GenomeNet

Database: UniProt
Entry: P13611
LinkDB: P13611
Original site: P13611 
ID   CSPG2_HUMAN             Reviewed;        3396 AA.
AC   P13611; P20754; Q13010; Q13189; Q15123; Q9UCL9; Q9UNW5;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   13-FEB-2019, entry version 222.
DE   RecName: Full=Versican core protein;
DE   AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE            Short=Chondroitin sulfate proteoglycan 2;
DE   AltName: Full=Glial hyaluronate-binding protein;
DE            Short=GHAP;
DE   AltName: Full=Large fibroblast proteoglycan;
DE   AltName: Full=PG-M;
DE   Flags: Precursor;
GN   Name=VCAN; Synonyms=CSPG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V1).
RC   TISSUE=Placenta;
RX   PubMed=2583089;
RA   Zimmermann D.R., Ruoslahti E.;
RT   "Multiple domains of the large fibroblast proteoglycan, versican.";
RL   EMBO J. 8:2975-2981(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V2).
RC   TISSUE=Glial tumor;
RX   PubMed=7806529;
RA   Dours-Zimmermann M.T., Zimmermann D.R.;
RT   "A novel glycosaminoglycan attachment domain identified in two
RT   alternative splice variants of human versican.";
RL   J. Biol. Chem. 269:32992-32998(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM V0).
RX   PubMed=7528742;
RA   Naso M.F., Zimmermann D.R., Iozzo R.V.;
RT   "Characterization of the complete genomic structure of the human
RT   versican gene and functional analysis of its promoter.";
RL   J. Biol. Chem. 269:32999-33008(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
RC   TISSUE=Brain;
RX   PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
RA   Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
RT   "Expression of PG-M(V3), an alternatively spliced form of PG-M without
RT   a chondroitin sulfate attachment in region in mouse and human
RT   tissues.";
RL   J. Biol. Chem. 270:3914-3918(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 208-1427; 2081-2372 AND 2897-3233
RP   (ISOFORM V1).
RX   PubMed=7921538; DOI=10.1016/0945-053X(94)90185-6;
RA   Yao L.Y., Moody C., Schoenherr E., Wight T.N., Sandell L.J.;
RT   "Identification of the proteoglycan versican in aorta and smooth
RT   muscle cells by DNA sequence analysis, in situ hybridization and
RT   immunohistochemistry.";
RL   Matrix Biol. 14:213-225(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-347.
RX   PubMed=1478664; DOI=10.1016/S0888-7543(05)80103-X;
RA   Iozzo R.V., Naso M.F., Cannizzaro L.A., Wasmuth J.J., McPherson J.D.;
RT   "Mapping of the versican proteoglycan gene (CSPG2) to the long arm of
RT   human chromosome 5 (5q12-5q14).";
RL   Genomics 14:845-851(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2709-3396.
RC   TISSUE=Lung fibroblast;
RX   PubMed=2820964;
RA   Krusius T., Gehlsen K.R., Ruoslahti E.;
RT   "A fibroblast chondroitin sulfate proteoglycan core protein contains
RT   lectin-like and growth factor-like sequences.";
RL   J. Biol. Chem. 262:13120-13125(1987).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3333-3396 (ISOFORM VINT).
RC   TISSUE=Aortic smooth muscle;
RX   PubMed=10397680; DOI=10.1161/01.ATV.19.7.1630;
RA   Lemire J.M., Braun K.R., Maurel P., Kaplan E.D., Schwartz S.M.,
RA   Wight T.N.;
RT   "Versican/PG-M isoforms in vascular smooth muscle cells.";
RL   Arterioscler. Thromb. Vasc. Biol. 19:1630-1639(1999).
RN   [9]
RP   PROTEIN SEQUENCE OF 21-37.
RX   PubMed=1429726;
RA   Perides G., Rahemtulla F., Lane W.S., Asher R.A., Bignami A.;
RT   "Isolation of a large aggregating proteoglycan from human brain.";
RL   J. Biol. Chem. 267:23883-23887(1992).
RN   [10]
RP   PROTEIN SEQUENCE OF 24-50; 80-119; 128-155; 167-218; 229-268 AND
RP   277-290.
RC   TISSUE=Brain;
RX   PubMed=2466833;
RA   Perides G., Lane W.S., Andrews D., Dahl D., Bignami A.;
RT   "Isolation and partial characterization of a glial hyaluronate-binding
RT   protein.";
RL   J. Biol. Chem. 264:5981-5987(1989).
RN   [11]
RP   PROTEIN SEQUENCE OF 171-210 AND 289-303.
