dbSNP:rs28933979)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:1517749, ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:3022108, ECO:0000269|PubMed:3818577,
FT                   ECO:0000269|PubMed:6583672, ECO:0000269|PubMed:6651852,
FT                   ECO:0000269|PubMed:7655883, ECO:0000269|PubMed:8382610,
FT                   ECO:0000269|PubMed:8428915"
FT                   /id="VAR_007554"
FT   VARIANT         53
FT                   /note="F -> C (in a patient with amyloidosis)"
FT                   /evidence="ECO:0000269|PubMed:12876326,
FT                   ECO:0000269|PubMed:15217993"
FT                   /id="VAR_038963"
FT   VARIANT         53
FT                   /note="F -> I (in AMYL-TTR; Jewish 'SKO' amyloid
FT                   polyneuropathy; dbSNP:rs121918068)"
FT                   /evidence="ECO:0000269|PubMed:6487335,
FT                   ECO:0000269|PubMed:8019560"
FT                   /id="VAR_007555"
FT   VARIANT         53
FT                   /note="F -> L (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918068)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:1932142,
FT                   ECO:0000269|PubMed:2046936"
FT                   /id="VAR_007556"
FT   VARIANT         53
FT                   /note="F -> V (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:10611950,
FT                   ECO:0000269|PubMed:12050338, ECO:0000269|PubMed:15478468,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038964"
FT   VARIANT         54
FT                   /note="R -> T (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:9605286"
FT                   /id="VAR_038965"
FT   VARIANT         55
FT                   /note="K -> N (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:7655883"
FT                   /id="VAR_038966"
FT   VARIANT         56
FT                   /note="A -> P (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918077)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007557"
FT   VARIANT         58
FT                   /note="D -> A (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:10611950,
FT                   ECO:0000269|PubMed:11866053"
FT                   /id="VAR_038967"
FT   VARIANT         58
FT                   /note="D -> V (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:17635579"
FT                   /id="VAR_038968"
FT   VARIANT         61
FT                   /note="W -> L (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:11866053"
FT                   /id="VAR_038969"
FT   VARIANT         62
FT                   /note="E -> D (in AMYL-TTR; dbSNP:rs11541796)"
FT                   /evidence="ECO:0000269|PubMed:10036587"
FT                   /id="VAR_038970"
FT   VARIANT         62
FT                   /note="E -> G (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs11541796)"
FT                   /evidence="ECO:0000269|PubMed:2363717,
FT                   ECO:0000269|PubMed:7923855"
FT                   /id="VAR_007558"
FT   VARIANT         64
FT                   /note="F -> S (in AMYL-TTR; dbSNP:rs104894665)"
FT                   /evidence="ECO:0000269|PubMed:11866053,
FT                   ECO:0000269|PubMed:9818883"
FT                   /id="VAR_038971"
FT   VARIANT         65
FT                   /note="A -> D (in AMYL-TTR; amyloid cardiomyopathy;
FT                   dbSNP:rs730881169)"
FT                   /id="VAR_007559"
FT   VARIANT         65
FT                   /note="A -> S (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:10842718"
FT                   /id="VAR_038972"
FT   VARIANT         65
FT                   /note="A -> T (in AMYL-TTR; amyloid cardiomyopathy;
FT                   dbSNP:rs121918078)"
FT                   /evidence="ECO:0000269|PubMed:1570831,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007560"
FT   VARIANT         67
FT                   /note="G -> A (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918090)"
FT                   /evidence="ECO:0000269|PubMed:17503405, ECO:0000269|Ref.91"
FT                   /id="VAR_007561"
FT   VARIANT         67
FT                   /note="G -> E (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:15217993"
FT                   /id="VAR_038973"
FT   VARIANT         67
FT                   /note="G -> R (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs387906523)"
FT                   /evidence="ECO:0000269|PubMed:1734866"
