ID F7ED35_CALJA Unreviewed; 1564 AA.
AC F7ED35;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Versican core protein {ECO:0000256|ARBA:ARBA00044099};
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2 {ECO:0000256|ARBA:ARBA00044230};
DE AltName: Full=Large fibroblast proteoglycan {ECO:0000256|ARBA:ARBA00044263};
DE AltName: Full=PG-M {ECO:0000256|ARBA:ARBA00044266};
GN Name=VCAN {ECO:0000313|Ensembl:ENSCJAP00000020649.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000020649.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000020649.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000020649.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00043896}.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000256|ARBA:ARBA00044030}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000256|ARBA:ARBA00004504}. Secreted, extracellular space,
CC extracellular matrix, interphotoreceptor matrix
CC {ECO:0000256|ARBA:ARBA00004593}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000256|ARBA:ARBA00006838}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSCJAT00000021825.5; ENSCJAP00000020649.4; ENSCJAG00000011161.5.
DR GeneTree; ENSGT00940000156102; -.
DR HOGENOM; CLU_000303_0_1_1; -.
DR Proteomes; UP000008225; Chromosome 2.
DR Bgee; ENSCJAG00000011161; Expressed in ovary and 5 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 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; 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; 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; 2.
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; 1.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1564
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035314274"
FT DOMAIN 34..146
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 150..245
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 251..347
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1336..1372
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1374..1410
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1419..1484
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1488..1548
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 421..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 196..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 294..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1362..1371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1400..1409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1490..1533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1519..1546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1564 AA; 172943 MW; C86C77D603C968C1 CRC64;
MLINIKSILW MCSTLIATHA LHKVKVEKSP TVRGSLSGKV SLPCHFSTMP TLSPSYNTSE
FLRIKWSKIE VDKNGKDLKE TTILVAQNGN IKVGQDYKGR VSMPTHPEPV GDATLTMVKL
LASDAGHYRC DVMYGIDDTQ DTVSLAVDGV VFHYRAATSR YTLNFEAAQK ACLDIGAVIA
TPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RTPREGCYGD MMGKEGVRTY GFRSPQETYD
VYCYVDHLDG DVFHITVPNK FTFEEAAKEC ENRDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKE ATTIDLSILA
ETTSPSLSKE PQIVSDRTTP IIPLVDELPV IPTEFPAVGN IVNLEQKSTV QPQAVTDSLA
AKLPTPTGST KKPWDTDDYS PSASGPLRKL DISEIKEEVL QSTTVISRYA TDSWDGVMED
TQTQESATQI EQIEVGPLVT SMEILKHIPS KEFLVTETPL VTARMTLEPK TEKKTVSTVS
ELETTGHRRF TLEEDDDDDR TVTVGSDEST LVFGQIPEVI NVSETSEDTT HTQPEDLESV
LASTTVSGPL IIPDHNESSM DRWEERQTNG RIMEDFFGKY LSITPFPSQH HTEVELFPYS
GDKILVEGIS TVIYPSPQTE MTRGRERTET LIPEMRTDTY TDEIQEEITK SSFMGKTEEE
GFPRIEPSTS PSEPICVTES SAEMTKAFDF PTLTTKLSAE TTEVRDMEEG FTATPGTTKY
DENVTTVHLT HSTLSVEVAT VSKWSWDEDN TTSKPLESTE PSTSSKLPPP LLPTVEMNAE
GKEIPSFTED GGDVFTLIPD STQKQLEEIT DEDLAAHGKF TIRFQPTTSI GIAEKSTLRD
STMKEEVPST TSTEGQVVYA TMEGSALGEV EDGDFSKPVS TVAQFAHPSE VEGLTFVSYS
STQEPTTYVD SSHTIPISVI PKTDWGVLVP SVPSEDEVVG EPSQDTRIID QTHLEATISP
ETMRTTRITE GTTQEEFPCK EETAEKPVPA VSSTAWTPKE AVRPLDEQEG DGSAYTVFED
KLLTGSERAP VLETTPAGKV DLSVSYQPGA ITEHKGKTDE MVTLTPSIGP KVSLSPGPEQ
KYETEGSSTT GFTSSVSPFS THVTRPMEET TTEKTYLEDI DLGSGLFEKP KATELEFSTI
KVTVPSDITT VFSSVDGLHT TSAFKPSSTF TKKPLLIDRE PGEETTSDMV IIGESSSHVP
PTTLEDIVAK ETEADIDREY FTTSSTPATQ PTRPPTAEDK EAFGPQALST LQPPAGTKLH
SDVNVYIIEV RENKTGPDHC KMNPCLNGGT CYPTETSYVC TCVPGYSGDQ CELDFDECHS
NPCRNGATCV DGFNTFRCLC LPSYIGALCE RGVGHDYQWI GLNDKMFEHD FRWTDGSTLQ
YENWRPNQPD SFFSAGEDCV VIIWHENGQW NDVPCNYHLT YTCKKGTVAC GQPPVVENAK
TFGKMKPRYE INSLIRYHCK EGFIQRHLPT IRCLGNGRWA IPKITCMNRK WSFRKNGLPC
YNNY
//