RX   PubMed=2469524; DOI=10.1016/0361-9230(89)90129-9;
RA   Bignami A., Lane W.S., Andrews D., Dahl D.;
RT   "Structural similarity of hyaluronate binding proteins in brain and
RT   cartilage.";
RL   Brain Res. Bull. 22:67-70(1989).
RN   [12]
RP   TISSUE SPECIFICITY (ISOFORMS V0; V1; V2 AND V3).
RX   PubMed=8627343;
RA   Paulus W., Baur I., Dours-Zimmermann M.T., Zimmermann D.R.;
RT   "Differential expression of versican isoforms in brain tumors.";
RL   J. Neuropathol. Exp. Neurol. 55:528-533(1996).
RN   [13]
RP   INVOLVEMENT IN WGVRP.
RX   PubMed=16043844; DOI=10.1167/iovs.05-0057;
RA   Miyamoto T., Inoue H., Sakamoto Y., Kudo E., Naito T., Mikawa T.,
RA   Mikawa Y., Isashiki Y., Osabe D., Shinohara S., Shiota H., Itakura M.;
RT   "Identification of a novel splice site mutation of the CSPG2 gene in a
RT   Japanese family with Wagner syndrome.";
RL   Invest. Ophthalmol. Vis. Sci. 46:2726-2735(2005).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   INVOLVEMENT IN WGVRP, AND PATHOLOGICAL MECHANISM.
RX   PubMed=22739342; DOI=10.1038/ejhg.2012.137;
RA   Kloeckener-Gruissem B., Neidhardt J., Magyar I., Plauchu H.,
RA   Zech J.C., Morle L., Palmer-Smith S.M., Macdonald M.J., Nas V.,
RA   Fry A.E., Berger W.;
RT   "Novel VCAN mutations and evidence for unbalanced alternative splicing
RT   in the pathogenesis of Wagner syndrome.";
RL   Eur. J. Hum. Genet. 21:352-356(2013).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2116 AND THR-2617, AND
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   PHOSPHORYLATION AT SER-2116.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted
RT   phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: May play a role in intercellular signaling and in
CC       connecting cells with the extracellular matrix. May take part in
CC       the regulation of cell motility, growth and differentiation. Binds
CC       hyaluronic acid.
CC   -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P14780:MMP9; NbExp=3; IntAct=EBI-8515977, EBI-1382326;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=V0;
CC         IsoId=P13611-1; Sequence=Displayed;
CC       Name=V1;
CC         IsoId=P13611-2; Sequence=VSP_003082, VSP_003083;
CC       Name=V2;
CC         IsoId=P13611-3; Sequence=VSP_003084;
CC       Name=V3;
CC         IsoId=P13611-4; Sequence=VSP_003082, VSP_003085;
CC       Name=Vint;
CC         IsoId=P13611-5; Sequence=VSP_003086;
CC   -!- TISSUE SPECIFICITY: Cerebral white matter and plasma. Isoform V0
CC       and isoform V1 are expressed in normal brain, gliomas,
CC       medulloblastomas, schwannomas, neurofibromas, and meningiomas.
CC       Isoform V2 is restricted to normal brain and gliomas. Isoform V3
CC       is found in all these tissues except medulloblastomas.
CC   -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000269|PubMed:26091039}.
CC   -!- DISEASE: Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare
CC       vitreoretinopathy characterized by an optically empty vitreous
CC       cavity with fibrillary condensations and a preretinal avascular
CC       membrane. Other optical features include progressive chorioretinal
CC       atrophy, perivascular sheating, subcapsular cataract and myopia.
CC       {ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry. The pathological mechanism involves a
CC       quantitave imbalance of the normally occurring splice variants
CC       (PubMed:22739342). {ECO:0000269|PubMed:22739342}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Versican;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_214";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/VCANID40173ch5q14.html";
DR   EMBL; X15998; CAA34128.1; -; mRNA.
DR   EMBL; U16306; AAA65018.1; -; mRNA.
DR   EMBL; U26555; AAA67565.1; -; mRNA.
DR   EMBL; D32039; BAA06801.1; -; mRNA.
DR   EMBL; S52488; AAB24878.1; -; Genomic_DNA.
DR   EMBL; J02814; AAA36437.1; -; mRNA.
DR   EMBL; AF084545; AAD48545.1; -; mRNA.
DR   CCDS; CCDS4060.1; -. [P13611-1]
DR   CCDS; CCDS47242.1; -. [P13611-4]
DR   CCDS; CCDS54875.1; -. [P13611-3]
DR   CCDS; CCDS54876.1; -. [P13611-2]
DR   PIR; S06014; A60979.
