THS7A_HUMAN
ID THS7A_HUMAN Reviewed; 1657 AA.
AC Q9UPZ6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7A;
DE Contains:
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7A, soluble form;
DE Flags: Precursor;
GN Name=THSD7A; Synonyms=KIAA0960;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-933.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-1657.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP DISEASE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=25394321; DOI=10.1056/nejmoa1409354;
RA Tomas N.M., Beck L.H. Jr., Meyer-Schwesinger C., Seitz-Polski B., Ma H.,
RA Zahner G., Dolla G., Hoxha E., Helmchen U., Dabert-Gay A.S., Debayle D.,
RA Merchant M., Klein J., Salant D.J., Stahl R.A.K., Lambeau G.;
RT "Thrombospondin type-1 domain-containing 7A in idiopathic membranous
RT nephropathy.";
RL N. Engl. J. Med. 371:2277-2287(2014).
RN [6]
RP FUNCTION (THROMBOSPONDIN TYPE-1 DOMAIN-CONTAINING PROTEIN 7A, SOLUBLE
RP FORM), PROTEOLYTIC CLEAVAGE, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=22194972; DOI=10.1371/journal.pone.0029000;
RA Kuo M.W., Wang C.H., Wu H.C., Chang S.J., Chuang Y.J.;
RT "Soluble THSD7A is an N-glycoprotein that promotes endothelial cell
RT migration and tube formation in angiogenesis.";
RL PLoS ONE 6:E29000-E29000(2011).
RN [7]
RP FUNCTION (THROMBOSPONDIN TYPE-1 DOMAIN-CONTAINING PROTEIN 7A), AND
RP SUBCELLULAR LOCATION.
RX PubMed=27214550; DOI=10.1172/jci85265;
RA Tomas N.M., Hoxha E., Reinicke A.T., Fester L., Helmchen U., Gerth J.,
RA Bachmann F., Budde K., Koch-Nolte F., Zahner G., Rune G., Lambeau G.,
RA Meyer-Schwesinger C., Stahl R.A.;
RT "Autoantibodies against thrombospondin type 1 domain-containing 7A induce
RT membranous nephropathy.";
RL J. Clin. Invest. 126:2519-2532(2016).
RN [8]
RP DOMAIN, DISEASE, AND GLYCOSYLATION.
RX PubMed=29555830; DOI=10.1681/asn.2017070805;
RA Seifert L., Hoxha E., Eichhoff A.M., Zahner G., Dehde S., Reinhard L.,
RA Koch-Nolte F., Stahl R.A.K., Tomas N.M.;
RT "The Most N-Terminal Region of THSD7A Is the Predominant Target for
RT Autoimmunity in THSD7A-Associated Membranous Nephropathy.";
RL J. Am. Soc. Nephrol. 29:1536-1548(2018).
RN [9]
RP ANALYSIS OF TSP TYPE-1 DOMAINS.
RX PubMed=30520531; DOI=10.1002/prot.25640;
RA Stoddard S.V., Welsh C.L., Palopoli M.M., Stoddard S.D., Aramandla M.P.,
RA Patel R.M., Ma H., Beck L.H. Jr.;
RT "Structure and function insights garnered from in silico modeling of the
RT thrombospondin type-1 domain-containing 7A antigen.";
RL Proteins 87:136-145(2019).
CC -!- FUNCTION: [Thrombospondin type-1 domain-containing protein 7A]: Plays a
CC role in actin cytoskeleton rearrangement.
CC {ECO:0000269|PubMed:27214550}.
CC -!- FUNCTION: [Thrombospondin type-1 domain-containing protein 7A, soluble
CC form]: The soluble form promotes endothelial cell migration and
CC filopodia formation during sprouting angiogenesis via a FAK-dependent
CC mechanism. {ECO:0000269|PubMed:22194972}.
