ID A0A2K6GZB1_PROCO Unreviewed; 1616 AA.
AC A0A2K6GZB1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ENSPCOP00000031612.1};
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:ENSPCOP00000031612.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000031612.1}
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 Ensembl; ENSPCOT00000042570.1; ENSPCOP00000031612.1; ENSPCOG00000028583.1.
DR GeneTree; ENSGT00940000156102; -.
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..1616
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014414565"
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 1309..1345
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1347..1383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1396..1510
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1514..1574
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 1243..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1616
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 DISULFID 196..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 294..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1335..1344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1373..1382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1516..1559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1545..1572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1616 AA; 179890 MW; 99AF8249CCF1740F 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 IEVRENKTGP DRCKTNPCLN
GGTCYPTETS YVCTCVPGYS GDRCELDFDE CHSNPCRNGA TCIDGFNTFR CLCLPSYVGA
LCEQDTETCD YGWHKFQGQC YKYFAHRRTW DAAERECRLQ GAHLTSILSH EEQMFVNRVG
HDYQWIGLND KMFEHDFRWT DGSTLQYENW RPNQPDSFFS AGEDCVVIIW HENGQWNDVP
CNYHLTYTCK KGTVACGQPP VVENAKTFGK MKPRYEINSL IRYHCKDGFI QRHLPTIRCL
GNGRWAMPKI TCMNPSAYQR TYSKKYFKNS SSEKDNSSNT SKHEHRWIRR WQESRR
//
