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Versican core protein (Chondroitin sulfate proteoglycan core protein 2) (Chondroitin sulfate proteoglycan 2) (Glial hyaluronate-binding protein) (GHAP) (Large fibroblast proteoglycan) (PG-M)

 CSPG2_HUMAN             Reviewed;        3396 AA.
P13611; P20754; Q13010; Q13189; Q15123; Q9UCL9; Q9UNW5;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
18-JUL-2018, entry version 216.
RecName: Full=Versican core protein;
AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
Short=Chondroitin sulfate proteoglycan 2;
AltName: Full=Glial hyaluronate-binding protein;
Short=GHAP;
AltName: Full=Large fibroblast proteoglycan;
AltName: Full=PG-M;
Flags: Precursor;
Name=VCAN; Synonyms=CSPG2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V1).
TISSUE=Placenta;
PubMed=2583089;
Zimmermann D.R., Ruoslahti E.;
"Multiple domains of the large fibroblast proteoglycan, versican.";
EMBO J. 8:2975-2981(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V2).
TISSUE=Glial tumor;
PubMed=7806529;
Dours-Zimmermann M.T., Zimmermann D.R.;
"A novel glycosaminoglycan attachment domain identified in two
alternative splice variants of human versican.";
J. Biol. Chem. 269:32992-32998(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM V0).
PubMed=7528742;
Naso M.F., Zimmermann D.R., Iozzo R.V.;
"Characterization of the complete genomic structure of the human
versican gene and functional analysis of its promoter.";
J. Biol. Chem. 269:32999-33008(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
TISSUE=Brain;
PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
"Expression of PG-M(V3), an alternatively spliced form of PG-M without
a chondroitin sulfate attachment in region in mouse and human
tissues.";
J. Biol. Chem. 270:3914-3918(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 208-1427; 2081-2372 AND 2897-3233
(ISOFORM V1).
PubMed=7921538; DOI=10.1016/0945-053X(94)90185-6;
Yao L.Y., Moody C., Schoenherr E., Wight T.N., Sandell L.J.;
"Identification of the proteoglycan versican in aorta and smooth
muscle cells by DNA sequence analysis, in situ hybridization and
immunohistochemistry.";
Matrix Biol. 14:213-225(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-347.
PubMed=1478664; DOI=10.1016/S0888-7543(05)80103-X;
Iozzo R.V., Naso M.F., Cannizzaro L.A., Wasmuth J.J., McPherson J.D.;
"Mapping of the versican proteoglycan gene (CSPG2) to the long arm of
human chromosome 5 (5q12-5q14).";
Genomics 14:845-851(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2709-3396.
TISSUE=Lung fibroblast;
PubMed=2820964;
Krusius T., Gehlsen K.R., Ruoslahti E.;
"A fibroblast chondroitin sulfate proteoglycan core protein contains
lectin-like and growth factor-like sequences.";
J. Biol. Chem. 262:13120-13125(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 3333-3396 (ISOFORM VINT).
TISSUE=Aortic smooth muscle;
PubMed=10397680; DOI=10.1161/01.ATV.19.7.1630;
Lemire J.M., Braun K.R., Maurel P., Kaplan E.D., Schwartz S.M.,
Wight T.N.;
"Versican/PG-M isoforms in vascular smooth muscle cells.";
Arterioscler. Thromb. Vasc. Biol. 19:1630-1639(1999).
[9]
PROTEIN SEQUENCE OF 21-37.
PubMed=1429726;
Perides G., Rahemtulla F., Lane W.S., Asher R.A., Bignami A.;
"Isolation of a large aggregating proteoglycan from human brain.";
J. Biol. Chem. 267:23883-23887(1992).
[10]
PROTEIN SEQUENCE OF 24-50; 80-119; 128-155; 167-218; 229-268 AND
277-290.
TISSUE=Brain;
PubMed=2466833;
Perides G., Lane W.S., Andrews D., Dahl D., Bignami A.;
"Isolation and partial characterization of a glial hyaluronate-binding
protein.";
J. Biol. Chem. 264:5981-5987(1989).
[11]
PROTEIN SEQUENCE OF 171-210 AND 289-303.