CC -!- INTERACTION:
CC Q9UPZ6; Q13520: AQP6; NbExp=3; IntAct=EBI-310962, EBI-13059134;
CC Q9UPZ6; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-310962, EBI-11343438;
CC Q9UPZ6; P20138: CD33; NbExp=3; IntAct=EBI-310962, EBI-3906571;
CC Q9UPZ6; P21964: COMT; NbExp=3; IntAct=EBI-310962, EBI-372265;
CC Q9UPZ6; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-310962, EBI-11037623;
CC Q9UPZ6; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-310962, EBI-712073;
CC Q9UPZ6; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-310962, EBI-18053395;
CC Q9UPZ6; Q86WI0: LHFPL1; NbExp=3; IntAct=EBI-310962, EBI-18268016;
CC Q9UPZ6; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-310962, EBI-10329546;
CC Q9UPZ6; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-310962, EBI-17247926;
CC Q9UPZ6; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-310962, EBI-2820477;
CC Q9UPZ6; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-310962, EBI-1055364;
CC -!- SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein
CC 7A]: Cell membrane {ECO:0000269|PubMed:22194972,
CC ECO:0000269|PubMed:25394321, ECO:0000269|PubMed:27214550}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:22194972}. Cell projection
CC {ECO:0000250|UniProtKB:Q69ZU6}. Note=Detected on podocyte foot
CC processes. {ECO:0000250|UniProtKB:Q69ZU6}.
CC -!- SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein
CC 7A, soluble form]: Secreted {ECO:0000269|PubMed:22194972}.
CC Note=Proteolytic cleavage in the extracellular region generates a 210
CC kDa soluble form. {ECO:0000269|PubMed:22194972}.
CC -!- TISSUE SPECIFICITY: Detected on kidney podocytes along the glomerular
CC capillary wall (at protein level). {ECO:0000269|PubMed:25394321}.
CC -!- DOMAIN: Sequence analysis combined with the expression of constructs
CC corresponding each to two or three adjacent TSP type-1 domains suggests
CC the presence of 21 TSP type-1 domains; not all of these are detected by
CC standard bioinformatic tools. {ECO:0000303|PubMed:29555830,
CC ECO:0000303|PubMed:30520531}.
CC -!- PTM: Proteolytic cleavage in the extracellular region generates a 210
CC kDa soluble form. {ECO:0000269|PubMed:22194972}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:22194972,
CC ECO:0000269|PubMed:25394321, ECO:0000269|PubMed:29555830}.
CC -!- DISEASE: Note=Autoantibodies against THSD7A have been detected in serum
CC and glomeruli from patients with idiopathic membranous nephropathy
CC (PubMed:25394321). The majority of the autoantibodies react with the
CC two most N-terminal TSP type-1 domains (PubMed:29555830).
CC {ECO:0000269|PubMed:25394321, ECO:0000269|PubMed:29555830}.
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DR EMBL; AC004141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK092252; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB023177; BAA76804.2; -; mRNA.
DR CCDS; CCDS47543.1; -.
DR RefSeq; NP_056019.1; NM_015204.2.
DR AlphaFoldDB; Q9UPZ6; -.
DR BioGRID; 128774; 22.
DR IntAct; Q9UPZ6; 16.
DR MINT; Q9UPZ6; -.
DR STRING; 9606.ENSP00000406482; -.
DR CarbonylDB; Q9UPZ6; -.
DR GlyGen; Q9UPZ6; 14 sites.
DR iPTMnet; Q9UPZ6; -.
DR PhosphoSitePlus; Q9UPZ6; -.
DR BioMuta; THSD7A; -.
DR DMDM; 296453024; -.
DR MassIVE; Q9UPZ6; -.
DR MaxQB; Q9UPZ6; -.
DR PaxDb; Q9UPZ6; -.
DR PeptideAtlas; Q9UPZ6; -.
DR PRIDE; Q9UPZ6; -.
DR ProteomicsDB; 85479; -.
DR Antibodypedia; 626; 38 antibodies from 10 providers.
DR DNASU; 221981; -.
DR Ensembl; ENST00000423059.9; ENSP00000406482.2; ENSG00000005108.17.
DR GeneID; 221981; -.
DR KEGG; hsa:221981; -.
