GenomeNet

Database: UniProt
Entry: P81282
LinkDB: P81282
Original site: P81282 
ID   CSPG2_BOVIN             Reviewed;        3381 AA.
AC   P81282; O77609; O77610; O77611; O77612;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   10-APR-2019, entry version 141.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1; V2 AND V3).
RC   TISSUE=Forebrain;
RX   PubMed=9624174; DOI=10.1074/jbc.273.25.15758;
RA   Schmalfeldt M., Dours-Zimmermann M.T., Winterhalter K.H.,
RA   Zimmermann D.R.;
RT   "Versican V2 is a major extracellular matrix component of the mature
RT   bovine brain.";
RL   J. Biol. Chem. 273:15758-15764(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-53; 78-96; 226-250; 262-277; 295-306; 314-324;
RP   329-331 AND 342-348.
RC   TISSUE=Spinal cord;
RX   PubMed=1720020; DOI=10.1016/0304-4165(91)90273-J;
RA   Perides G., Biviano F., Bignami A.;
RT   "Interaction of a brain extracellular matrix protein with hyaluronic
RT   acid.";
RL   Biochim. Biophys. Acta 1075:248-258(1991).
CC   -!- FUNCTION: May play a role in intercellular signaling and in
CC       connecting cells with the extracellular matrix. May take part in
CC       the regulation of cell motility, growth and differentiation. Binds
CC       hyaluronic acid.
CC   -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=V0;
CC         IsoId=P81282-1; Sequence=Displayed;
CC       Name=V1;
CC         IsoId=P81282-2; Sequence=VSP_003078, VSP_003079;
CC       Name=V2;
CC         IsoId=P81282-3; Sequence=VSP_003080;
CC       Name=V3;
CC         IsoId=P81282-4; Sequence=VSP_003078, VSP_003081;
CC   -!- TISSUE SPECIFICITY: Cerebral white matter. Isoform V0 and isoform
CC       V1 are expressed in the central nervous system, and in a number of
CC       mesenchymal and epithelial tissues; the major isoform V2 is
CC       restricted to the central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P13611}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
DR   EMBL; AF060456; AAC24358.1; -; mRNA.
DR   EMBL; AF060457; AAC24359.1; -; mRNA.
DR   EMBL; AF060458; AAC24360.1; -; mRNA.
DR   EMBL; AF060459; AAC24361.1; -; mRNA.
DR   PIR; T14274; T14274.
DR   PIR; T42389; T42389.
DR   RefSeq; NP_851378.1; NM_181035.2. [P81282-1]
DR   RefSeq; XP_015327844.1; XM_015472358.1. [P81282-4]
DR   UniGene; Bt.5395; -.
DR   ProteinModelPortal; P81282; -.
DR   SMR; P81282; -.
DR   STRING; 9913.ENSBTAP00000019848; -.
DR   PaxDb; P81282; -.
DR   PeptideAtlas; P81282; -.
DR   PRIDE; P81282; -.
DR   Ensembl; ENSBTAT00000042717; ENSBTAP00000040348; ENSBTAG00000014906. [P81282-4]
DR   GeneID; 282662; -.
DR   KEGG; bta:282662; -.
DR   CTD; 1462; -.
DR   eggNOG; ENOG410IFXS; Eukaryota.
DR   eggNOG; ENOG410ZPDG; LUCA.
DR   GeneTree; ENSGT00940000156102; -.
DR   HOGENOM; HOG000168523; -.
DR   HOVERGEN; HBG051140; -.
DR   InParanoid; P81282; -.
DR   KO; K06793; -.
DR   OrthoDB; 74642at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; 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:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; 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   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 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; IPR013032; EGF-like_CS.
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   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; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF56436; SSF56436; 3.
DR   SUPFAM; SSF57535; SSF57535; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Lectin; Phosphoprotein; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   3381       Versican core protein.
FT                                /FTId=PRO_0000017521.
FT   DOMAIN       21    147       Ig-like V-type.
