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 27-MAR-2024, entry version 251. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V1), AND SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=2583089; DOI=10.1002/j.1460-2075.1989.tb08447.x; 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; DOI=10.1016/s0021-9258(20)30089-2; RA Dours-Zimmermann M.T., Zimmermann D.R.; RT "A novel glycosaminoglycan attachment domain identified in two alternative RT 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; DOI=10.1016/s0021-9258(20)30090-9; RA Naso M.F., Zimmermann D.R., Iozzo R.V.; RT "Characterization of the complete genomic structure of the human versican RT 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 a RT chondroitin sulfate attachment in region in mouse and human tissues."; RL J. Biol. Chem. 270:3914-3918(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-1427; 2081-2372 AND 2897-3233 (ISOFORM RP V1), AND DEVELOPMENTAL STAGE. 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 muscle RT 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 human RT 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; DOI=10.1016/s0021-9258(18)45176-9; 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., 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; DOI=10.1016/s0021-9258(18)35919-2; 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 277-290. RC TISSUE=Brain; RX PubMed=2466833; DOI=10.1016/s0021-9258(18)83646-8; 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, AND TISSUE SPECIFICITY. 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; DOI=10.1097/00005072-199605000-00005; 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., Buerckstuemmer T., RA 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., Zech J.C., RA Morle L., Palmer-Smith S.M., Macdonald M.J., Nas V., Fry A.E., Berger W.; RT "Novel VCAN mutations and evidence for unbalanced alternative splicing in RT 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT 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 phosphoproteome."; RL Cell 161:1619-1632(2015). RN [18] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-1548. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [19] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023; RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y., RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C., RA Lako M.; RT "Extracellular matrix component expression in human pluripotent stem cell- RT derived retinal organoids recapitulates retinogenesis in vivo and reveals RT an important role for IMPG1 and CD44 in the development of photoreceptors RT and interphotoreceptor matrix."; RL Acta Biomater. 74:207-221(2018). RN [20] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-659; SER-1548; SER-1631; RP SER-1959; SER-2247 AND SER-2767. RX PubMed=32337544; DOI=10.1093/glycob/cwaa039; RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A., RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D., RA Larson G., Salanti A., Clausen T.M.; RT "An affinity chromatography and glycoproteomics workflow to profile the RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in RT the placenta and in cancer."; RL Glycobiology 30:989-1002(2020). RN [21] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-1548; SER-1631; SER-1935; RP SER-1959; SER-2254; SER-2723 AND SER-2941. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). CC -!- FUNCTION: May play a role in intercellular signaling and in connecting CC cells with the extracellular matrix. May take part in the regulation of CC cell motility, growth and differentiation. Binds hyaluronic acid. CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}. CC -!- INTERACTION: CC P13611; P14780: MMP9; NbExp=3; IntAct=EBI-8515977, EBI-1382326; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000305|PubMed:2583089}. Cell projection, cilium, CC photoreceptor outer segment {ECO:0000269|PubMed:29777959}. Secreted, CC extracellular space, extracellular matrix, interphotoreceptor matrix CC {ECO:0000269|PubMed:29777959}. Secreted {ECO:0000269|PubMed:25326458}. 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: Detected in placenta (at protein level) CC (PubMed:32337544). Detected in cerebrospinal fluid, fibroblasts and CC urine (at protein level) (PubMed:25326458, PubMed:36213313). Expressed CC in the retina (at protein level) (PubMed:29777959). Cerebral white CC matter and plasma (PubMed:2469524). Isoform V0: Expressed in normal CC brain, gliomas, medulloblastomas, schwannomas, neurofibromas, and CC meningiomas (PubMed:8627343). Isoform V1: Expressed in normal brain, CC gliomas, medulloblastomas, schwannomas, neurofibromas, and meningiomas CC (PubMed:8627343). Isoform V2: Restricted to normal brain and gliomas CC (PubMed:8627343). Isoform V3: Found in all these tissues except CC medulloblastomas (PubMed:8627343). {ECO:0000269|PubMed:2469524, CC ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:29777959, CC ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313, CC ECO:0000269|PubMed:8627343}. CC -!- DEVELOPMENTAL STAGE: Expressed in developing photoreceptors and the CC interphotoreceptor matrix between 12 and 17 weeks post conception (at CC protein level) (PubMed:29777959). Disappears in aorta after the CC cartilage development (PubMed:7921538). {ECO:0000269|PubMed:29777959, CC ECO:0000269|PubMed:7921538}. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000269|PubMed:26091039}. CC -!- PTM: Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the CC pericellular matrix surrounding myoblasts, facilitating myoblast CC contact and fusion which is required for skeletal muscle development CC and regeneration. {ECO:0000250|UniProtKB:Q62059}. CC -!