ID A0A3Q7RUK8_VULVU Unreviewed; 3402 AA.
AC A0A3Q7RUK8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|RefSeq:XP_025848723.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025848723.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025848723.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025848723.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025848723.1};
RG RefSeq;
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 RefSeq; XP_025848723.1; XM_025992938.1.
DR STRING; 9627.ENSVVUP00000032019; -.
DR OrthoDB; 5323609at2759; -.
DR Proteomes; UP000286640; 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: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; 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; 2.
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:UP000286640};
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..3402
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018565380"
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 3095..3131
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3133..3169
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3182..3296
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 3300..3360
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 586..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2041..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2324..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2507..2550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2652..2674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2704..2723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2838..2941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3376..3402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1975..1990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2332..2370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2383..2410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2507..2532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2533..2550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2652..2666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2706..2720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2879..2894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2927..2941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3384..3402
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 3121..3130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3159..3168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3302..3345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 3331..3358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 3402 AA; 369140 MW; D06A396A1AB91B14 CRC64;
MLINIKGILW MCSTLIAAHA LHKAKVEKSP PVKGSLSGKV NLPCHFSTMP TLPPSYNTSS
EFLRIKWSKI ELDKNGKDLK ETTVLVAQNG NVKIGQGYQG RVSVPTHAEV VGDASLTVVK
LHASDAGLYR CDVMYGIEDT QDTVSLAVDG VVFHYRAATS RYTLNFEAAQ KACLDIGAVI
ATPEQLYAAY EDGFEQCDAG WLSDQTVRYP IRAPRVGCYG DMMGKEGVRT YGFRSPHETY
DVYCYVDHLD GDVFHITAPN KFTFEEAEEE CENQDARLAT VGELQAAWRN GFDQCDYGWL
SDASVRHPVT VARAQCGGGL LGVRTLYRFE NQTGFPPPDS RFDAYCFKPK QNISEATTIE
LNILAETASS SFSEELHMVP DRTTPVIPLI TELPIITTKF PPVGNIVNFE QKTTVQAQAI
THGVATESST PAGSTMKPGD MDYYSPSGSG PLGKADIPEI QKEVPQSTTV VSHHATESWD