FT                   /id="VAR_007562"
FT   VARIANT         67
FT                   /note="G -> V (in AMYL-TTR; amyloid polyneuropathy with
FT                   carpal tunnel syndrome)"
FT                   /id="VAR_007563"
FT   VARIANT         69
FT                   /note="T -> A (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918081)"
FT                   /evidence="ECO:0000269|PubMed:1301926,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:7655883"
FT                   /id="VAR_007564"
FT   VARIANT         69
FT                   /note="T -> I (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:10436378,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038974"
FT   VARIANT         70
FT                   /note="S -> I (in AMYL-TTR; amyloid cardiomyopathy;
FT                   dbSNP:rs121918080)"
FT                   /evidence="ECO:0000269|PubMed:1520336"
FT                   /id="VAR_007565"
FT   VARIANT         70
FT                   /note="S -> R (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs386134269)"
FT                   /evidence="ECO:0000269|PubMed:10611950,
FT                   ECO:0000269|PubMed:23317988, ECO:0000269|PubMed:2363717,
FT                   ECO:0000269|PubMed:7655883"
FT                   /id="VAR_007566"
FT   VARIANT         72
FT                   /note="S -> P (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /id="VAR_007567"
FT   VARIANT         73
FT                   /note="G -> E (in AMYL-TTR; dbSNP:rs121918097)"
FT                   /evidence="ECO:0000269|PubMed:11445644"
FT                   /id="VAR_038975"
FT   VARIANT         74
FT                   /note="E -> G (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /id="VAR_007568"
FT   VARIANT         74
FT                   /note="E -> K (in AMYL-TTR; early-onset amyloid
FT                   polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:15214015"
FT                   /id="VAR_038976"
FT   VARIANT         75
FT                   /note="L -> P (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918079)"
FT                   /evidence="ECO:0000269|PubMed:1351039,
FT                   ECO:0000269|PubMed:16627944, ECO:0000269|PubMed:7910950,
FT                   ECO:0000269|PubMed:9733771"
FT                   /id="VAR_007569"
FT   VARIANT         75
FT                   /note="L -> Q (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:12557757"
FT                   /id="VAR_038977"
FT   VARIANT         78
FT                   /note="L -> H (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918069)"
FT                   /evidence="ECO:0000269|PubMed:15217993"
FT                   /id="VAR_007570"
FT   VARIANT         78
FT                   /note="L -> R (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918069)"
FT                   /evidence="ECO:0000269|PubMed:1656975"
FT                   /id="VAR_007571"
FT   VARIANT         79
FT                   /note="T -> K (in AMYL-TTR; amyloid cardiomyopathy;
FT                   dbSNP:rs730881163)"
FT                   /evidence="ECO:0000269|PubMed:7850982"
FT                   /id="VAR_007572"
FT   VARIANT         80
FT                   /note="T -> A (in AMYL-TTR; amyloid polyneuropathy and
FT                   cardiomyopathy; dbSNP:rs121918070)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:15217993, ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:7655883"
FT                   /id="VAR_007573"
FT   VARIANT         81
FT                   /note="E -> G (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:17453626"
FT                   /id="VAR_038978"
FT   VARIANT         81
FT                   /note="E -> K (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918086)"
FT                   /evidence="ECO:0000269|PubMed:8352764"
FT                   /id="VAR_007574"
FT   VARIANT         84
FT                   /note="F -> L (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918091)"
FT                   /evidence="ECO:0000269|PubMed:11866053,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:2046936"
FT                   /id="VAR_007575"
FT   VARIANT         88
FT                   /note="I -> L (in AMYL-TTR; amyloid cardiomyopathy;
FT                   dbSNP:rs121918085)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:8038017"
FT                   /id="VAR_007576"
FT   VARIANT         89
FT                   /note="Y -> H (in AMYL-TTR; leptomeningeal amyloidosis;
