ID   TSP4_HUMAN              Reviewed;         961 AA.
AC   P35443; B2R909; Q86TG2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   24-JAN-2024, entry version 212.
DE   RecName: Full=Thrombospondin-4;
DE   Flags: Precursor;
GN   Name=THBS4; Synonyms=TSP4;
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], AND VARIANT VAL-420.
RC   TISSUE=Heart;
RX   PubMed=8350346; DOI=10.1007/bf00556355;
RA   Lawler J., Duquette M., Urry L., McHenry K., Smith T.F.;
RT   "The evolution of the thrombospondin gene family.";
RL   J. Mol. Evol. 36:509-516(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420, AND SUBUNIT.
RX   PubMed=7852353; DOI=10.1074/jbc.270.6.2809;
RA   Lawler J., McHenry K., Duquette M., Derick L.;
RT   "Characterization of human thrombospondin-4.";
RL   J. Biol. Chem. 270:2809-2814(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-387.
RC   TISSUE=Synovium;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-55; PRO-387; VAL-420
RP   AND ILE-646.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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   [6]
RP   FUNCTION IN CELL PROLIFERATION, AND INTERACTION WITH PTBP3.
RX   PubMed=19441079; DOI=10.1002/jcp.21817;
RA   Sadvakassova G., Dobocan M.C., Difalco M.R., Congote L.F.;
RT   "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal
RT   peptide of thrombospondin-4 and is involved in its mitogenic activity.";
RL   J. Cell. Physiol. 220:672-679(2009).
RN   [7]
RP   INTERACTION WITH ATF6.
RX   PubMed=22682248; DOI=10.1016/j.cell.2012.03.050;
RA   Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A.,
RA   Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R.,
RA   Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.;
RT   "A thrombospondin-dependent pathway for a protective ER stress response.";
RL   Cell 149:1257-1268(2012).
RN   [8]
RP   REVIEW.
RX   PubMed=23287452; DOI=10.1161/circresaha.112.280560;
RA   Doroudgar S., Glembotski C.C.;
RT   "ATF6 [corrected] and thrombospondin 4: the dynamic duo of the adaptive
RT   endoplasmic reticulum stress response.";
RL   Circ. Res. 112:9-12(2013).
RN   [9]
RP   ERRATUM OF PUBMED:23287452.
RX   DOI=10.1161/RES.0b013e318286c21f;
RA   Doroudgar S., Glembotski C.C.;
RL   Circ. Res. 112:E31-E31(2013).
RN   [10]
RP   REVIEW.
RX   PubMed=23892609; DOI=10.1097/mol.0b013e3283642912;
RA   Stenina-Adognravi O.;
RT   "Thrombospondins: old players, new games.";
RL   Curr. Opin. Lipidol. 24:401-409(2013).
RN   [11]
RP   VARIANT PRO-387.
RX   PubMed=22011848; DOI=10.1160/th11-03-0206;
RA   Corsetti J.P., Ryan D., Moss A.J., McCarthy J., Goldenberg I., Zareba W.,
RA   Sparks C.E.;
RT   "Thrombospondin-4 polymorphism (A387P) predicts cardiovascular risk in
RT   postinfarction patients with high HDL cholesterol and C-reactive protein
RT   levels.";
RL   Thromb. Haemost. 106:1170-1178(2011).
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC       matrix interactions and is involved in various processes including
CC       cellular proliferation, migration, adhesion and attachment,
CC       inflammatory response to CNS injury, regulation of vascular
CC       inflammation and adaptive responses of the heart to pressure overload
CC       and in myocardial function and remodeling. Binds to structural
CC       extracellular matrix (ECM) proteins and modulates the ECM in response
CC       to tissue damage, contributing to cardioprotective and adaptive ECM
CC       remodeling. Plays a role in ER stress response, via its interaction
CC       with the activating transcription factor 6 alpha (ATF6) which produces
CC       adaptive ER stress response factors and protects myocardium from
CC       pressure overload. May contribute to spinal presynaptic
CC       hypersensitivity and neuropathic pain states after peripheral nerve
CC       injury. May play a role in regulating protective astrogenesis from the
CC       subventricular zone (SVZ) niche after injury in a NOTCH1-dependent
CC       manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:19441079}.
CC   -!- SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3.
CC       Interacts with NOTCH1 (By similarity). Interacts (via EGF-like 3;
CC       calcium-binding domain) with ATF6 and facilitates its processing,
CC       activation and nuclear translocation. {ECO:0000250,
CC       ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:22682248,
CC       ECO:0000269|PubMed:7852353}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:Q9Z1T2}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/thbs4/";
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DR   EMBL; Z19585; CAA79635.1; -; mRNA.