DR MANE-Select; ENST00000423059.9; ENSP00000406482.2; NM_015204.3; NP_056019.1.
DR UCSC; uc064bok.1; human.
DR CTD; 221981; -.
DR DisGeNET; 221981; -.
DR GeneCards; THSD7A; -.
DR HGNC; HGNC:22207; THSD7A.
DR HPA; ENSG00000005108; Tissue enhanced (kidney).
DR MIM; 612249; gene.
DR neXtProt; NX_Q9UPZ6; -.
DR OpenTargets; ENSG00000005108; -.
DR PharmGKB; PA162405715; -.
DR VEuPathDB; HostDB:ENSG00000005108; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000155427; -.
DR HOGENOM; CLU_004819_0_0_1; -.
DR InParanoid; Q9UPZ6; -.
DR OMA; SCNPPCT; -.
DR OrthoDB; 20284at2759; -.
DR PhylomeDB; Q9UPZ6; -.
DR TreeFam; TF329791; -.
DR PathwayCommons; Q9UPZ6; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9UPZ6; -.
DR BioGRID-ORCS; 221981; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; THSD7A; human.
DR GenomeRNAi; 221981; -.
DR Pharos; Q9UPZ6; Tbio.
DR PRO; PR:Q9UPZ6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UPZ6; protein.
DR Bgee; ENSG00000005108; Expressed in decidua and 181 other tissues.
DR ExpressionAtlas; Q9UPZ6; baseline and differential.
DR Genevisible; Q9UPZ6; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 12.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF19028; TSP1_spondin; 4.
DR Pfam; PF00090; TSP_1; 6.
DR SMART; SM00209; TSP1; 16.
DR SUPFAM; SSF82895; SSF82895; 13.
DR PROSITE; PS50092; TSP1; 11.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Cell projection; Coiled coil; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..1657
FT /note="Thrombospondin type-1 domain-containing protein 7A"
FT /id="PRO_0000256126"
FT CHAIN 48..?
FT /note="Thrombospondin type-1 domain-containing protein 7A,
FT soluble form"
FT /id="PRO_0000444430"
FT TOPO_DOM 48..1607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1608..1628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1629..1657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..116
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 120..192
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255"
FT DOMAIN 194..247
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 360..416
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 423..510
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 512..574
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 634..695
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 696..769
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 771..831
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 832..904
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255"
FT DOMAIN 906..959
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 960..1033
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1035..1095
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1096..1163
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255"
FT DOMAIN 1166..1220
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255"
FT DOMAIN 1221..1284
FT /note="TSP type-1 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1286..1341
FT /note="TSP type-1 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1342..1412
FT /note="TSP type-1 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1414..1475
FT /note="TSP type-1 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 265..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 267..315
FT /evidence="ECO:0000255"
FT COMPBIAS 277..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 435..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 455..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 466..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 635..677
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 646..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 689..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 707..764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 728..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 739..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 772..814
