ID F1MZ83_BOVIN Unreviewed; 1643 AA.
AC F1MZ83;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 95.
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:ENSBTAP00000019852.5,
GN ECO:0000313|VGNC:VGNC:36778};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000019852.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000019852.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019852.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000019852.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019852.5};
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; ENSBTAT00000019852.5; ENSBTAP00000019852.5; ENSBTAG00000014906.6.
DR VEuPathDB; HostDB:ENSBTAG00000014906; -.
DR VGNC; VGNC:36778; VCAN.
DR GeneTree; ENSGT00940000156102; -.
DR HOGENOM; CLU_000303_0_1_1; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014906; Expressed in granulosa cell and 104 other cell types or tissues.
DR ExpressionAtlas; F1MZ83; baseline and differential.
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:InterPro.
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 1: Evidence at protein level;
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 Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1MZ83};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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 DOMAIN 33..147
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 151..246
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 252..348
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 1423..1537
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1541..1601
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 197..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 295..316
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 1543..1586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1572..1599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1643 AA; 182928 MW; 6D0BBB44E6A693ED CRC64;
MLINIKSILW MCSTLIAAHA LQKVNMEKSP PVKGSLSGKV NLPCHFSTMP TLPPSYNTTS
EFLRIKWSKI ELDKTGKDLK ETTVLVAQNG NIKIGQDYKG RVSVPTHPED VGDASLTMVK
LLASDAGRYR CDVMYGIEDT QDTVSLTVEG VVFHYRAATS RYTLNFEMAQ KACVDIGAVI
ATPEQLHAAY EDGFEQCDAG WLSDQTVRYP IRVPREGCYG DMMGKEGVRT YGFRAPHETY
DVYCYVDHLD GDVFHITAPN KFTFEEAGEE CKTQDARLAT VGELQAAWRN GFDRCDYGWL
LDASVRHPVT VARAQCGGGL LGVRTLYRFE NQTGFPTPDS RFDAYCFKPK QNISEATTIE
LNMLAETVSP TLLEELQMGL DRMTPIVPLI TELPVITTKV PPIGNIVNFE QKSTVQPLTS
THRSATESLP PDGSMKKPWD MDYYSPSASG PLGEPDVSEI KEEVPQSTTV VSHHAPDSWD
GVKEDLQIKD SVTQIEQIEV GPLVTSMEIS KHIPSKEFTV TVTPFVSTTM TLESKTEKKA
ISTVSESVTT SHYGFTLREG DGEDRISTVR SGQSTSIFSQ IPEVITVSKT SEDTTRGQLE
DVESVSASTI VSPDSDGSPM DHRQEKQTHG RITEGFLGQY VSTTPFPSQH HTEVELFPYS
GDKRLVEGTS TVISPTPRTG RERTETLRPA MRTVTYTNDE IQEKITKDSS IEKIEEEGFS
GMKFPTASPE QIHHTKYSVG MTKSFESPAL MTTTKPGVTP TEATDVEEDF TTPSGLETDG
YQDTTEYEEG ITTVHLIQST LNVEVVTVSK WSLDEDNTTS KPLGSTEHVG SPKLPPALIT
TTGVSGKDKE MPSLTEDGRD EFTRIPGSTQ RPLEEFTEED TTDHEKFTVR FQPTTSIATT
EKSTLRDSIT EERVPPFTST EVRVTHATIE GSALDEGEDV DVSKPLSTVP QFAHPSDVEG
STFVNYSSTQ EPTTYVDTSH TIPLPVIPKT EWGVLVPSIP SEGEVLGEPS QDIRVINQTH
FEASMYPETV RTTTEITQEA TREDFLWKEQ TPEKPVSPPS STTDTAKETT PPLDEQESDG
SAYTVFEDRS VMGSDRVSVL VTTPIGKFEQ HTSFPPGAVT KAKTDEVVTL TPTTGSKVTF
SPWPKQKYET EGTSPRGFVS PFSIGVTQLI EETTTEKREK TSLDYIDLGS GLFEKPKATE
LPEFSTVKAT VPSDTAAFSS ADRLHTPSAS TEKPPLIDRE PDEETTSDMV IIGESTSRVP
PTTLEDIVAK ETETDIDREY FTTSSTSTTQ PTRPPTVEGK EAFGPQAFST PEPPAGTKFH
PDINVYIIEV RENKTGPDRC KMNPCLNGGT CYPTETSYVC TCVPGYSGDR CELDFDECHS
NPCRNGATCI DGFNTFRCLC LPSYVGALCE QDTETCDYGW HKFQGQCYKY FAHRRTWDAA
ERECRLQGAH LTSILSHEEQ MFVNRVGHDY QWIGLNDKMF EHDFRWTDGS TLQYENWRPN
QPDSFFSTGE DCVVIIWHEN GQWNDVPCNY HLTYTCKKGT VACGQPPVVE NAKTFGKMKP
RYEINSLIRY HCKDGFIQRH LPTIRCLGNG RWAMPKITCL NPSAYQRTYS KKYFKNSSSA
KDNSINTSKH DHRWSRRWQE SRR
//
