GenomeNet

Database: UniProt
Entry: W5Q233_SHEEP
LinkDB: W5Q233_SHEEP
Original site: W5Q233_SHEEP 
ID   W5Q233_SHEEP            Unreviewed;      3375 AA.
AC   W5Q233;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Versican {ECO:0000313|Ensembl:ENSOARP00000016771.1};
GN   Name=VCAN {ECO:0000313|Ensembl:ENSOARP00000016771.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016771.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000016771.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016771.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000016771.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
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   EMBL; AMGL01094251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004009116.1; XM_004009067.3.
DR   SMR; W5Q233; -.
DR   STRING; 9940.ENSOARP00000016771; -.
DR   PaxDb; 9940-ENSOARP00000016771; -.
DR   Ensembl; ENSOART00000017009.1; ENSOARP00000016771.1; ENSOARG00000015632.1.
DR   GeneID; 100294605; -.
DR   KEGG; oas:100294605; -.
DR   CTD; 1462; -.
DR   eggNOG; ENOG502QRBE; Eukaryota.
DR   HOGENOM; CLU_000303_1_1_1; -.
DR   OMA; ELTWKPE; -.
DR   OrthoDB; 5323609at2759; -.
DR   Proteomes; UP000002356; Chromosome 5.
DR   Bgee; ENSOARG00000015632; Expressed in mitral valve and 51 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: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   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   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
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..3375
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004869736"
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          3068..3104
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3106..3142
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3155..3269
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          3273..3333
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          417..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..865
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          1219..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1414..1539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1707..1760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1795..1818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1954..1984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2038..2087
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2099..2138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2312..2389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2593..2614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2815..2898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3350..3375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..617
FT                   /note="Polar residues"
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        1219..1233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1430..1469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1508..1532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1722..1760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1956..1984
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2041..2058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2059..2073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2115..2138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2316..2332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2341..2389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2831..2850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2866..2882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3357..3375
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        3094..3103
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3132..3141
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3275..3318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        3304..3331
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   3375 AA;  368506 MW;  98977C685F13D130 CRC64;