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 783..787
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 824..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 972..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 994..1032
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1005..1018
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1036..1073
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1047..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1090..1094
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1213..1219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1232..1279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1240..1283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1251..1264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1287..1325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1298..1302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1335..1340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1351..1407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1358..1411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1369..1388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1415..1459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1426..1430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1469..1474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VARIANT 238
FT /note="F -> L (in dbSNP:rs2074599)"
FT /id="VAR_057366"
FT VARIANT 583
FT /note="N -> H (in dbSNP:rs47)"
FT /id="VAR_068676"
FT VARIANT 771
FT /note="D -> E (in dbSNP:rs2285744)"
FT /id="VAR_057367"
FT VARIANT 906
FT /note="D -> E (in dbSNP:rs1432)"
FT /id="VAR_068677"
FT VARIANT 1652
FT /note="D -> E (in dbSNP:rs56264449)"
FT /id="VAR_068678"
FT CONFLICT 131
FT /note="Q -> R (in Ref. 2; AK092252)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="N -> D (in Ref. 3; BAA76804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1657 AA; 185363 MW; 4CF0FC4EDA26E516 CRC64;
MGLQARRWAS GSRGAAGPRR GVLQLLPLPL PLPLLLLLLL RPGAGRAAAQ GEAEAPTLYL
WKTGPWGRCM GDECGPGGIQ TRAVWCAHVE GWTTLHTNCK QAERPNNQQN CFKVCDWHKE
LYDWRLGPWN QCQPVISKSL EKPLECIKGE EGIQVREIAC IQKDKDIPAE DIICEYFEPK
PLLEQACLIP CQQDCIVSEF SAWSECSKTC GSGLQHRTRH VVAPPQFGGS GCPNLTEFQV
CQSSPCEAEE LRYSLHVGPW STCSMPHSRQ VRQARRRGKN KEREKDRSKG VKDPEARELI
KKKRNRNRQN RQENKYWDIQ IGYQTREVMC INKTGKAADL SFCQQEKLPM TFQSCVITKE
CQVSEWSEWS PCSKTCHDMV SPAGTRVRTR TIRQFPIGSE KECPEFEEKE PCLSQGDGVV
PCATYGWRTT EWTECRVDPL LSQQDKRRGN QTALCGGGIQ TREVYCVQAN ENLLSQLSTH
KNKEASKPMD LKLCTGPIPN TTQLCHIPCP TECEVSPWSA WGPCTYENCN DQQGKKGFKL
RKRRITNEPT GGSGVTGNCP HLLEAIPCEE PACYDWKAVR LGNCEPDNGK ECGPGTQVQE
VVCINSDGEE VDRQLCRDAI FPIPVACDAP CPKDCVLSTW STWSSCSHTC SGKTTEGKQI
RARSILAYAG EEGGIRCPNS SALQEVRSCN EHPCTVYHWQ TGPWGQCIED TSVSSFNTTT
TWNGEASCSV GMQTRKVICV RVNVGQVGPK KCPESLRPET VRPCLLPCKK DCIVTPYSDW
TSCPSSCKEG DSSIRKQSRH RVIIQLPANG GRDCTDPLYE EKACEAPQAC QSYRWKTHKW
RRCQLVPWSV QQDSPGAQEG CGPGRQARAI TCRKQDGGQA GIHECLQYAG PVPALTQACQ
IPCQDDCQLT SWSKFSSCNG DCGAVRTRKR TLVGKSKKKE KCKNSHLYPL IETQYCPCDK
YNAQPVGNWS DCILPEGKVE VLLGMKVQGD IKECGQGYRY QAMACYDQNG RLVETSRCNS
HGYIEEACII PCPSDCKLSE WSNWSRCSKS CGSGVKVRSK WLREKPYNGG RPCPKLDHVN
QAQVYEVVPC HSDCNQYLWV TEPWSICKVT FVNMRENCGE GVQTRKVRCM QNTADGPSEH
VEDYLCDPEE MPLGSRVCKL PCPEDCVISE WGPWTQCVLP CNQSSFRQRS ADPIRQPADE
GRSCPNAVEK EPCNLNKNCY HYDYNVTDWS TCQLSEKAVC GNGIKTRMLD CVRSDGKSVD
LKYCEALGLE KNWQMNTSCM VECPVNCQLS DWSPWSECSQ TCGLTGKMIR RRTVTQPFQG
DGRPCPSLMD QSKPCPVKPC YRWQYGQWSP CQVQEAQCGE GTRTRNISCV VSDGSADDFS
KVVDEEFCAD IELIIDGNKN MVLEESCSQP CPGDCYLKDW SSWSLCQLTC VNGEDLGFGG
IQVRSRPVII QELENQHLCP EQMLETKSCY DGQCYEYKWM ASAWKGSSRT VWCQRSDGIN
VTGGCLVMSQ PDADRSCNPP CSQPHSYCSE TKTCHCEEGY TEVMSSNSTL EQCTLIPVVV
LPTMEDKRGD VKTSRAVHPT QPSSNPAGRG RTWFLQPFGP DGRLKTWVYG VAAGAFVLLI
FIVSMIYLAC KKPKKPQRRQ NNRLKPLTLA YDGDADM
