ID A0A3B3BI63_ORYME Unreviewed; 623 AA.
AC A0A3B3BI63;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000005170.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000005170.1}
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 -!- 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3B3BI63; -.
DR STRING; 30732.ENSOMEP00000005170; -.
DR PaxDb; 30732-ENSOMEP00000005170; -.
DR Ensembl; ENSOMET00000007935.1; ENSOMEP00000005170.1; ENSOMEG00000006164.1.
DR GeneTree; ENSGT00940000156102; -.
DR OMA; CFGDMMG; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 2.
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; 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 PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF6; VERSICAN CORE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
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; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..149
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 251..348
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 349..385
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 387..423
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 436..550
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 554..614
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 197..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 295..316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 375..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 556..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 585..612
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 623 AA; 70381 MW; B144C2B0535E7DBA CRC64;
MVLNIRHVLW LYCLFPSIFF LKSLLVTPPQ PVTGSLSGKV TLPCFFSTIP TSAPVISPNG
AIIYGRDSLR IKWTKMEGNT ESVVLVAQEG MIKIDSSYRN RVSVPSHPED VGDASLTMVK
LRASDAGTYR CEVLYGIEDT QDTVSLDVSG VVFHYRAKTS RYTLDYQKAV QACKDIGATI
ATYDQLKAAY EDGFDQCDAG WMADQTVRYP ITRPRKGCFG NLMTKPGIRS YGIRKLTETY
DVYCYVDKLD GEVYYAPVTR KMTFQEASEE CKKRNAVLAS PGQLHAAWRQ GLDRCDYGWM
SDGSVRHPVA VSRIQCGGGL LGVRTMYRYR NQTGFPEPTM KLGAYCFKGL YSCAKNICLN
GGSCYKSGSV LSCSCAPGYT GPLCENDIDE CQSNPCRNGG TCVDGLASFS CVCLPSYTGL
FCESDTETCE YGWHKFQGHC YKHSPQRKNW DSAERECRIQ GAHLTSILSH EEQQFVNRLG
QDYQWIGLND KMFQNDFRWT DGSVVQYEHW RPNQPDSFFS TGEDCVVMIW HEDGQWNDVP
CNYHLTYTCK KGTVACSQPP VVENARTYGK KRERYEINSL VRYRCQTGFI QRHVPTIRCR
GDGRWDVPKI TCLNRKYIFC ISS
//
