ID A0A2K6GZB4_PROCO Unreviewed; 3374 AA.
AC A0A2K6GZB4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:ENSPCOP00000031611.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000031611.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000031611.1}
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 STRING; 379532.ENSPCOP00000031611; -.
DR Ensembl; ENSPCOT00000042569.1; ENSPCOP00000031611.1; ENSPCOG00000028583.1.
DR GeneTree; ENSGT00940000156102; -.
DR OMA; ELTWKPE; -.
DR Proteomes; UP000233160; 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:UP000233160};
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..3374
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014419622"
FT DOMAIN 40..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 3067..3103
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3105..3141
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3154..3268
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3272..3332
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 591..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2801..2834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2860..2881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2953..2982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3347..3374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2083..2097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2801..2817
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 3093..3102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3131..3140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3274..3317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 3303..3330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 3374 AA; 369885 MW; 4318477C75EC385F CRC64;
MLINIKSILW MCSTLIATHA LHKVKVEKSP PVKGALSGKV SLPCHFSTMP TLPPSYNTSE
FLRIKWSKIE VDKNGKDLKE TTVLVAQNGN IKIGQGYKGR VSVPTHPEDV GDASLTMVKL
RASDAGLYRC DVMYGIEDTQ DSVSLAVDGV VFHYRAATSR YTLNFEMAQK ACVDVGAVIA
TPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPRETYD
VYCYVDHLDG EVFHITAPSK FTFEEAEEEC ENQDARLATV GELQAAWRNG FDQCDYGWLL
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKQ NISEATTIEL
NILAETASHR LSKEPQMVPN RTTPIIPLVN ELPVITTKFP PVESIVNFEQ KATVQPQAVT
DSLATESPTP AGSTKKLWDM DYYSPSASGP LGKPDISKIK EEVLQSTTVI SRHATDSSDG
VMEDTQTQES VTQIEQIEVG PLVTSMEISR HPPSKEFSVT ETPFVYTRMT LESKTEKKTV
STISELVTTS SYGFTLGEDD DEDRTLTVRS GQTTLVFSKI PEVITVSKTS EDTTHVQLED
SESVSASTTV SPLTMPDNGS SMDSWEGRQT NGRITEDFFG QYLSSTPFPS QRHTEVELFP
YSGDKILVEG ISTVTYPSPQ TEMTQGRERT KTLIPEMRTD TYTEDEIQEK ITKDPFAGKT
EEEGFSGMKL STSSSEQIHF TETSVEMTDT TKYSEDITTV HLTPSTLDVE VVTVSKWSLD
EDNTTSKPLE SIEHSGSPKL PPAFLITTGV NGKDKEIPSF TEDGGDEFTL IPDIARKQLE
EITEEDLIDH GKFTIRFQPT TSVGIAEKST LRYFATEESV PPITSTEDQV VYATMEGSAL
