ID   TFPI2_HUMAN             Reviewed;         235 AA.
AC   P48307; Q66ME8; Q8NAK6; Q9UC86;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Tissue factor pathway inhibitor 2;
DE            Short=TFPI-2;
DE   AltName: Full=Placental protein 5;
DE            Short=PP5;
DE   Flags: Precursor;
GN   Name=TFPI2;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Placenta;
RX   PubMed=7896752; DOI=10.1093/oxfordjournals.jbchem.a124648;
RA   Miyagi Y., Koshikawa N., Yasumitsu H., Miyagi E., Hirahara F., Aoki I.,
RA   Misugi K., Umeda M., Miyazaki K.;
RT   "cDNA cloning and mRNA expression of a serine proteinase inhibitor secreted
RT   by cancer cells: identification as placental protein 5 and tissue factor
RT   pathway inhibitor-2.";
RL   J. Biochem. 116:939-942(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=8159751; DOI=10.1073/pnas.91.8.3353;
RA   Sprecher C.A., Kisiel W., Mathewes S., Foster D.C.;
RT   "Molecular cloning, expression, and partial characterization of a second
RT   human tissue-factor-pathway inhibitor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3353-3357(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11342222; DOI=10.1016/s0167-4781(00)00298-0;
RA   Kamei S., Kazama Y., Kuijper J.L., Foster D.C., Kisiel W.;
RT   "Genomic structure and promoter activity of the human tissue factor pathway
RT   inhibitor-2 gene.";
RL   Biochim. Biophys. Acta 1517:430-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Xu Y., Li T., Du G.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [10]
RP   PROTEIN SEQUENCE OF 23-42, AND FUNCTION.
RC   TISSUE=Fibroblast;
RX   PubMed=7872799; DOI=10.1006/abbi.1995.1168;
RA   Rao C.N., Liu Y.Y., Peavey C.L., Woodley D.T.;
RT   "Novel extracellular matrix-associated serine proteinase inhibitors from
RT   human skin fibroblasts.";
RL   Arch. Biochem. Biophys. 317:311-314(1995).
RN   [11]
RP   PROTEIN SEQUENCE OF 23-35; 47-53 AND 133-146.
RC   TISSUE=Placenta;
RX   PubMed=3276312; DOI=10.1016/0006-291x(88)90546-3;
RA   Buetzow R., Huhtala M.-L., Bohn H., Virtanen I., Seppaelae M.;
RT   "Purification and characterization of placental protein 5.";
RL   Biochem. Biophys. Res. Commun. 150:483-490(1988).
RN   [12]
RP   ERRATUM OF PUBMED:3276312.
RA   Buetzow R., Huhtala M.-L., Bohn H., Virtanen I., Seppaelae M.;
RL   Biochem. Biophys. Res. Commun. 151:630-631(1988).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-90 IN COMPLEX WITH BOVINE
RP   TRYPSIN, AND DISULFIDE BONDS.
RX   PubMed=15932872; DOI=10.1074/jbc.m504105200;
RA   Schmidt A.E., Chand H.S., Cascio D., Kisiel W., Bajaj S.P.;
RT   "Crystal structure of Kunitz domain 1 (KD1) of tissue factor pathway
RT   inhibitor-2 in complex with trypsin. Implications for KD1 specificity of
RT   inhibition.";
RL   J. Biol. Chem. 280:27832-27838(2005).
RN   [14]
RP   INTERACTION WITH PPP2R3C.
RX   PubMed=24333728; DOI=10.1016/j.canlet.2013.12.007;
RA   Katayama K., Yamaguchi M., Noguchi K., Sugimoto Y.;
RT   "Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-
RT   glycoprotein/ABCB1 and down-regulates the expression and function.";
RL   Cancer Lett. 345:124-131(2014).
CC   -!- FUNCTION: May play a role in the regulation of plasmin-mediated matrix
CC       remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and
CC       weakly factor Xa. Has no effect on thrombin.
CC       {ECO:0000269|PubMed:7872799}.
CC   -!- SUBUNIT: Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to
CC       the dephosphorylation of ABCB1. {ECO:0000269|PubMed:24333728}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P48307-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48307-2; Sequence=VSP_056031;
CC   -!- TISSUE SPECIFICITY: Umbilical vein endothelial cells, liver, placenta,
CC       heart, pancreas, and maternal serum at advanced pregnancy.
CC   -!- DOMAIN: This inhibitor contains three inhibitory domains.
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DR   EMBL; D29992; BAA06272.1; -; mRNA.
DR   EMBL; L27624; AAA20094.1; -; mRNA.
DR   EMBL; AF217542; AAK13254.1; -; Genomic_DNA.
DR   EMBL; AY691946; AAU04568.1; -; mRNA.
DR   EMBL; AK092499; BAC03906.1; -; mRNA.
DR   EMBL; AK313260; BAG36070.1; -; mRNA.
DR   EMBL; AC002076; AAS02022.1; -; Genomic_DNA.
DR   EMBL; CH236949; EAL24140.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76809.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76811.1; -; Genomic_DNA.
DR   EMBL; BC005330; AAH05330.1; -; mRNA.
DR   CCDS; CCDS5632.1; -. [P48307-1]
DR   PIR; A54951; A54951.
DR   PIR; S71593; S71593.
DR   RefSeq; NP_001257932.1; NM_001271003.1. [P48307-2]
DR   RefSeq; NP_006519.1; NM_006528.3. [P48307-1]
DR   PDB; 1ZR0; X-ray; 1.80 A; B/D=28-90.
DR   PDBsum; 1ZR0; -.
DR   AlphaFoldDB; P48307; -.