FT   DOMAIN      151    246       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      252    348       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN     3074   3110       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3112   3148       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     3161   3275       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     3279   3339       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      349   1336       GAG-alpha (glucosaminoglycan attachment
FT                                domain).
FT   REGION     1337   3074       GAG-beta.
FT   MOD_RES    2109   2109       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13611}.
FT   MOD_RES    2607   2607       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62059}.
FT   MOD_RES    2608   2608       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62059}.
FT   MOD_RES    2612   2612       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P13611}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    817    817       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    965    965       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1017   1017       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1333   1333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1393   1393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1437   1437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1463   1463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1653   1653       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1974   1974       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2045   2045       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2074   2074       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2103   2103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2263   2263       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2290   2290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2356   2356       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2623   2623       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2641   2641       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2919   2919       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3052   3052       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3354   3354       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3364   3364       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     44    131       {ECO:0000250}.
FT   DISULFID    173    244       {ECO:0000250}.
FT   DISULFID    197    218       {ECO:0000250}.
FT   DISULFID    271    346       {ECO:0000250}.
FT   DISULFID    295    316       {ECO:0000250}.
FT   DISULFID   3078   3089       {ECO:0000250}.
FT   DISULFID   3083   3098       {ECO:0000250}.
FT   DISULFID   3100   3109       {ECO:0000250}.
FT   DISULFID   3116   3127       {ECO:0000250}.
FT   DISULFID   3121   3136       {ECO:0000250}.
FT   DISULFID   3138   3147       {ECO:0000250}.
FT   DISULFID   3154   3165       {ECO:0000250}.
FT   DISULFID   3182   3274       {ECO:0000250}.
FT   DISULFID   3250   3266       {ECO:0000250}.
FT   DISULFID   3281   3324       {ECO:0000250}.
FT   DISULFID   3310   3337       {ECO:0000250}.
FT   VAR_SEQ     349    349       P -> R (in isoform V1 and isoform V3).
FT                                {ECO:0000303|PubMed:9624174}.
FT                                /FTId=VSP_003078.
FT   VAR_SEQ     350   3074       Missing (in isoform V3).