GEGEDVDISK PVSTVPKFAH TSEVEGLAFV NYSTTQEPTT YVDSSHTFPL SVISKTEWGV
LVPPVPSEGE VLGEPSQDIR VIDQTRLEAT VSHETITTTE TTQGTTQEEF PWKEETAEKP
VPALSSTAGM PKEATPPFDE QEGDGSAYTV SEERLMTGSE RVPVLETTSV GKIDHSMSYP
PGAITEHKMK MDEMVTLTPS IGPRVSLSPE TEQRYETEGS SPTEFITPLS TTQLIEETTT
EKREKTSLEY IDLGSELFEK PKATELPRFS TIKATGPSDI TGVWDVVDKL HTTSAFKPSS
ASTGKPPLID REPGEETTSD MVIIGESTSR VPPTTLDDIV PKETETDIDR EYFTTSSTPS
ATQPTGPPTV EGKEAVGPQA LSTPQPPMGT KFHPDINVYI IEVRENKTGR MSDLSVIGHP
IDSESKEDEP CSEETDPDHD LIAQILPGLP DIIEIDIYHS EEDEEDDEEC ANATDVTTTP
SVQYINGKHL ITTVPKDPEA AEARRGQFES VAPSQNFSDS SESDTHQFLI AETELSTAMQ
PSDSKETTEY LEITWKPETY PETSESFSGG ETDVSPTSPF HEAEATEGVE SITERSPELG
NQVHEYTEAV PLFPEESSGE AAIDQESQKI VFSGATDVTF GEVAEKSTSI MYTPTVVPSS
MSARVSEEGS VTLLGNLQPN DPLSTRESWI EITPRQIVEV SGSSSVPIAE GSGEVEEYKD
KMFTMVTDLS QRNTTDTIIT LDTSKVVITE NLFEIPATTI YSVSEQPSAE VVPTSLVSES
DTSKWVFSTS FEGKKRKEEE EGPTGTASAV EVHSPTQGSD QLILSSELES LDVATSSDSA
TGKTFMSLTT PTQSEREMTS STPVFTEGNV LEDLRAQTTK HSSSSQPGIQ EGLTTLPGST
FSLFMEQGSG EAAGVPETTT LSSFSLNIES EIPTKKETAG TLSPHVEKTF SSEPTRLVLS
TVIDREVEEI ISQTSKEKLV SEVSGKPNYG AEIRGFSTGF PLGEDFSGDF REYSTVSHPI
TKEEIVIMEG SGDAAFRDIQ ISPSAIPTSV RVSGTPNSEG PSSTSISTSA LLWEEFIASA
EGSGEQLVIV GSSVGPVLPS AVEFSGTDSP FIDQGLGEVG AINEADKRST VLPTVEAEGT
IVPTEKGEVK VNDTISMNFP QTMEPLKLWS RQEVNTVRQE IESETASEGK IQEEKSFESP
RSSLAPEQRI FDSQTFTETE RQTTDYSILT TKETYSTDKE MKEEGISLVN MSTPDPDAKG
LESYTILPEA TEKTHFSLAT ALVTESIPAE SMVTDSSIEE EESVKLFPKG MKPTIKESYT
DLLFSGLGSG EDVLPTLPTV SVNFTEMEQI VNTLYPQTSQ VENLETSSLS DKTEDYEGVE
NVANEVKPLI SKTDNSSESS EAVSSTTLIE ISSDTGAERP TMTPLPFSTD SKHLQNQTLG
WAEENRTSRP QTITERDSNK NSSTAETKET ATSFSVFLDR PYGLDMAKEF VTSAPKPTDL
FYEHSGEGSG ELAIVDSVHT SGTTQATRQG SITFVSDRSL EKHPEAPSAK AVTADEFPTV
PVVLPLHSEQ NQSSPDPTSI LSNTMLYERS TDATTGSFQD HFRGLEDSTL KPSRRKPTEN
IIIDLDKEDK DLILTITERT VLETLPVLTS DKNTIIDIDH TKPVYEDILG MQTDIDPEIP
SGSHGGNDES TQVQEKYGAA VNLSLTEETF EGSGDPLLAS YTQATHNESM TSKDRSQSDH
KGFNFTTEIP VPSKEAELDI LLPTATSLPI PSKSATENPE IEEPKIEAKA LDDIFESSTL
SDGQAIADQS EIISTLGHLE GTKEEYEEKK YAGPSFQPEF SSGAEETLID HTPYVSISTV
HVMAQSLTEA PNVVDGSSSP YYTDTTSAVS AFAKLSSQTP SSPLTTYIGS GASEHTEVPQ
PSALPGIDAG SSQMSPEYSF KEIHANIEAT FKPSSEEYFH ITEPPSLSPD TKLEPSEDES
KPKLLKEMEA SPTELIAGEG TEILQDFHNK INGQLFGETI IVVPSVKTPT PEAGTVLTDA
NEINLEGATQ WPHATSASAP SGVEAGVVPQ PSPETSEEPT IPSSFLEINP ETQTAFIRME
DSTAASAEQQ VSARILDSNN QATVSTLELN TELATPPFPH LETSNETDFL IGISEESVEG
TAIYLPGPDR CKTNPCLNGG TCYPTETSYV CTCVPGYSGD RCELDFDECH SNPCRNGATC
IDGFNTFRCL CLPSYVGALC EQDTETCDYG WHKFQGQCYK YFAHRRTWDA AERECRLQGA
HLTSILSHEE QMFVNRVGHD YQWIGLNDKM FEHDFRWTDG STLQYENWRP NQPDSFFSAG
EDCVVIIWHE NGQWNDVPCN YHLTYTCKKG TVACGQPPVV ENAKTFGKMK PRYEINSLIR
YHCKDGFIQR HLPTIRCLGN GRWAMPKITC MNPSAYQRTY SKKYFKNSSS EKDNSSNTSK
HEHRWIRRWQ ESRR
//