DR   RefSeq; NP_001119808.1; NM_001126336.2. [P13611-4]
DR   RefSeq; NP_001157569.1; NM_001164097.1. [P13611-2]
DR   RefSeq; NP_001157570.1; NM_001164098.1. [P13611-3]
DR   RefSeq; NP_004376.2; NM_004385.4. [P13611-1]
DR   UniGene; Hs.643801; -.
DR   ProteinModelPortal; P13611; -.
DR   SMR; P13611; -.
DR   BioGrid; 107844; 21.
DR   IntAct; P13611; 6.
DR   MINT; P13611; -.
DR   STRING; 9606.ENSP00000265077; -.
DR   DrugBank; DB08818; Hyaluronic acid.
DR   CarbonylDB; P13611; -.
DR   GlyConnect; 1890; -.
DR   iPTMnet; P13611; -.
DR   PhosphoSitePlus; P13611; -.
DR   SwissPalm; P13611; -.
DR   BioMuta; VCAN; -.
DR   DMDM; 2506816; -.
DR   EPD; P13611; -.
DR   jPOST; P13611; -.
DR   MaxQB; P13611; -.
DR   PaxDb; P13611; -.
DR   PeptideAtlas; P13611; -.
DR   PRIDE; P13611; -.
DR   ProteomicsDB; 52938; -.
DR   ProteomicsDB; 52939; -. [P13611-2]
DR   ProteomicsDB; 52940; -. [P13611-3]
DR   ProteomicsDB; 52941; -. [P13611-4]
DR   ProteomicsDB; 52942; -. [P13611-5]
DR   DNASU; 1462; -.
DR   Ensembl; ENST00000265077; ENSP00000265077; ENSG00000038427. [P13611-1]
DR   Ensembl; ENST00000342785; ENSP00000342768; ENSG00000038427. [P13611-3]
DR   Ensembl; ENST00000343200; ENSP00000340062; ENSG00000038427. [P13611-2]
DR   Ensembl; ENST00000502527; ENSP00000421362; ENSG00000038427. [P13611-4]
DR   GeneID; 1462; -.
DR   KEGG; hsa:1462; -.
DR   UCSC; uc003kii.4; human. [P13611-1]
DR   CTD; 1462; -.
DR   DisGeNET; 1462; -.
DR   EuPathDB; HostDB:ENSG00000038427.15; -.
DR   GeneCards; VCAN; -.
DR   GeneReviews; VCAN; -.
DR   HGNC; HGNC:2464; VCAN.
DR   HPA; CAB008979; -.
DR   HPA; HPA004726; -.
DR   MalaCards; VCAN; -.
DR   MIM; 118661; gene.
DR   MIM; 143200; phenotype.
DR   neXtProt; NX_P13611; -.
DR   OpenTargets; ENSG00000038427; -.
DR   Orphanet; 898; Wagner disease.
DR   PharmGKB; PA162408788; -.
DR   eggNOG; ENOG410IFXS; Eukaryota.
DR   eggNOG; ENOG410ZPDG; LUCA.
DR   GeneTree; ENSGT00940000156102; -.
DR   HOVERGEN; HBG051140; -.
DR   InParanoid; P13611; -.
DR   KO; K06793; -.
DR   OMA; RENKTGR; -.
DR   OrthoDB; 74642at2759; -.
DR   PhylomeDB; P13611; -.
DR   TreeFam; TF332134; -.
DR   Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-HSA-2024101; CS/DS degradation.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR   Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR   Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR   Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR   Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SIGNOR; P13611; -.
DR   ChiTaRS; VCAN; human.
DR   GeneWiki; Versican; -.
DR   GenomeRNAi; 1462; -.
DR   PMAP-CutDB; P13611; -.
DR   PRO; PR:P13611; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000038427; Expressed in 242 organ(s), highest expression level in endometrium.
DR   ExpressionAtlas; P13611; baseline and differential.
DR   Genevisible; P13611; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; HDA:BHF-UCL.
DR   GO; GO:0005539; F:glycosaminoglycan binding; TAS:ProtInc.
DR   GO; GO:0005540; F:hyaluronic acid binding; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0008037; P:cell recognition; TAS:ProtInc.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
DR   GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome.
DR   GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0008347; P:glial cell migration; IDA:BHF-UCL.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd03588; CLECT_CSPGs; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 3.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033987; CSPG_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link_dom.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF56436; SSF56436; 3.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cataract; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Lectin; Phosphoprotein; Polymorphism;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     20       {ECO:0000269|PubMed:1429726}.
FT   CHAIN        21   3396       Versican core protein.