DR   EMBL; AK313587; BAG36356.1; -; mRNA.
DR   EMBL; AY566253; AAS66982.1; -; Genomic_DNA.
DR   EMBL; BC050456; AAH50456.1; -; mRNA.
DR   CCDS; CCDS4049.1; -.
DR   PIR; A55710; TSHUP4.
DR   RefSeq; NP_001293141.1; NM_001306212.1.
DR   RefSeq; NP_001293142.1; NM_001306213.1.
DR   RefSeq; NP_001293143.1; NM_001306214.1.
DR   RefSeq; NP_003239.2; NM_003248.5.
DR   AlphaFoldDB; P35443; -.
DR   SMR; P35443; -.
DR   BioGRID; 112918; 5.
DR   ComplexPortal; CPX-1790; Thrombospondin 4 complex.
DR   IntAct; P35443; 5.
DR   STRING; 9606.ENSP00000339730; -.
DR   GlyCosmos; P35443; 5 sites, 3 glycans.
DR   GlyGen; P35443; 7 sites, 5 O-linked glycans (5 sites).
DR   iPTMnet; P35443; -.
DR   PhosphoSitePlus; P35443; -.
DR   BioMuta; THBS4; -.
DR   DMDM; 55977790; -.
DR   CPTAC; non-CPTAC-2703; -.
DR   jPOST; P35443; -.
DR   MassIVE; P35443; -.
DR   MaxQB; P35443; -.
DR   PaxDb; 9606-ENSP00000339730; -.
DR   PeptideAtlas; P35443; -.
DR   ProteomicsDB; 55063; -.
DR   Antibodypedia; 3891; 205 antibodies from 26 providers.
DR   DNASU; 7060; -.
DR   Ensembl; ENST00000350881.6; ENSP00000339730.2; ENSG00000113296.14.
DR   GeneID; 7060; -.
DR   KEGG; hsa:7060; -.
DR   MANE-Select; ENST00000350881.6; ENSP00000339730.2; NM_003248.6; NP_003239.2.
DR   UCSC; uc021yaw.2; human.
DR   AGR; HGNC:11788; -.
DR   CTD; 7060; -.
DR   DisGeNET; 7060; -.
DR   GeneCards; THBS4; -.
DR   HGNC; HGNC:11788; THBS4.
DR   HPA; ENSG00000113296; Tissue enhanced (adipose tissue, heart muscle, smooth muscle, tongue).
DR   MIM; 600715; gene.
DR   neXtProt; NX_P35443; -.
DR   OpenTargets; ENSG00000113296; -.
DR   PharmGKB; PA36500; -.
DR   VEuPathDB; HostDB:ENSG00000113296; -.
DR   eggNOG; ENOG502QRK8; Eukaryota.
DR   GeneTree; ENSGT00940000155227; -.
DR   InParanoid; P35443; -.
DR   OMA; DSNPCFQ; -.
DR   OrthoDB; 5345349at2759; -.
DR   PhylomeDB; P35443; -.
DR   TreeFam; TF324917; -.
DR   PathwayCommons; P35443; -.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   SignaLink; P35443; -.
DR   BioGRID-ORCS; 7060; 10 hits in 1146 CRISPR screens.
DR   ChiTaRS; THBS4; human.
DR   GeneWiki; THBS4; -.
DR   GenomeRNAi; 7060; -.
DR   Pharos; P35443; Tbio.
DR   PRO; PR:P35443; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P35443; Protein.
DR   Bgee; ENSG00000113296; Expressed in calcaneal tendon and 183 other cell types or tissues.
DR   ExpressionAtlas; P35443; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0051451; P:myoblast migration; IDA:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEP:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0034103; P:regulation of tissue remodeling; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd16080; TSP-4cc; 1.
DR   Gene3D; 1.20.5.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR024665; TSP/COMP_coiled-coil.
DR   InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF92; THROMBOSPONDIN-4; 1.
DR   Pfam; PF11598; COMP; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF02412; TSP_3; 6.