PubMed=2469524; DOI=10.1016/0361-9230(89)90129-9;
Bignami A., Lane W.S., Andrews D., Dahl D.;
"Structural similarity of hyaluronate binding proteins in brain and
cartilage.";
Brain Res. Bull. 22:67-70(1989).
[12]
TISSUE SPECIFICITY (ISOFORMS V0; V1; V2 AND V3).
PubMed=8627343;
Paulus W., Baur I., Dours-Zimmermann M.T., Zimmermann D.R.;
"Differential expression of versican isoforms in brain tumors.";
J. Neuropathol. Exp. Neurol. 55:528-533(1996).
[13]
INVOLVEMENT IN WGVRP.
PubMed=16043844; DOI=10.1167/iovs.05-0057;
Miyamoto T., Inoue H., Sakamoto Y., Kudo E., Naito T., Mikawa T.,
Mikawa Y., Isashiki Y., Osabe D., Shinohara S., Shiota H., Itakura M.;
"Identification of a novel splice site mutation of the CSPG2 gene in a
Japanese family with Wagner syndrome.";
Invest. Ophthalmol. Vis. Sci. 46:2726-2735(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INVOLVEMENT IN WGVRP, AND PATHOLOGICAL MECHANISM.
PubMed=22739342; DOI=10.1038/ejhg.2012.137;
Kloeckener-Gruissem B., Neidhardt J., Magyar I., Plauchu H.,
Zech J.C., Morle L., Palmer-Smith S.M., Macdonald M.J., Nas V.,
Fry A.E., Berger W.;
"Novel VCAN mutations and evidence for unbalanced alternative splicing
in the pathogenesis of Wagner syndrome.";
Eur. J. Hum. Genet. 21:352-356(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2116 AND THR-2617, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
PHOSPHORYLATION AT SER-2116.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: May play a role in intercellular signaling and in
connecting cells with the extracellular matrix. May take part in
the regulation of cell motility, growth and differentiation. Binds
hyaluronic acid.
-!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
-!- INTERACTION:
P14780:MMP9; NbExp=3; IntAct=EBI-8515977, EBI-1382326;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=V0;
IsoId=P13611-1; Sequence=Displayed;
Name=V1;
IsoId=P13611-2; Sequence=VSP_003082, VSP_003083;
Name=V2;
IsoId=P13611-3; Sequence=VSP_003084;
Name=V3;
IsoId=P13611-4; Sequence=VSP_003082, VSP_003085;
Name=Vint;
IsoId=P13611-5; Sequence=VSP_003086;
-!- TISSUE SPECIFICITY: Cerebral white matter and plasma. Isoform V0
and isoform V1 are expressed in normal brain, gliomas,
medulloblastomas, schwannomas, neurofibromas, and meningiomas.
Isoform V2 is restricted to normal brain and gliomas. Isoform V3
is found in all these tissues except medulloblastomas.
-!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- DISEASE: Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare
vitreoretinopathy characterized by an optically empty vitreous
cavity with fibrillary condensations and a preretinal avascular
membrane. Other optical features include progressive chorioretinal
atrophy, perivascular sheating, subcapsular cataract and myopia.
{ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. The pathological mechanism involves a
quantitave imbalance of the normally occurring splice variants
(PubMed:22739342). {ECO:0000269|PubMed:22739342}.
-!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Versican;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_214";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/VCANID40173ch5q14.html";
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EMBL; X15998; CAA34128.1; -; mRNA.
EMBL; U16306; AAA65018.1; -; mRNA.
EMBL; U26555; AAA67565.1; -; mRNA.
EMBL; D32039; BAA06801.1; -; mRNA.
EMBL; S52488; AAB24878.1; -; Genomic_DNA.
EMBL; J02814; AAA36437.1; -; mRNA.
EMBL; AF084545; AAD48545.1; -; mRNA.
CCDS; CCDS4060.1; -. [P13611-1]
CCDS; CCDS47242.1; -. [P13611-4]
CCDS; CCDS54875.1; -. [P13611-3]
CCDS; CCDS54876.1; -. [P13611-2]
PIR; S06014; A60979.