FT                                /FTId=PRO_0000017522.
FT   DOMAIN       21    146       Ig-like V-type.
FT   DOMAIN      150    245       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      251    347       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN     3089   3125       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3127   3163       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     3176   3290       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     3294   3354       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      348   1335       GAG-alpha (glucosaminoglycan attachment
FT                                domain).
FT   REGION     1336   3089       GAG-beta.
FT   MOD_RES    2116   2116       Phosphoserine; by FAM20C.
FT                                {ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:26091039}.
FT   MOD_RES    2608   2608       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62059}.
FT   MOD_RES    2617   2617       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...) asparagine.
FT   CARBOHYD    615    615       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    782    782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    809    809       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1332   1332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1398   1398       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1442   1442       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1468   1468       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1663   1663       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1898   1898       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2179   2179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2272   2272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2280   2280       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2360   2360       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2385   2385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2392   2392       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2496   2496       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2628   2628       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2934   2934       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3067   3067       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3369   3369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3379   3379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     44    130       {ECO:0000250}.
FT   DISULFID    172    243       {ECO:0000250}.
FT   DISULFID    196    217       {ECO:0000250}.
FT   DISULFID    270    345       {ECO:0000250}.
FT   DISULFID    294    315       {ECO:0000250}.
FT   DISULFID   3093   3104       {ECO:0000250}.
FT   DISULFID   3098   3113       {ECO:0000250}.
FT   DISULFID   3115   3124       {ECO:0000250}.
FT   DISULFID   3131   3142       {ECO:0000250}.
FT   DISULFID   3136   3151       {ECO:0000250}.
FT   DISULFID   3153   3162       {ECO:0000250}.
FT   DISULFID   3169   3180       {ECO:0000250}.
FT   DISULFID   3197   3289       {ECO:0000250}.
FT   DISULFID   3265   3281       {ECO:0000250}.
FT   DISULFID   3296   3339       {ECO:0000250}.
FT   DISULFID   3325   3352       {ECO:0000250}.
FT   VAR_SEQ     348    348       P -> R (in isoform V1 and isoform V3).
FT                                {ECO:0000303|PubMed:2583089,
FT                                ECO:0000303|PubMed:7876137,
FT                                ECO:0000303|PubMed:7921538}.
FT                                /FTId=VSP_003082.
FT   VAR_SEQ     349   3089       Missing (in isoform V3).
FT                                {ECO:0000303|PubMed:7876137}.
FT                                /FTId=VSP_003085.
FT   VAR_SEQ     349   1335       Missing (in isoform V1).
FT                                {ECO:0000303|PubMed:2583089,
FT                                ECO:0000303|PubMed:7921538}.
FT                                /FTId=VSP_003083.
FT   VAR_SEQ    1336   3089       Missing (in isoform V2).
FT                                {ECO:0000303|PubMed:7806529}.
FT                                /FTId=VSP_003084.
FT   VAR_SEQ    3355   3396       PSAYQRTYSMKYFKNSSSAKDNSINTSKHDHRWSRRWQESR
FT                                R -> RKWSFRKNGLPCYNNY (in isoform Vint).
FT                                {ECO:0000303|PubMed:10397680}.
FT                                /FTId=VSP_003086.
FT   VARIANT     300    300       S -> L (in dbSNP:rs2652098).
FT                                /FTId=VAR_021958.
FT   VARIANT     428    428       G -> D (in dbSNP:rs2287926).
FT                                /FTId=VAR_020214.
FT   VARIANT    1516   1516       K -> R (in dbSNP:rs309559).
FT                                /FTId=VAR_021959.
FT   VARIANT    1826   1826       R -> H (in dbSNP:rs188703).
FT                                /FTId=VAR_031632.
FT   VARIANT    2301   2301       F -> Y (in dbSNP:rs160278).
FT                                /FTId=VAR_020215.
FT   VARIANT    2315   2315       V -> L (in dbSNP:rs3734094).
FT                                /FTId=VAR_020216.
FT   VARIANT    2937   2937       D -> Y (in dbSNP:rs160277).
FT                                /FTId=VAR_021960.
FT   VARIANT    3011   3011       N -> K (in dbSNP:rs16900532).
FT                                /FTId=VAR_031633.
FT   CONFLICT     88     88       N -> D (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    260    260       K -> I (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    274    274       D -> A (in Ref. 4; BAA06801).
FT                                {ECO:0000305}.
FT   CONFLICT    284    284       Q -> G (in Ref. 10; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   2709   2713       IKAEA -> EFREV (in Ref. 7; AAA36437).
FT                                {ECO:0000305}.
SQ   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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