FT                   vitreous amyloid in some patients; dbSNP:rs121918100)"
FT                   /evidence="ECO:0000269|PubMed:12771253"
FT                   /id="VAR_007577"
FT   VARIANT         90
FT                   /note="K -> N (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs267607160)"
FT                   /evidence="ECO:0000269|PubMed:1436517"
FT                   /id="VAR_007578"
FT   VARIANT         91
FT                   /note="V -> A (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918084)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:8095302, ECO:0000269|PubMed:8257997"
FT                   /id="VAR_007579"
FT   VARIANT         93
FT                   /note="I -> V (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:10694917"
FT                   /id="VAR_007580"
FT   VARIANT         94
FT                   /note="D -> H (in dbSNP:rs730881164)"
FT                   /id="VAR_007581"
FT   VARIANT         97
FT                   /note="S -> Y (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918071)"
FT                   /evidence="ECO:0000269|PubMed:15217993,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:2891727,
FT                   ECO:0000269|PubMed:7655883"
FT                   /id="VAR_007582"
FT   VARIANT         98
FT                   /note="Y -> F (in AMYL-TTR; dbSNP:rs958191819)"
FT                   /evidence="ECO:0000269|PubMed:16627944,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038979"
FT   VARIANT         104
FT                   /note="I -> N (in AMYL-TTR; vitrous amyloid)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007583"
FT   VARIANT         104
FT                   /note="I -> S (in AMYL-TTR; amyloid polyneuropathy; almost
FT                   no RBP binding; dbSNP:rs121918072)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:3722385, ECO:0000269|PubMed:8089102"
FT                   /id="VAR_007584"
FT   VARIANT         104
FT                   /note="I -> T (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038980"
FT   VARIANT         109
FT                   /note="E -> K (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:10842705"
FT                   /id="VAR_010659"
FT   VARIANT         109
FT                   /note="E -> Q (in AMYL-TTR; amyloid polyneuropathy and
FT                   cardiomyopathy; dbSNP:rs121918082)"
FT                   /evidence="ECO:0000269|PubMed:1301926,
FT                   ECO:0000269|PubMed:7655883"
FT                   /id="VAR_007585"
FT   VARIANT         110
FT                   /note="H -> N (in dbSNP:rs121918074)"
FT                   /evidence="ECO:0000269|PubMed:1997217,
FT                   ECO:0000269|PubMed:7923855"
FT                   /id="VAR_007586"
FT   VARIANT         111
FT                   /note="A -> S (in AMYL-TTR; amyloid polyneuropathy)"
FT                   /evidence="ECO:0000269|PubMed:10627135"
FT                   /id="VAR_007587"
FT   VARIANT         114
FT                   /note="V -> A (in a patient with amyloidosis)"
FT                   /evidence="ECO:0000269|PubMed:15217993,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038981"
FT   VARIANT         117
FT                   /note="A -> G (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918087)"
FT                   /evidence="ECO:0000269|PubMed:10611950,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:8133316"
FT                   /id="VAR_007588"
FT   VARIANT         117
FT                   /note="A -> S (in AMYL-TTR; dbSNP:rs267607161)"
FT                   /evidence="ECO:0000269|PubMed:10611950"
FT                   /id="VAR_038982"
FT   VARIANT         121
FT                   /note="G -> S (in dbSNP:rs755337715)"
FT                   /evidence="ECO:0000269|PubMed:10671063,
FT                   ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007589"
FT   VARIANT         122
FT                   /note="P -> R"
FT                   /id="VAR_007590"
FT   VARIANT         124
FT                   /note="R -> C (in dbSNP:rs745834030)"
FT                   /id="VAR_007591"
FT   VARIANT         124
FT                   /note="R -> H (in dbSNP:rs121918095)"
FT                   /evidence="ECO:0000269|PubMed:10529370,
FT                   ECO:0000269|PubMed:15735344"
FT                   /id="VAR_038983"
FT   VARIANT         126
FT                   /note="T -> N (in AMYL-TTR; dbSNP:rs1456101911)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038984"