RefSeq; NP_001119808.1; NM_001126336.2. [P13611-4]
RefSeq; NP_001157569.1; NM_001164097.1. [P13611-2]
RefSeq; NP_001157570.1; NM_001164098.1. [P13611-3]
RefSeq; NP_004376.2; NM_004385.4. [P13611-1]
UniGene; Hs.643801; -.
ProteinModelPortal; P13611; -.
SMR; P13611; -.
BioGrid; 107844; 19.
IntAct; P13611; 6.
MINT; P13611; -.
STRING; 9606.ENSP00000265077; -.
DrugBank; DB08818; Hyaluronic acid.
CarbonylDB; P13611; -.
iPTMnet; P13611; -.
PhosphoSitePlus; P13611; -.
SwissPalm; P13611; -.
BioMuta; VCAN; -.
DMDM; 2506816; -.
EPD; P13611; -.
MaxQB; P13611; -.
PaxDb; P13611; -.
PeptideAtlas; P13611; -.
PRIDE; P13611; -.
ProteomicsDB; 52938; -.
ProteomicsDB; 52939; -. [P13611-2]
ProteomicsDB; 52940; -. [P13611-3]
ProteomicsDB; 52941; -. [P13611-4]
ProteomicsDB; 52942; -. [P13611-5]
DNASU; 1462; -.
Ensembl; ENST00000265077; ENSP00000265077; ENSG00000038427. [P13611-1]
Ensembl; ENST00000342785; ENSP00000342768; ENSG00000038427. [P13611-3]
Ensembl; ENST00000343200; ENSP00000340062; ENSG00000038427. [P13611-2]
Ensembl; ENST00000502527; ENSP00000421362; ENSG00000038427. [P13611-4]
GeneID; 1462; -.
KEGG; hsa:1462; -.
UCSC; uc003kii.4; human. [P13611-1]
CTD; 1462; -.
DisGeNET; 1462; -.
EuPathDB; HostDB:ENSG00000038427.15; -.
GeneCards; VCAN; -.
GeneReviews; VCAN; -.
HGNC; HGNC:2464; VCAN.
HPA; CAB008979; -.
HPA; HPA004726; -.
MalaCards; VCAN; -.
MIM; 118661; gene.
MIM; 143200; phenotype.
neXtProt; NX_P13611; -.
OpenTargets; ENSG00000038427; -.
Orphanet; 898; Wagner disease.
PharmGKB; PA162408788; -.
eggNOG; ENOG410IFXS; Eukaryota.
eggNOG; ENOG410ZPDG; LUCA.
GeneTree; ENSGT00760000119025; -.
HOVERGEN; HBG051140; -.
InParanoid; P13611; -.
KO; K06793; -.
OMA; REYFTTS; -.
OrthoDB; EOG091G0CY8; -.
PhylomeDB; P13611; -.
TreeFam; TF332134; -.
Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
Reactome; R-HSA-2024101; CS/DS degradation.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P13611; -.
ChiTaRS; VCAN; human.
GeneWiki; Versican; -.
GenomeRNAi; 1462; -.
PMAP-CutDB; P13611; -.
PRO; PR:P13611; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000038427; -.
CleanEx; HS_VCAN; -.
ExpressionAtlas; P13611; baseline and differential.
Genevisible; P13611; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; HDA:BHF-UCL.
GO; GO:0005539; F:glycosaminoglycan binding; TAS:ProtInc.
GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0008037; P:cell recognition; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome.
GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0008347; P:glial cell migration; IDA:BHF-UCL.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
CDD; cd00033; CCP; 1.
CDD; cd03588; CLECT_CSPGs; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.100.10; -; 3.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033987; CSPG_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR000538; Link_dom.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00008; EGF; 2.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 1.
Pfam; PF07686; V-set; 1.
Pfam; PF00193; Xlink; 2.
PRINTS; PR01265; LINKMODULE.
SMART; SM00032; CCP; 1.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00409; IG; 1.
SMART; SM00445; LINK; 2.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56436; SSF56436; 3.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS01241; LINK_1; 2.