DVWEDIQTQE SVTQVEQIEV GPLVTSMEVF KHVPSKELSI TETPFVSTTM TLESKTEKKT
VITVSESVTT SRYGFTLGED DSEDSTVTVR STQSTLAFSQ VPEVVTVSKT SEDTASTPPE
DREQVSASTI LSPVTVPDSD GSSTDTWEER QTNGRKTEDV FGPYASTTPF PSQHHTEVEL
FPYSGDKKLV EGIPTVIYPS PRTEMAQGRE RTETLSPEMR TDTYTDDEIQ EKITKDPFIG
KIEEEGFSGM KFSTASSEEI HLTESSVEMT KSFDSPTPTT AKLSVVPTEA RDIEEDLTTT
PAELETDGYQ DTTKYDEGVT TVPLSHSTVS VEVVTVSKWA WDEDDTTVKP LESTEDAGPP
KLPPALLTTT EVSGKDKEIP SFTEDVGDEF TLVPDSTQKP LEEFTEEDST DHGKFTVGFQ
PTTLIGISEK PTLRDSTPEE RVPPVTSVEG QVIYATTEGS ALDEEAMDVS EPVSTISQFV
HTSDVEGLAF VNYSSTQEPT TYVDSSHTIP LSVIPKTEWG VLVPSVPPED EVLGEPSQDI
RVINQTQLEA TLFPETIRTA TEATQGTSLE EFPWKEQTTE KPVPALSSTA ATAKEAATPM
GKEESDRTAY TVSEDRLVTA SERAPGLETT PVGKIEHAMS HPPGAVTEHK AETDEMVTRT
PSIGPTVSLS PEPEQKHETE SASPGGFVSP YSTHVTQLTE ETTTEKREKT SLDYTDLGSG
LFERPIATEL PEFSTAKATV PSDFTAAFSS VERLHTTSAS KPSSAPTEKP PLIDREPGEE
TTSDMVIIGE STSRVPPTTL EDVVGKETET DIDREYFTTS STPSATQPAR PPTVEGQEAL
GPQALSTPEP PAGTKFRPDI NVFVIEVREN KTGRMSDLSV IGHPIDSESK EDEPCSEETD
PEHVLSLPEL IEITLYHSEE DEEEDEECTN ATDVTTTPSV QYINGKQLVT TVPKDPEAAE
ARRGQFESVA PSQNFSHSSE SETHPFVVAE NGLSTAVQPN ESKETTESLE LTWRPETYPE
TPEHFSGGEP DVFPTVPFHE GEATDGPESA PERGLELDNL VHEPIEHVPL FSEESSGDAA
TDQESQKMIS SKATEVTFGE EAEKSTSVTP APNVVPSSVS ADVSEEVSVT FTRNVLPHGP
LSTVESWVEI APQENVELSG SPSIPFPEGS GETEEDTNTM FTVATDLSQR NITDTLVSLA
TSKTMITESL SDIPATTFHS SSQQPSTEVA PTKFVGETDT PEWVFRPPLE GKRRKEEEEE
GTTGTASTVQ VHVSTQRSDQ LILPSDLESS SEVTTSHSAS ATRNSLMSST KPTQPEKAMT
SSALVSTETS VLDHLGAQTA KPSSSSQPGF QEGLSTLPGR PISFSLEPGS GEAAADPETA
TVASFSLNLE SGIPTEKEAA GTLSPHVETI FPFEPTGLVL STVIDREVAD ITSQTLKENL
ISEVSGEQNH GPEIKGFSTD FPLEEDFSGD FREYSTVTYP TEEETVMMEG SGDAASKDTQ
ISSSVVPASD HSNHRADPEG PSSTSVSTSA FPWEELTASA EGSGEELVSA STSVDQVFPS
TMGNASGTDS PFIDQGLGEE GAINDANKRS TVLPTAEAEG TEAATTEGEV RVDGTVSVTF
PQTMEPAKLW SLQEINPVQQ GTESETASEE EIEEPNSFES PQSSVAPGQI NFDSQTFTET
GLRTTDYSAL TMKRTDSIGE EMEKEGISFT DVSSPDPDAT GLGPYTALPE VTEKSHLFLA
TTSVTESVSA ESVVTDSPVE KEETIKPFPK VVTPIIKEAD TDLLFSGLGS GEEVLATTVP
VNFTEMEQII STLYPQVSQM ESSETSHISN TTEDYEGMEN VAHEVGPPIS KTDSLSEDSE
TASSTTLLEI VSDTTTAGPS TAPLTFSTDA EHPQHETHGW AEEIQTSRPQ PMTEPVSNEN
SPTAETKETA TPPSDFLART YGLEMAKGFV TSAPKPSDLL YEHSGEGSGE LDMVDLVHTS
GTTQASRQGS TTFVSDRSLE KHPEVPSAKA VTVDGFPTVS VLLPLHVEQN ESSPAPTSTL
SSTRSYERST EGAADSFQDH VRGFEDSTVK PNRRKTTENI IIDLDKEDKD LILTITESTI
LEHLPELTSD KNTIIDIDHT KPIYVDILGM QTDIDPEVLA GPHGSSEESA QVQEKYEAAV
NLSLTEENFE GSGDTLLAND TQTTHSESMP SEDRSRLDHM GFIFTTRIPV PSTETELDML
LPTATSLPIP SPSATVTPET EEPKSEAKAL DDTFESSTLS DGQAIADQSE VISTLGHLEP
RDEYEEKKYV APSFQPEFSS GAEEALIDPT PYVSIGTIHH MAQSLTEAPN VIEGSNPSDD
TDTTSAASAF AKLSFQTPSS PLTGYVGGGA SEQAEGPQAG AVPGTVAGIA HRSPGKLADT
EVTFTSSSKE PFHITEPPSL SPDTGLEPSE DESNPKLLEP TEASPTKPTA EEGTEILQGS
QTQTNIQLSG ETMKNHVRTP QAGTVVTTAG EIKLEGATLW PHSTSASAVY GVEADVMPQP
SPQTSERPTV PSSLEINPET QAALIGGEDY TVAASDQQVS ARILDPNNQA TVSIAELHTE
LATPSFSLLE TSNETGFLIG INEESVEGTA VYLPGPDRCK TNPCLNGGTC YPTETSYVCT
CVPGFSGDQC ELDFDECHSN PCRNGATCVD GFNTFRCLCL PSYVGALCEQ DTETCDYGWH
KFQGQCYKYF AHRRTWDAAE RECRLQGAHL TSILSHEEQM FVNRVGHDYQ WIGLNDKMFE
HDFRWTDGST LQYENWRPNQ PDSFFSAGED CVVIIWHENG QWNDVPCNYH LTYTCKKGTV
ACGQPPVVEN AKTFGKMKPR YEINSLIRYH CKDGFIQRHL PTIRCLGNGR WAMPKITCMN
PSAYQRTYSK KYFKNSSSAK DNSINTSKHD HRWSRRWQES RR
//