FT   VARIANT         127
FT                   /note="I -> M (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_038985"
FT   VARIANT         127
FT                   /note="I -> V (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918089)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:7914929, ECO:0000269|PubMed:8081397"
FT                   /id="VAR_007592"
FT   VARIANT         129
FT                   /note="A -> T (in DTTRH; increased affinity for thyroxine;
FT                   dbSNP:rs267607159)"
FT                   /evidence="ECO:0000269|PubMed:17503405,
FT                   ECO:0000269|PubMed:1979335"
FT                   /id="VAR_007593"
FT   VARIANT         131
FT                   /note="L -> M (in AMYL-TTR; dbSNP:rs121918073)"
FT                   /evidence="ECO:0000269|PubMed:17503405"
FT                   /id="VAR_007594"
FT   VARIANT         134
FT                   /note="Y -> C (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs121918075)"
FT                   /evidence="ECO:0000269|PubMed:12403615,
FT                   ECO:0000269|PubMed:16185074, ECO:0000269|PubMed:2161654"
FT                   /id="VAR_007595"
FT   VARIANT         134
FT                   /note="Y -> H (in CTS1; amyloid deposit on carpal tunnel;
FT                   patients show no other abnormalities; dbSNP:rs121918088)"
FT                   /evidence="ECO:0000269|PubMed:8309582"
FT                   /id="VAR_007598"
FT   VARIANT         136
FT                   /note="Y -> S (in AMYL-TTR; amyloid polyneuropathy;
FT                   dbSNP:rs730881167)"
FT                   /evidence="ECO:0000269|PubMed:10627135"
FT                   /id="VAR_007596"
FT   VARIANT         136
FT                   /note="Y -> V (requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:3675594"
FT                   /id="VAR_007597"
FT   VARIANT         139
FT                   /note="T -> M (in Chicago variant; dbSNP:rs28933981)"
FT                   /evidence="ECO:0000269|PubMed:11866053,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:1877623"
FT                   /id="VAR_007599"
FT   VARIANT         140
FT                   /note="A -> S (in AMYL-TTR; dbSNP:rs876658108)"
FT                   /evidence="ECO:0000269|PubMed:12050338"
FT                   /id="VAR_038986"
FT   VARIANT         142
FT                   /note="V -> A (in AMYL-TTR)"
FT                   /evidence="ECO:0000269|PubMed:10211412"
FT                   /id="VAR_038987"
FT   VARIANT         142
FT                   /note="V -> I (in AMYL-TTR; dbSNP:rs76992529)"
FT                   /evidence="ECO:0000269|PubMed:12050338,
FT                   ECO:0000269|PubMed:17503405, ECO:0000269|PubMed:3135807"
FT                   /id="VAR_007600"
FT   VARIANT         144
FT                   /note="N -> S (in AMYL-TTR; dbSNP:rs144965179)"
FT                   /evidence="ECO:0000269|PubMed:17577687"
FT                   /id="VAR_038988"
FT   MUTAGEN         107
FT                   /note="F->M: Loss of tetramerization; when associated with
FT                   M-130."
FT                   /evidence="ECO:0000269|PubMed:11560492"
FT   MUTAGEN         130
FT                   /note="L->M: Loss of tetramerization; when associated with
FT                   M-107."
FT                   /evidence="ECO:0000269|PubMed:11560492"
FT   CONFLICT        41
FT                   /note="R -> P (in Ref. 3; AAA98771)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="E -> D (in Ref. 12; CAG33189)"
FT                   /evidence="ECO:0000305"
FT   TURN            23..26
FT                   /evidence="ECO:0007829|PDB:1TSH"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   TURN            39..42
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:6E78"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:2QEL"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   HELIX           95..101
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          107..118
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:5JIM"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:1F86"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:1F86"
SQ   SEQUENCE   147 AA;  15887 MW;  3A6AEBCBBA56BC44 CRC64;
     MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT
     WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS
     GPRRYTIAAL LSPYSYSTTA VVTNPKE
//