PROSITE; PS50963; LINK_2; 2.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cataract; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Extracellular matrix; Glycoprotein; Hyaluronic acid;
Immunoglobulin domain; Lectin; Phosphoprotein; Polymorphism;
Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 20 {ECO:0000269|PubMed:1429726}.
CHAIN 21 3396 Versican core protein.
/FTId=PRO_0000017522.
DOMAIN 21 146 Ig-like V-type.
DOMAIN 150 245 Link 1. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 251 347 Link 2. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 3089 3125 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3127 3163 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 3176 3290 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 3294 3354 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 348 1335 GAG-alpha (glucosaminoglycan attachment
domain).
REGION 1336 3089 GAG-beta.
MOD_RES 2116 2116 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 2608 2608 Phosphoserine.
{ECO:0000250|UniProtKB:Q62059}.
MOD_RES 2617 2617 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 809 809 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1332 1332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1398 1398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1442 1442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1468 1468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1663 1663 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1898 1898 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2179 2179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2272 2272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2280 2280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2360 2360 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2385 2385 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2392 2392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2496 2496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2628 2628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2934 2934 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3067 3067 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3369 3369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3379 3379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 130 {ECO:0000250}.
DISULFID 172 243 {ECO:0000250}.
DISULFID 196 217 {ECO:0000250}.
DISULFID 270 345 {ECO:0000250}.
DISULFID 294 315 {ECO:0000250}.
DISULFID 3093 3104 {ECO:0000250}.
DISULFID 3098 3113 {ECO:0000250}.
DISULFID 3115 3124 {ECO:0000250}.
DISULFID 3131 3142 {ECO:0000250}.
DISULFID 3136 3151 {ECO:0000250}.
DISULFID 3153 3162 {ECO:0000250}.
DISULFID 3169 3180 {ECO:0000250}.
DISULFID 3197 3289 {ECO:0000250}.
DISULFID 3265 3281 {ECO:0000250}.
DISULFID 3296 3339 {ECO:0000250}.
DISULFID 3325 3352 {ECO:0000250}.
VAR_SEQ 348 348 P -> R (in isoform V1 and isoform V3).
{ECO:0000303|PubMed:2583089,
ECO:0000303|PubMed:7876137,
ECO:0000303|PubMed:7921538}.
/FTId=VSP_003082.
VAR_SEQ 349 3089 Missing (in isoform V3).
{ECO:0000303|PubMed:7876137}.
/FTId=VSP_003085.
VAR_SEQ 349 1335 Missing (in isoform V1).
{ECO:0000303|PubMed:2583089,
ECO:0000303|PubMed:7921538}.
/FTId=VSP_003083.
VAR_SEQ 1336 3089 Missing (in isoform V2).
{ECO:0000303|PubMed:7806529}.
/FTId=VSP_003084.
VAR_SEQ 3355 3396 PSAYQRTYSMKYFKNSSSAKDNSINTSKHDHRWSRRWQESR
R -> RKWSFRKNGLPCYNNY (in isoform Vint).
{ECO:0000303|PubMed:10397680}.
/FTId=VSP_003086.
VARIANT 300 300 S -> L (in dbSNP:rs2652098).
/FTId=VAR_021958.
VARIANT 428 428 G -> D (in dbSNP:rs2287926).
/FTId=VAR_020214.
VARIANT 1516 1516 K -> R (in dbSNP:rs309559).
/FTId=VAR_021959.
VARIANT 1826 1826 R -> H (in dbSNP:rs188703).
/FTId=VAR_031632.
VARIANT 2301 2301 F -> Y (in dbSNP:rs160278).
/FTId=VAR_020215.
VARIANT 2315 2315 V -> L (in dbSNP:rs3734094).
/FTId=VAR_020216.
VARIANT 2937 2937 D -> Y (in dbSNP:rs160277).
/FTId=VAR_021960.
VARIANT 3011 3011 N -> K (in dbSNP:rs16900532).
/FTId=VAR_031633.
CONFLICT 88 88 N -> D (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 260 260 K -> I (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 274 274 D -> A (in Ref. 4; BAA06801).
{ECO:0000305}.
CONFLICT 284 284 Q -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 2709 2713 IKAEA -> EFREV (in Ref. 7; AAA36437).
