ID A0A2K5DC77_AOTNA Unreviewed; 1644 AA.
AC A0A2K5DC77;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ENSANAP00000018553.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000018553.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000018553.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_012333028.1; XM_012477605.1.
DR Ensembl; ENSANAT00000036414.1; ENSANAP00000018551.1; ENSANAG00000027105.1.
DR Ensembl; ENSANAT00000036416.1; ENSANAP00000018553.1; ENSANAG00000027105.1.
DR GeneID; 105734690; -.
DR CTD; 1462; -.
DR GeneTree; ENSGT00940000156102; -.
DR OrthoDB; 5323609at2759; -.
DR Proteomes; UP000233020; Unplaced.
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; 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; SM00406; IGv; 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; 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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW 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:UP000233020};
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..1644
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014561321"
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 1337..1373
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1375..1411
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1424..1538
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1542..1602
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 420..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..614
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 1142..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1644
FT /note="Basic and acidic 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 1363..1372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1401..1410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1544..1587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1573..1600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1644 AA; 182640 MW; 70FE4E35C47CC909 CRC64;
MLINIKSILW MCSTLIATHA LHKVKVEKSP LVRGSLSGKV SLPCHFSTIP TLSPSYNTSE
FLRIKWSKIE MDKNGKDLKE ITILVAQNGN IKVGQDYKGR VSMPTHPEPV GDATLTMVKL
LASDAGHYRC DVMYGIDDTQ DTVSLAVDGV VFHYRAATSR YTLNFEAAQK ACLDIGAVIA
TPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RTPREGCYGD MMGKEGVRTY GLRSPQETYD
VYCYVDHLDG DVFHITVPNK FTFEEAAEEC ENRDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKE ATTIDLSILA
ETTSPSLSKE PQMVSDRTTP IIPLVDELPV IPTEFPPVGN IVNFEQKATV QPQAMTHSLA
TKLPTPTGST KKPWDMDDYS PSASGPLRKP DISEIKEEVL QSTTVISHYA TDSWDGVMED
TQTQESATQI EQIEVGPLVT SMEILKHIPS KEFPVTETPL VTAGMTLESK TEKKTVSTIS
ELETTGHRRF TLKEDDDEDK TVTVGSDEST LIFGQIPEVI KVSETSEDTT HTQLEDLESV
SASTTVSGPL TVPDRNESSM DRWEERQTNG RIMEDFFGKY LSITPFPSQH HTEVELFPYS
GDKILVEGIS TVIYPSPQTE MTHGREKTES LIPEMRTDTY TDEIQEEITE SSFMGKTEEE
GFPRMKPSTS PSKPICVTES SAEVTKAFDF PTLTTKLSAE TTEVRDTEEG FTATPGTIKY
DENVTTVHLT HSTLSVEVAT VSKWSWDEDN TTSKPLESTE PSASSKLPPA LLPTVGMNGE
DKEIPSFTED GGDEFILIPD STQKQLEEIT DEDLAAHGKF TIRFQPTTSI GIAEKSTLRD
STTEEKVPPT TSTEGQVVYA TTEGSALGEV EYVDFSKPIA TVTQFAHTSE VEGLAFVSYS
STQEPTTYVD SSHTFPISVI PKTDWGVLVP SVPSEDEVVG EPSQDMHVID QTHLEATISP
VTMRTTKITE GTTQEEFPCK EETTEKPVPA VSSTAWTPKE AVTPLDEQEG DGSAYTVFED
KLFTGSERVP FLETTPAGKV DHSVSYPPGA ITEHKVKTDE MVTLTPSIGP KVSLSPGPEQ
KYETEGHSTT GFTSSLSPFS THVTRPMEET TTEKTYLEDI DLGSGLFEKP KATELPEFST
IKVTVPSDIT TVFSSVDGLH TTSAFKPSSV FTKKPPLIDR EPGEETTSDM VIIGESSSHV
PPTTLEDIVA KETEADIDKE YFTTSGTPAT QPTRPPTAED KEAFGPQALS TPQPPTGTKL
HSDVNVYIIE VRENKTGPDH CKMNPCLNGG TCYPTETSYV CTCVPGYSGD QCELDFDECH
SNPCRNGATC VDGFNTFRCL CLPSYVGALC ERDTETCDYG WHKFQGQCYK YFAHRRTWDA
AERECRLQGA HLTSILSHEE QMFVNRVGHD YQWIGLNDKM FEHDFRWTDG STLQYENWRP
NQPDSFFSAG EDCVVIIWHE NGQWNDVPCN YHLTYTCKKG TVACGQPPVV ENAKTFGKMK
PRYEINSLIR YHCKEGFIQR HLPTIRCLGN GRWAIPKITC MNPSAYQRTY SMKYFKTSSS
AKDNSVNTSK HDHRWSRRWQ ESRR
//