FT                                {ECO:0000303|PubMed:9624174}.
FT                                /FTId=VSP_003081.
FT   VAR_SEQ     350   1336       Missing (in isoform V1).
FT                                {ECO:0000303|PubMed:9624174}.
FT                                /FTId=VSP_003079.
FT   VAR_SEQ    1337   3074       Missing (in isoform V2).
FT                                {ECO:0000303|PubMed:9624174}.
FT                                /FTId=VSP_003080.
FT   CONFLICT     25     25       Missing (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       Missing (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       N -> D (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     96     96       Q -> D (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    346    346       C -> R (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3381 AA;  369990 MW;  F09716FA7778D459 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 TLLEELQVGL 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 KTETDIDREY FTTSSTSTTQ PTRPPTVEGK EAFGPQAFST PEPPAGTKFH
     PDINVYIIEV RENKTGRMSD FSVSGHPIDS ESKEDEPCSE ETDPEHDLIA EILPELLGML
     HSEEDEEDEE CANATDVTTT PSVQYINGKH VVTTVPKDPE AAEARRGQFE SVAPSQNFSD
     SSESDSHQFI ITHAGLPTAM QPNESKETTE SLEITWRPEI YPETAEPFSS GEPDIFPTAS
     IHEGEATEGP DSITEKNPEL DHLVHEHAES VPLFPEESSG DAAIDQESQK IIFSGATEGT
     FGEEAEKSST THTPSMVASS VSAPVSEDAS FILTGTPQSD EPLSTVESWV EITPRHTVEF
     SGSPSIPIPE GSGEAEEDKD KIFAMITDLS QRNTTDPRVT SDTSKIMITE SLVDVPTTTI
     YSISEQVSAV VPTKFVRETD TYEWVFSPPL EETTRKEEEK GTTGTASTVE VHSPTQRLDQ
     FVSPSELESS SETPPDDSAA ATRKSFTSQM TPTQSERETT SSTVVFKETE VLDNLAAQTT
     DPSLSSQPGV LEVSPTVPGS PVSLFMEQGS GEAAVDPETT TVSSLSLNIE PEILAKEEAA
     GAWSPNVETV FPFEPTEQVL STAVDREVAE TISQTSKENL VSEISGEPTH RAEIKGFSTD
     FPLEEDFSGD FREYSTVSYP ITKEEIVMME GSGDAAFKDT QMLPSVTPTS DLSNHTADSE
     EPGSTLVSTS AFPWEEFTAS AEGSGEPLLS VSSSVDQVFP SAAGKASGTD SPFIDQRLGE
     EGAINETDQR STILPTAEAE STKASTEEGE VKENHTVSMD FPPTVEPDEL WPRQEVNPVR
     QGNGSEIVSE EKTQEQESFE PLQSSVAPEQ TTFDSQTFPE PGLQTTGYFT LTTKKTYSTD
     ERMEEEVISL ADVSTPTLDS KGLVLYTTLP EVTEKSHFFL ATASVTESVP AESVIAGSTI
     KEEESIKPFP KVTSPIIKES DTDLIFSGLG SGEEVLPTLG SVNFTEIEQV LSTLYPLTSQ
     VQSLEASILN DTSGDYEGME NVANEMRPLI SKTDSIFEDG ETASSTTLPE ILSDARTEGP
     FTAPLTFSTG PGQPQNQTHR RAEEIQTSRP QPLTDQVSSE NSVTAETKET ATPATDFLAR
     TYDLEMAKGF VTPTPKPSDL FYEHSGEGSG ELDAVGAEVH ASGMTQATRQ GSTTFVSDRS
     LEKHPKVPSV EAVTVNGFPT VSMVLPLHPE QREGSPEATG TPASTASYEK ATEGAADSFQ
     DHFWGFKDST LKPDKRKATE SIIIDLDKED KDLILTMTES TILEIIPELT SDKNTVIDID
     HTKPIYEDIL GMQTDLDPEV PSGPPDSSEE STQVQEKYEA AVNLSSTEEN FEASGDILLA
     NYTQATPESK APEDRNPLDH TDFIFTTGIP ILSSETELDV LLPTATSLPI PSKSATVNPE
     SKTEAKTLED IFESSTLSDG QAIADQSEVI STLGYLERTQ NEDEAKKYVS PSFQPEFSSG
     AEEALTDPTP YVSIGTTYLT AQSLTEAPDV MEGARLPDSI DTSTVSAFSE LLSQTPSFPP
     LSIHLGSGDS EHSEDLQPSA LPSTDASTPP VSSGELANIE ATFKPSSEED FYITEPPSLP
     PDTEPSEDES KPKLLEPTEA SATELIAQEE IEIFQNSDNT TSVQVSGEAV KVFPSIETPE
     AEAIVTAASE TKLEGATLRP HSTSASVIHG VEAGVVPQPS PQTSERPTIL SPLEISPETQ
     AALIRGEDST VAAPKQQVPT RMLDSNKQAT LSTTELNTEL ATPSFPLLET SNETSFLIGI
     NEESVEGTAV YLPGPDRCKM NPCLNGGTCY PTETSYVCTC VPGYSGDRCE LDFDECHSNP
     CRNGATCIDG FNTFRCLCLP SYVGALCEQD TETCDYGWHK FQGQCYKYFA HRRTWDAAER
     ECRLQGAHLT SILSHEEQMF VNRVGHDYQW IGLNDKMFEH DFRWTDGSTL QYENWRPNQP
     DSFFSTGEDC VVIIWHENGQ WNDVPCNYHL TYTCKKGTVA CGQPPVVENA KTFGKMKPRY
     EINSLIRYHC KDGFIQRHLP TIRCLGNGRW AMPKITCLNP SAYQRTYSKK YFKNSSSAKD
     NSINTSKHDH RWSRRWQESR R
//
DBGET integrated database retrieval system