{ECO:0000305}.
SEQUENCE 3396 AA; 372820 MW; D174A1BBB8304FEC CRC64;
MFINIKSILW MCSTLIVTHA LHKVKVGKSP PVRGSLSGKV SLPCHFSTMP TLPPSYNTSE
FLRIKWSKIE VDKNGKDLKE TTVLVAQNGN IKIGQDYKGR VSVPTHPEAV GDASLTVVKL
LASDAGLYRC DVMYGIEDTQ DTVSLTVDGV VFHYRAATSR YTLNFEAAQK ACLDVGAVIA
TPEQLFAAYE DGFEQCDAGW LADQTVRYPI RAPRVGCYGD KMGKAGVRTY GFRSPQETYD
VYCYVDHLDG DVFHLTVPSK FTFEEAAKEC ENQDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKE ATTIDLSILA
ETASPSLSKE PQMVSDRTTP IIPLVDELPV IPTEFPPVGN IVSFEQKATV QPQAITDSLA
TKLPTPTGST KKPWDMDDYS PSASGPLGKL DISEIKEEVL QSTTGVSHYA TDSWDGVVED
KQTQESVTQI EQIEVGPLVT SMEILKHIPS KEFPVTETPL VTARMILESK TEKKMVSTVS
ELVTTGHYGF TLGEEDDEDR TLTVGSDEST LIFDQIPEVI TVSKTSEDTI HTHLEDLESV
SASTTVSPLI MPDNNGSSMD DWEERQTSGR ITEEFLGKYL STTPFPSQHR TEIELFPYSG
DKILVEGIST VIYPSLQTEM THRRERTETL IPEMRTDTYT DEIQEEITKS PFMGKTEEEV
FSGMKLSTSL SEPIHVTESS VEMTKSFDFP TLITKLSAEP TEVRDMEEDF TATPGTTKYD
ENITTVLLAH GTLSVEAATV SKWSWDEDNT TSKPLESTEP SASSKLPPAL LTTVGMNGKD
KDIPSFTEDG ADEFTLIPDS TQKQLEEVTD EDIAAHGKFT IRFQPTTSTG IAEKSTLRDS
TTEEKVPPIT STEGQVYATM EGSALGEVED VDLSKPVSTV PQFAHTSEVE GLAFVSYSST
QEPTTYVDSS HTIPLSVIPK TDWGVLVPSV PSEDEVLGEP SQDILVIDQT RLEATISPET
MRTTKITEGT TQEEFPWKEQ TAEKPVPALS STAWTPKEAV TPLDEQEGDG SAYTVSEDEL
LTGSERVPVL ETTPVGKIDH SVSYPPGAVT EHKVKTDEVV TLTPRIGPKV SLSPGPEQKY
ETEGSSTTGF TSSLSPFSTH ITQLMEETTT EKTSLEDIDL GSGLFEKPKA TELIEFSTIK
VTVPSDITTA FSSVDRLHTT SAFKPSSAIT KKPPLIDREP GEETTSDMVI IGESTSHVPP
TTLEDIVAKE TETDIDREYF TTSSPPATQP TRPPTVEDKE AFGPQALSTP QPPASTKFHP
DINVYIIEVR ENKTGRMSDL SVIGHPIDSE SKEDEPCSEE TDPVHDLMAE ILPEFPDIIE
IDLYHSEENE EEEEECANAT DVTTTPSVQY INGKHLVTTV PKDPEAAEAR RGQFESVAPS
QNFSDSSESD THPFVIAKTE LSTAVQPNES TETTESLEVT WKPETYPETS EHFSGGEPDV
FPTVPFHEEF ESGTAKKGAE SVTERDTEVG HQAHEHTEPV SLFPEESSGE IAIDQESQKI
AFARATEVTF GEEVEKSTSV TYTPTIVPSS ASAYVSEEEA VTLIGNPWPD DLLSTKESWV
EATPRQVVEL SGSSSIPITE GSGEAEEDED TMFTMVTDLS QRNTTDTLIT LDTSRIITES