- DISEASE: Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare CC vitreoretinopathy characterized by an optically empty vitreous cavity CC with fibrillary condensations and a preretinal avascular membrane. CC Other optical features include progressive chorioretinal atrophy, CC perivascular sheating, subcapsular cataract and myopia. CC {ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. The pathological mechanism involves a quantitative imbalance of CC the normally occurring splice variants (PubMed:22739342). CC {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 and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40173/VCAN"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P13611; -. DR BioGRID; 107844; 52. DR IntAct; P13611; 11. DR MINT; P13611; -. DR STRING; 9606.ENSP00000265077; -. DR DrugBank; DB08818; Hyaluronic acid. DR CarbonylDB; P13611; -. DR GlyConnect; 1890; 14 N-Linked glycans (9 sites), 1 O-Linked glycan (1 site). DR GlyCosmos; P13611; 191 sites, 23 glycans. DR GlyGen; P13611; 276 sites, 13 N-linked glycans (9 sites), 11 O-linked glycans (242 sites). DR iPTMnet; P13611; -. DR PhosphoSitePlus; P13611; -. DR SwissPalm; P13611; -. DR BioMuta; VCAN; -. DR DMDM; 2506816; -. DR CPTAC; CPTAC-5841; -. DR CPTAC; CPTAC-5866; -. DR EPD; P13611; -. DR jPOST; P13611; -. DR MassIVE; P13611; -. DR MaxQB; P13611; -. DR PaxDb; 9606-ENSP00000265077; -. DR PeptideAtlas; P13611; -. DR ProteomicsDB; 52938; -. [P13611-1] DR ProteomicsDB; 52939; -. [P13611-2] DR ProteomicsDB; 52940; -. [P13611-3] DR ProteomicsDB; 52941; -. [P13611-4] DR ProteomicsDB; 52942; -. [P13611-5] DR Pumba; P13611; -. DR Antibodypedia; 1346; 360 antibodies from 30 providers. DR DNASU; 1462; -. DR Ensembl; ENST00000265077.8; ENSP00000265077.3; ENSG00000038427.16. [P13611-1] DR Ensembl; ENST00000342785.8; ENSP00000342768.4; ENSG00000038427.16. [P13611-3] DR Ensembl; ENST00000343200.9; ENSP00000340062.5; ENSG00000038427.16. [P13611-2] DR Ensembl; ENST00000502527.2; ENSP00000421362.2; ENSG00000038427.16. [P13611-4] DR GeneID; 1462; -. DR KEGG; hsa:1462; -. DR MANE-Select; ENST00000265077.8; ENSP00000265077.3; NM_004385.5; NP_004376.2. DR UCSC; uc003kii.4; human. [P13611-1] DR AGR; HGNC:2464; -. DR CTD; 1462; -. DR DisGeNET; 1462; -. DR GeneCards; VCAN; -. DR GeneReviews; VCAN; -. DR HGNC; HGNC:2464; VCAN. DR HPA; ENSG00000038427; Tissue enhanced (lymphoid tissue, placenta). 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 VEuPathDB; HostDB:ENSG00000038427; -. DR eggNOG; ENOG502QRBE; Eukaryota. DR GeneTree; ENSGT00940000156102; -. DR HOGENOM; CLU_000303_1_1_1; -. DR InParanoid; P13611; -. DR OMA; ELTWKPE; -. DR OrthoDB; 5323609at2759; -. DR PhylomeDB; P13611; -. DR TreeFam; TF332134; -. DR PathwayCommons; P13611; -. 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 SignaLink; P13611; -. DR SIGNOR; P13611; -. DR BioGRID-ORCS; 1462; 8 hits in 1144 CRISPR screens. DR ChiTaRS; VCAN; human. DR GeneWiki; Versican; -. DR GenomeRNAi; 1462; -. DR Pharos; P13611; Tbio. DR PRO; PR:P13611; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P13611; Protein. DR Bgee; ENSG00000038427; Expressed in monocyte and 208 other cell types or tissues. DR ExpressionAtlas; P13611; baseline and differential. 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; TAS:ProtInc. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0072534; C:perineuronal net; IBA:GO_Central. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IBA:GO_Central. 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; ISS: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:0007417; P:central nervous system development; IBA:GO_Central. DR GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central. DR GO; GO:0008347; P:glial cell migration; IDA:BHF-UCL. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. DR CDD; cd00033; CCP; 1. DR CDD; cd03588; CLECT_CSPGs; 1. DR CDD; cd00054; EGF_CA; 2. DR CDD; cd05901; Ig_Versican; 1. DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1. DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; 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 PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1. DR PANTHER; PTHR22804:SF6; VERSICAN CORE PROTEIN; 1. 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; SSF56436; C-type lectin-like; 3. DR SUPFAM; SSF57535; Complement control module/SCR domain; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF48726; Immunoglobulin; 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. DR Genevisible; P13611; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cataract; Cell projection; KW Direct protein sequencing; Disulfide bond; EGF-like domain; KW Extracellular matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin domain; KW Lectin; Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted; KW Signal; Sushi. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:1429726" FT CHAIN 21..3396 FT /note="Versican core protein" FT /id="PRO_0000017522" FT DOMAIN 21..146 FT /note="Ig-like V-type" FT DOMAIN 150..245 FT /note="Link 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323" FT DOMAIN 251..347 FT /note="Link 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323" FT DOMAIN 3089..3125 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 3127..3163 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 3176..3290 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 3294..3354 FT /note="Sushi" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT REGION 348..1335 FT /note="GAG-alpha (glucosaminoglycan attachment domain)" FT REGION 420..