ID A0A2K6KUN6_RHIBE Unreviewed; 2409 AA.
AC A0A2K6KUN6;
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:ENSRBIP00000014991.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000014991.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000014991.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000014991.1}
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; ENSRBIT00000038831.1; ENSRBIP00000014991.1; ENSRBIG00000031473.1.
DR GeneTree; ENSGT00940000156102; -.
DR Proteomes; UP000233180; 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; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000233180};
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..2409
FT /note="Versican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014477954"
FT DOMAIN 33..145
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 149..244
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 250..346
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 2102..2138
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2140..2176
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2189..2303
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2307..2367
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 436..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2384..2409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2391..2409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 195..216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 293..314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2128..2137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2166..2175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2309..2352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2338..2365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 2409 AA; 265050 MW; EC63B6D056DAD10E CRC64;
MLININSILW MYSTLIATHA LHKVKVKSPP VRGSLSGKIS LPCHFSTLPT LPPSYNTSEF
LRIKWSKIEV DKNGKDLKET TVLVAQNGNI KIGQDYKGRV SVPTHPEAVG DASLTVVKLL
ASDAGLYRCD VMYGIDDTQD TVSLAVDGVV FHYRASTSRY TLNFEAAQKA CLDIGAVIAT
PEQLFAAYED GFEQCDAGWL ADQTVRYPIR APRVGCYGDM MGKAGVRTYG FRSPQETYDV
YCYVDHLDGD VFHLTAPSKF TFEEAAKECE NQDARLATVG ELQAAWRNGF DQCDYGWLSD
ASVRHPVTVA RAQCGGGLLG VRTLYRFENQ TGFPPPDSRF DAYCFKRRMS DLSVIGHPID
SESKEDEPCS EETDPVHDLM AEILPEFPDI IEIDLYHSEE NEEEEEECAN ATDVTTTPSV
QYINGKHLVT TVPKDPEAAE ARRGQFESVA PSQNFSDSSE SDTRPFVIAE TELSTAVQPN
GSTETTESLE ITWKPETYPE TSEHFSGGEP DVFPTVPFHE EFESGTAIKG AESVTERDTE
VGHQAHEHIE PISLFPEESS GEIAIDQESQ KIAFARPTEV TFGEEVEKST SVTYTPTVVP
SSVSAYVSEE KAVTLIGNPW PDDLLSTKES WVEATPRQVV ELSGSSSIPI TEGSGEAEED
EDTMFTMVTD LSQRNTTDTL ITLDTSRIIT ESFFEVPATT IYSVSEQPSA KVVPTKFVSE
TDASEWISST SVEEEKRKEQ EGTTGTASTV EVYSPTQRLD QLILPSELES SNVVASSDSS
TRKSFMSLTT PTQSEREMTD STLVFTETNT LENLEAQTTE HSSIHQPGVQ EGVTTLPGSP
ASFFMEQGSG EAAADPETTT VSSFSLNLEY EIQAKKEAAG TLSPHVETTF STEPTGLVMS
TVMDREVAEN ISQTAREILI SERLGEPNHG AEIRGFSTGF PLEEDFSGDF KEYSTMSHPI
AKEETVMMEG SGDAAFRDTQ TSPSTVPTSV HISHISDSEG PSSTMVSTSA FPWEEFTSSA
EGSGEQLATV SSSVDPVLPS AVGKFSGTAS SIIDEGLGEV DTVNEIDRRS TILPTAEVEG
TKAPVEKEEV KVSGTISTNF PQTMEPAKLW SRQEANPERQ EIESETTSEE QIQEEKSFES
PQNSPATEQT IFDSQTFTET ELKTTGYSVL TTKKTYSDDK EMEEEGTSLA NMSTPDPVAN
GMESYTTLPE ATEKSHFFLA TALVTESIPA EHVVTDSPIK EEESTKHFPK GMRPTIQESD
TELLFSGLGS GEEVLTTLPT KSVNFTEVEQ IRNTFYPHSS QVESTSSDKT EDSNRMENVV
KEVGPLVSQT DTFEGNESVT STTLIETLSD TGAEGPTVAP LPFSMNIGHP QNQTLRWAEE
IQTSRLQTIT EQDSNKNSST AEINETTTSS TDFLARAYGF EMAKEFVTSA PKPSDMFYEP
SGEGSGEVDI VDSFHTSATT QATRQESSTT FVSDGSPEKH PEVPSTKAVT ADGFPTVSAM
LPLHSEQNKS SPDPTSTLSN TVSYERSTDG SFQDHFREFE DSTLKPNRKK PTENIIIDLD
KEDKDLILTI TESTILEILP ELTSDKNTII DIDHTKPVYE DILGMQTDID PEVPSEPHDS
NDESNDDSTQ VQETYEAAVN LSLTEETFEG SGDVLLASYT QATHDESMTY EDRSQLDHMD
FNFTTGIPAP STETELDILL PTATSLQIPR KSATVIPETE EIKAEAKALD DMFESSTLSD
GQAIADQSEI IPTLGQFERT QEEYEDKKHA GPSFQPEFSS GVEEALVDHT PYLSIATTHL
VDESLTEVPH VMEGSNAPYY TDTTLAVSTF AKLSSQTPSS PLTIYSGSEA SGHTEIPQPS
ALPGIDVGSS VMSPEDSFKE IHVNIEATFK PSSEEYLHIT EPPSLPPDTK LEPSEDDGKP
ELLEETEASP TELIAVEGTE ILQDFQNKTD GQVSGEAIKM FSTIKTPEAG TVITTANEIK
LEGATQWPHS TSASATYGVE AGVVPWLSPQ TSERPTLSSS PEINPETQAA LIRGQDSTVA
ASEQQVAARI VDSNNQATVS PVEFNTEVAT PPFSLLETSN ETDFLIGINE ESVEGTAIYL
PGPDRCKMNP CLNGGTCYPT ETSYVCTCVP GYSGDQCELD FDECHSNPCR NGATCVDGFN
TFRCLCLPSY VGALCEQDTE TCDYGWHKFQ GQCYKYFAHR RTWDAAEREC RLQGAHLTSI
LSHEEQMFVN RVGHDYQWIG LNDKMFEHDF RWTDGSTLQY ENWRPNQPDS FFSAGEDCVV
IIWHENGQWN DVPCNYHLTY TCKKGTVACG QPPVVENAKT FGKMKPRYEI NSLIRYHCKD
GFIQRHLPTI RCLGNGRWAI PKITCMNPSA YQRTYSMKYF KNSSSAKDNS INTSKHDHRW
SRRWQESRR
//