FFEVPATTIY PVSEQPSAKV VPTKFVSETD TSEWISSTTV EEKKRKEEEG TTGTASTFEV
YSSTQRSDQL ILPFELESPN VATSSDSGTR KSFMSLTTPT QSEREMTDST PVFTETNTLE
NLGAQTTEHS SIHQPGVQEG LTTLPRSPAS VFMEQGSGEA AADPETTTVS SFSLNVEYAI
QAEKEVAGTL SPHVETTFST EPTGLVLSTV MDRVVAENIT QTSREIVISE RLGEPNYGAE
IRGFSTGFPL EEDFSGDFRE YSTVSHPIAK EETVMMEGSG DAAFRDTQTS PSTVPTSVHI
SHISDSEGPS STMVSTSAFP WEEFTSSAEG SGEQLVTVSS SVVPVLPSAV QKFSGTASSI
IDEGLGEVGT VNEIDRRSTI LPTAEVEGTK APVEKEEVKV SGTVSTNFPQ TIEPAKLWSR
QEVNPVRQEI ESETTSEEQI QEEKSFESPQ NSPATEQTIF DSQTFTETEL KTTDYSVLTT
KKTYSDDKEM KEEDTSLVNM STPDPDANGL ESYTTLPEAT EKSHFFLATA LVTESIPAEH
VVTDSPIKKE ESTKHFPKGM RPTIQESDTE LLFSGLGSGE EVLPTLPTES VNFTEVEQIN
NTLYPHTSQV ESTSSDKIED FNRMENVAKE VGPLVSQTDI FEGSGSVTST TLIEILSDTG
AEGPTVAPLP FSTDIGHPQN QTVRWAEEIQ TSRPQTITEQ DSNKNSSTAE INETTTSSTD
FLARAYGFEM AKEFVTSAPK PSDLYYEPSG EGSGEVDIVD SFHTSATTQA TRQESSTTFV
SDGSLEKHPE VPSAKAVTAD GFPTVSVMLP LHSEQNKSSP DPTSTLSNTV SYERSTDGSF
QDRFREFEDS TLKPNRKKPT ENIIIDLDKE DKDLILTITE STILEILPEL TSDKNTIIDI
DHTKPVYEDI LGMQTDIDTE VPSEPHDSND ESNDDSTQVQ EIYEAAVNLS LTEETFEGSA
DVLASYTQAT HDESMTYEDR SQLDHMGFHF TTGIPAPSTE TELDVLLPTA TSLPIPRKSA
TVIPEIEGIK AEAKALDDMF ESSTLSDGQA IADQSEIIPT LGQFERTQEE YEDKKHAGPS
FQPEFSSGAE EALVDHTPYL SIATTHLMDQ SVTEVPDVME GSNPPYYTDT TLAVSTFAKL
SSQTPSSPLT IYSGSEASGH TEIPQPSALP GIDVGSSVMS PQDSFKEIHV NIEATFKPSS
EEYLHITEPP SLSPDTKLEP SEDDGKPELL EEMEASPTEL IAVEGTEILQ DFQNKTDGQV
SGEAIKMFPT IKTPEAGTVI TTADEIELEG ATQWPHSTSA SATYGVEAGV VPWLSPQTSE
RPTLSSSPEI NPETQAALIR GQDSTIAASE QQVAARILDS NDQATVNPVE FNTEVATPPF
SLLETSNETD FLIGINEESV EGTAIYLPGP DRCKMNPCLN GGTCYPTETS YVCTCVPGYS
GDQCELDFDE CHSNPCRNGA TCVDGFNTFR CLCLPSYVGA LCEQDTETCD YGWHKFQGQC
YKYFAHRRTW DAAERECRLQ GAHLTSILSH EEQMFVNRVG HDYQWIGLND KMFEHDFRWT
DGSTLQYENW RPNQPDSFFS AGEDCVVIIW HENGQWNDVP CNYHLTYTCK KGTVACGQPP
VVENAKTFGK MKPRYEINSL IRYHCKDGFI QRHLPTIRCL GNGRWAIPKI TCMNPSAYQR
TYSMKYFKNS SSAKDNSINT SKHDHRWSRR WQESRR


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