     MLINIKSILW MCSTLIAAHA LQKVNMEKSP SVKGSLSGKV NLPCHFSTMP TLPPSYNTTS
     EFLRIKWSKI ELDKTGKDLK ETTVLVAQNG NIKIGQDYKG RVSVPTHPED VGDASLTMVK
     LLASDAGRYR CDVMYGIEDT QDTVSLTVEG VVFHYRAATS RYTLNFEMAQ KACVDIGAVI
     ATPEQLHAAY EDGFEQCDAG WLSDQTVRYP IRVPREGCYG DMMGKEGVRT YGFRAPHETY
     DVYCYVDHLD GDVFHITAPN KFTFEEAGEE CKNQDARLAT VGELQAAWRN GFDRCDYGWL
     LDASVRHPVT VARAQCGGGL LGVRTLYRFE NQTGFPPPDS RFDAYCFKPK QNISEATTIE
     LNMLAETVSP TLLEELQMGP DRTTPIVPLI TELPVTTTKV PAIGNIVNIE QKSTVQPLTS
     THRSAAESLP PDGSTKKPWD MDYYSPSASG PLGEPDISEI KEEMPQSTTV ISHHAPESWD
     SVKEDLQRKE SVTQVEQIEV GPLVTSMEIS KHMPSKEFTV TATPFVSTTM TLESKTAKKA
     ISTVSEPVTT SHYGFTLRED DGQDRTSTVR SGQRTSIFSQ IPEVITVSKT SEDTTRSQLE
     DVESVPASTV VSPDSDGSSM DHRQEKQTHG RIIEDFLGQY VSTTPFPSQH HTEVELFPFS
     GDKRLVEGTS TVISPSPRTG RESTETLRPA MRTVTYTNDE IQEKITKDSF IEKIEEEGFS
     GMKFPTASPE QIHHTEYSVG MTKSFESPAL TTTTKLGVIP TEATGVEEDF TTPGGLETDG
     YQDTTKYEEG IATVHLIQST LNVEVVTVSK WSLDEDNTTS KPLWSTEHVG SPKLPPALIT
     TTGVSGKDKE MPSLTEDGRD EFTHIPGSIQ KPLEEFTEED TIDHEKFIVR FQPTTSIATT
     EKSTLRDSIT EERVAPFTST EVRVTHATTE GSALDEGQDV DVSKPLSTVP QFAHPSDVEG
     STFVNYSSTQ EPTTYVDTSH TIPLSVIPKT EWGVLVPSLP SEGEVLGEPS QDIRVINQTH
     FEASIYPETV RTTTEIIQEA TGEDFPWKEQ TPEKPVSPPR STTDTAKETL PLDEQESDGS
     AYTVFEDRSV TGSDRVSVLV TTPIGKFEQS TSFPPGAVTK AKTDDVVTLT PTTGSKVTFS
     PWPEQKYETE GTSPRGFVSP FSIGVTQVIE ETTPEKREKT SLDYTDLGSG LFEKPKATEL
     PEFSTVKATV PSDITAAFSS ADRFHTPSSS TEKPPLIDRE PDEETTSDMV IIGESTSRVP
     PTTLEDIVAK ETETDIDREY FTTSSTSTTQ PTRPPTVEGK EAFGPQAFST PEPPAGTKFH
     PDINVYIIEV RENKTGRMSD LSVIGHPIDS ESKEDEPCSE ETDPEHDLIA EILPELLGML
     HSEEDEEDEE CANATDVTTT PSVQYINGKH VVTTVPKDPE AAEARRGQFE SVAPSQNFSD
     SSESDSHQFI ITHAGLSTAM QPNESKETTE SLEITWRPEI YPETAEPFSS GEPDIFPTAS
     IHEGEATEGP DSVTEKSPEL DHRAHEHTES VPLFPEESSG DAAIDQESQK VIFSGATEGT
     FGEEAEESST THTPSIVASS VSAPVSEDAL FISTGTPQSD EPLSTVESWV EITPRHTVEF
     SGSPSIPIPE GSGEAEEDKD KIFAMITDLS QRNTTDSLVT LDTSKIMITE SLLGVPATTV
     YSTSERVSAA VPTKFVRETD TYEWVFSPPL EETRKDEKGT TGTASTAEVH SPTQRSDQFV
     SPSELESSSD TPPDDSTAAP RKSFLSLMTA TQSERETTSS TVVFTETEVL DNLAAQTTDP
     SLSSQPGVLE GSPTVPGSPT SLFMEQGSGE AALDPETTTV SSPALNLEPE ILAEEEAAGT
     WSPHVETVFP FEPTEQVLST AVDREVAEII SQTSKENLVS ETSGEPTHRA EIKGFSTDFP
     LEEDFSGDFR EYSTVSYPIT KEEIVMMEGS GDAAFKDTQM SPSVTPTSDL SNHSADSEEP
     GSTLVSTSAF PWEEFTASAE GSGEQLLSVS SSVDQVFPSA VGKASGTDSP FIDQRLGEGA
     INETDQRSTI LPTAEAESTK ASTKEEEVKE NHTVSMDFPP TAEPDELWPR QEVNPVRQGN
     GSEIVSEEKT QEQESFEPLQ SSVAPEQTTF DSQTFPEPGL RTTGYFALTT KKTYSTDEKM
     EEEVISLADV STPTLDSKGS ALYTTLPEVT EKSHFFLATA SVTESVPAES VIAGSTIKEE
     ESIKSFPKVT SPIIKESDTD LLFSGLGSGE EVLPTIGSVN FTEIEQVLST LYPPTSQVQS
     LEASILNDTS GDYEGMENVA NENEVRPLIS KTDSVFEDGE TASSTTSPEI LSDARTEGPF
     TAPLTFSTGP GHPQNQTHGR AEEIQPSRPQ PLTDQVSSEN SLTAGTKETA TSSADFLART
     YDLEMAKGFV TSTPKPSDLF YEHSGEGSGE LDAVDAEVHA SGMTQATRQG STTFVSDRPL
     EKHPKVPSVE AVTVDGFPTV SMVLPLHPEQ NEGSPGAAST LASTASYERA TEGAADSFQD
     HFGGFKDSTL KPDRRKATES IIIDLDKDDK DLILTMTEST ILEILPELTS DKNTIIDIDH
     TKPIYEDILG MQTDLDPEAP SGPPESSEES TQVQEKYEAA VNLSSTEENF EASGDILLVN
     YTQATPESKA PEDRNPLDHT GFIFTTGIPI LSSETELDVL LPTATSLPIP SKSATVNPES
     KTEDKTLEDI FESSTLSDGQ AIADQSEVIS TLGYLERTQN EDEEKKYVSP SFQPEFSSGA
     EEALIDPTPY VSIGTTYLTA QSLTEAPDVM EGARLPDSIG TSTISAFAEL LSQTPSSPPL
     SVHLGSGDSE HSEDLQPSAL PSTDASTPPV PSGELANIEA TFKPSSEEGF HTTEPPSLSL
     DTEPSEDENK PKPLEPTEAS ATELIAQEEI EIFQNSHSTT SVQVSGETVK VFPSIETVVT
     AASERKLEGA TLRPHSTSAS VMHGAEAVVV PQPSPQTSEQ PTIPSPLEIN PETQAALIRG
     EDSTVAAPKL QVPTRKLDSN KQATLSTTEL NTELATPSFP PLETSNETSF LIGINEESVE
     GTAIYLPGPD RCKTNPCLNG GTCYATETSY VCTCVPGYSG DRCELDFDEC HSNPCRNGAT
     CIDGFNTFRC LCLPSYVGAL CEQDTETCDY GWHKFQGQCY KYFAHRRTWD AAERECRLQG
     AHLTSILSHE EQMFVNRVGH DYQWIGLNDK MFEHDFRWTD GSTLQYENWR PNQPDSFFST
     GEDCVVIIWH ENGQWNDVPC NYHLTYTCKK GTVACGQPPV VENAKTFGKM KPRYEINSLI
     RYHCKDGFIQ RHLPTIRCLG NGRWAMPKIT CLNPSAYQRT YSQKYFKNSS SAKDNSINTS
     KHDHRWSRRW QESRR
//
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