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 603..622 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 807..829 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1126..1154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1277..1316 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1336..3089 FT /note="GAG-beta" FT REGION 1420..1497 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1510..1539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1717..1737 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1759..1789 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1962..1994 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2107..2134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2168..2188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2371..2396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2445..2473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2493..2518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2598..2617 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2834..2856 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2881..2905 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3371..3396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1138..1154 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1435..1453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1461..1480 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1717..1732 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1963..1994 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2445..2463 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2493..2517 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3378..3396 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1428..1429 FT /note="Cleavage; by ADAMTS15" FT /evidence="ECO:0000250|UniProtKB:Q62059" FT MOD_RES 2116 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2608 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62059" FT MOD_RES 2617 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 615 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 659 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:32337544" FT CARBOHYD 782 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 809 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1332 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1398 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1442 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1468 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1548 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313" FT CARBOHYD 1631 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:32337544, FT ECO:0000269|PubMed:36213313" FT CARBOHYD 1663 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1898 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1935 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT CARBOHYD 1959 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:32337544, FT ECO:0000269|PubMed:36213313" FT CARBOHYD 2179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2247 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:32337544" FT CARBOHYD 2254 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT CARBOHYD 2272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2360 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2385 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2392 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2496 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2628 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2722 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000255" FT CARBOHYD 2723 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT CARBOHYD 2767 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:32337544" FT CARBOHYD 2934 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2941 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT CARBOHYD 3067 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 3369 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 3379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 44..130 FT /evidence="ECO:0000250" FT DISULFID 172..243 FT /evidence="ECO:0000250" FT DISULFID 196..217 FT /evidence="ECO:0000250" FT DISULFID 270..345 FT /evidence="ECO:0000250" FT DISULFID 294..315 FT /evidence="ECO:0000250" FT DISULFID 3093..3104 FT /evidence="ECO:0000250" FT DISULFID 3098..3113 FT /evidence="ECO:0000250" FT DISULFID 3115..3124 FT /evidence="ECO:0000250" FT DISULFID 3131..3142 FT /evidence="ECO:0000250" FT DISULFID 3136..3151 FT /evidence="ECO:0000250" FT DISULFID 3153..3162 FT /evidence="ECO:0000250" FT DISULFID 3169..3180 FT /evidence="ECO:0000250" FT DISULFID 3197..3289 FT /evidence="ECO:0000250" FT DISULFID 3265..3281 FT /evidence="ECO:0000250" FT DISULFID 3296..3339 FT /evidence="ECO:0000250" FT DISULFID 3325..3352 FT /evidence="ECO:0000250" FT VAR_SEQ 348 FT /note="P -> R (in isoform V1 and isoform V3)" FT /evidence="ECO:0000303|PubMed:2583089, FT ECO:0000303|PubMed:7876137, ECO:0000303|PubMed:7921538" FT /id="VSP_003082" FT VAR_SEQ 349..3089 FT /note="Missing (in isoform V3)" FT /evidence="ECO:0000303|PubMed:7876137" FT /id="VSP_003085" FT VAR_SEQ 349..1335 FT /note="Missing (in isoform V1)" FT /evidence="ECO:0000303|PubMed:2583089, FT ECO:0000303|PubMed:7921538" FT /id="VSP_003083" FT VAR_SEQ 1336..3089 FT /note="Missing (in isoform V2)" FT /evidence="ECO:0000303|PubMed:7806529" FT /id="VSP_003084" FT VAR_SEQ 3355..3396 FT /note="PSAYQRTYSMKYFKNSSSAKDNSINTSKHDHRWSRRWQESRR -> RKWSFR FT KNGLPCYNNY (in isoform Vint)" FT /evidence="ECO:0000303|PubMed:10397680" FT /id="VSP_003086" FT VARIANT 300 FT /note="S -> L (in dbSNP:rs2652098)" FT /id="VAR_021958" FT VARIANT 428 FT /note="G -> D (in dbSNP:rs2287926)" FT /id="VAR_020214" FT VARIANT 1516 FT /note="K -> R (in dbSNP:rs309559)" FT /id="VAR_021959" FT VARIANT 1826 FT /note="R -> H (in dbSNP:rs188703)" FT /id="VAR_031632" FT VARIANT 2301 FT /note="F -> Y (in dbSNP:rs160278)" FT /id="VAR_020215" FT VARIANT 2315 FT /note="V -> L (in dbSNP:rs3734094)" FT /id="VAR_020216" FT VARIANT 2937 FT /note="D -> Y (in dbSNP:rs160277)" FT /id="VAR_021960" FT VARIANT 3011 FT /note="N -> K (in dbSNP:rs16900532)" FT /id="VAR_031633" FT CONFLICT 88 FT /note="N -> D (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="K -> I (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="D -> A (in Ref. 4; BAA06801)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="Q -> G (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 2709..2713 FT /note="IKAEA -> EFREV (in Ref. 7; AAA36437)" FT /evidence="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 //