DR   SMR; P48307; -.
DR   BioGRID; 113693; 46.
DR   CORUM; P48307; -.
DR   IntAct; P48307; 2.
DR   MINT; P48307; -.
DR   STRING; 9606.ENSP00000222543; -.
DR   MEROPS; I02.013; -.
DR   MEROPS; I02.014; -.
DR   MEROPS; I02.951; -.
DR   GlyCosmos; P48307; 2 sites, No reported glycans.
DR   GlyGen; P48307; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P48307; -.
DR   PhosphoSitePlus; P48307; -.
DR   BioMuta; TFPI2; -.
DR   DMDM; 1351226; -.
DR   jPOST; P48307; -.
DR   MassIVE; P48307; -.
DR   MaxQB; P48307; -.
DR   PaxDb; 9606-ENSP00000222543; -.
DR   PeptideAtlas; P48307; -.
DR   ProteomicsDB; 55875; -. [P48307-1]
DR   Pumba; P48307; -.
DR   Antibodypedia; 4115; 598 antibodies from 34 providers.
DR   DNASU; 7980; -.
DR   Ensembl; ENST00000222543.11; ENSP00000222543.5; ENSG00000105825.14. [P48307-1]
DR   GeneID; 7980; -.
DR   KEGG; hsa:7980; -.
DR   MANE-Select; ENST00000222543.11; ENSP00000222543.5; NM_006528.4; NP_006519.1.
DR   UCSC; uc003umy.2; human. [P48307-1]
DR   AGR; HGNC:11761; -.
DR   CTD; 7980; -.
DR   DisGeNET; 7980; -.
DR   GeneCards; TFPI2; -.
DR   HGNC; HGNC:11761; TFPI2.
DR   HPA; ENSG00000105825; Tissue enriched (placenta).
DR   MIM; 600033; gene.
DR   neXtProt; NX_P48307; -.
DR   OpenTargets; ENSG00000105825; -.
DR   PharmGKB; PA36476; -.
DR   VEuPathDB; HostDB:ENSG00000105825; -.
DR   eggNOG; KOG4295; Eukaryota.
DR   GeneTree; ENSGT00940000159917; -.
DR   HOGENOM; CLU_058441_1_0_1; -.
DR   InParanoid; P48307; -.
DR   OrthoDB; 3558236at2759; -.
DR   PhylomeDB; P48307; -.
DR   TreeFam; TF315349; -.
DR   PathwayCommons; P48307; -.
DR   SignaLink; P48307; -.
DR   BioGRID-ORCS; 7980; 12 hits in 1149 CRISPR screens.
DR   ChiTaRS; TFPI2; human.
DR   EvolutionaryTrace; P48307; -.
DR   GeneWiki; TFPI2; -.
DR   GenomeRNAi; 7980; -.
DR   Pharos; P48307; Tbio.
DR   PRO; PR:P48307; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P48307; Protein.
DR   Bgee; ENSG00000105825; Expressed in stromal cell of endometrium and 128 other cell types or tissues.
DR   ExpressionAtlas; P48307; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR   CDD; cd22615; Kunitz_TFPI1_TFPI2_3-like; 1.
DR   CDD; cd22616; Kunitz_TFPI2_1-like; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 3.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR008296; TFPI-like.
DR   PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR10083:SF352; TISSUE FACTOR PATHWAY INHIBITOR 2; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 3.
DR   PIRSF; PIRSF001620; TFPI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 3.
DR   SUPFAM; SSF57362; BPTI-like; 3.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 3.
DR   Genevisible; P48307; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Blood coagulation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW   Protease inhibitor; Reference proteome; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:3276312,
FT                   ECO:0000269|PubMed:7872799"
FT   CHAIN           23..235
FT                   /note="Tissue factor pathway inhibitor 2"
FT                   /id="PRO_0000016876"
FT   DOMAIN          36..86
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          96..149
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          158..208
FT                   /note="BPTI/Kunitz inhibitor 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            46..47
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            107..108
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            168..169
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:15932872"
FT   DISULFID        45..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:15932872"
FT   DISULFID        61..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000269|PubMed:15932872"
FT   DISULFID        96..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        106..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        122..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        158..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        167..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        183..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   VAR_SEQ         30..40
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056031"
FT   VARIANT         102
FT                   /note="V -> A (in dbSNP:rs1804202)"
FT                   /id="VAR_012005"
FT   VARIANT         231
FT                   /note="R -> Q (in dbSNP:rs12669450)"
FT                   /id="VAR_050064"
FT   CONFLICT        23
FT                   /note="D -> A (in Ref. 11; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="D -> G (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="C -> I (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="Y -> R (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:1ZR0"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1ZR0"
FT   TURN            56..59
FT                   /evidence="ECO:0007829|PDB:1ZR0"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:1ZR0"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:1ZR0"
FT   HELIX           79..85
FT                   /evidence="ECO:0007829|PDB:1ZR0"
SQ   SEQUENCE   235 AA;  26934 MW;  975ABA5C53F7C65F CRC64;
     MDPARPLGLS ILLLFLTEAA LGDAAQEPTG NNAEICLLPL DYGPCRALLL RYYYDRYTQS
     CRQFLYGGCE GNANNFYTWE ACDDACWRIE KVPKVCRLQV SVDDQCEGST EKYFFNLSSM
     TCEKFFSGGC HRNRIENRFP DEATCMGFCA PKKIPSFCYS PKDEGLCSAN VTRYYFNPRY
     RTCDAFTYTG CGGNDNNFVS REDCKRACAK ALKKKKKMPK LRFASRIRKI RKKQF
//