DR   Pfam; PF05735; TSP_C; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   Genevisible; P35443; HS.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Growth factor;
KW   Mitogen; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted;
KW   Signal; Tissue remodeling; Unfolded protein response.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..961
FT                   /note="Thrombospondin-4"
FT                   /id="PRO_0000035852"
FT   DOMAIN          27..192
FT                   /note="Laminin G-like"
FT   DOMAIN          286..325
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          326..363
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          379..419
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          420..462
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          463..495
FT                   /note="TSP type-3 1"
FT   REPEAT          496..531
FT                   /note="TSP type-3 2"
FT   REPEAT          532..554
FT                   /note="TSP type-3 3"
FT   REPEAT          555..590
FT                   /note="TSP type-3 4"
FT   REPEAT          591..613
FT                   /note="TSP type-3 5"
FT   REPEAT          614..651
FT                   /note="TSP type-3 6"
FT   REPEAT          652..691
FT                   /note="TSP type-3 7"
FT   REPEAT          692..727
FT                   /note="TSP type-3 8"
FT   DOMAIN          731..945
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT   REGION          579..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           562..564
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        585..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..672
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        612
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        941
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        258
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        261
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        290..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        295..310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        313..324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        330..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        335..350
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        353..377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        383..394
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        388..403
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        406..418
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        424..438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        432..448
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        450..461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        477..482
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        487..507
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        523..543
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        546..566
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        582..602
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        605..625
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        643..663
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        683..703
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        719..940
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VARIANT         55
FT                   /note="L -> Q (in dbSNP:rs17881847)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_019951"
FT   VARIANT         387
FT                   /note="A -> P (associated with a pro-atherogenic phenotype;
FT                   dbSNP:rs1866389)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:22011848, ECO:0000269|Ref.4"
FT                   /id="VAR_019952"
FT   VARIANT         420
FT                   /note="A -> V (in dbSNP:rs17882372)"
FT                   /evidence="ECO:0000269|PubMed:7852353,
FT                   ECO:0000269|PubMed:8350346, ECO:0000269|Ref.4"
FT                   /id="VAR_019953"
FT   VARIANT         646
FT                   /note="V -> I (in dbSNP:rs2229396)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_019954"
FT   VARIANT         737
FT                   /note="V -> I (in dbSNP:rs2229398)"
FT                   /id="VAR_052659"
FT   CONFLICT        96
FT                   /note="N -> S (in Ref. 1; no nucleotide entry and 2;
FT                   CAA79635)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="P -> A (in Ref. 1; no nucleotide entry and 2;
FT                   CAA79635)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        737
FT                   /note="V -> G (in Ref. 1; no nucleotide entry and 2;
FT                   CAA79635)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   961 AA;  105869 MW;  18F867AA5FFDA54B CRC64;
     MLAPRGAAVL LLHLVLQRWL AAGAQATPQV FDLLPSSSQR LNPGALLPVL TDPALNDLYV
     ISTFKLQTKS SATIFGLYSS TDNSKYFEFT VMGRLNKAIL RYLKNDGKVH LVVFNNLQLA
     DGRRHRILLR LSNLQRGAGS LELYLDCIQV DSVHNLPRAF AGPSQKPETI ELRTFQRKPQ
     DFLEELKLVV RGSLFQVASL QDCFLQQSEP LAATGTGDFN RQFLGQMTQL NQLLGEVKDL
     LRQQVKETSF LRNTIAECQA CGPLKFQSPT PSTVVPPAPP APPTRPPRRC DSNPCFRGVQ
     CTDSRDGFQC GPCPEGYTGN GITCIDVDEC KYHPCYPGVH CINLSPGFRC DACPVGFTGP
     MVQGVGISFA KSNKQVCTDI DECRNGACVP NSICVNTLGS YRCGPCKPGY TGDQIRGCKA
     ERNCRNPELN PCSVNAQCIE ERQGDVTCVC GVGWAGDGYI CGKDVDIDSY PDEELPCSAR
     NCKKDNCKYV PNSGQEDADR DGIGDACDED ADGDGILNEQ DNCVLIHNVD QRNSDKDIFG
     DACDNCLSVL NNDQKDTDGD GRGDACDDDM DGDGIKNILD NCPKFPNRDQ RDKDGDGVGD
     ACDSCPDVSN PNQSDVDNDL VGDSCDTNQD SDGDGHQDST DNCPTVINSA QLDTDKDGIG
     DECDDDDDND GIPDLVPPGP DNCRLVPNPA QEDSNSDGVG DICESDFDQD QVIDRIDVCP
     ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD
     FEGTFHVNTQ TDDDYAGFIF GYQDSSSFYV VMWKQTEQTY WQATPFRAVA EPGIQLKAVK
     SKTGPGEHLR NSLWHTGDTS DQVRLLWKDS RNVGWKDKVS YRWFLQHRPQ VGYIRVRFYE
     GSELVADSGV TIDTTMRGGR LGVFCFSQEN IIWSNLKYRC NDTIPEDFQE FQTQNFDRFD
     N
//