ID A0A3B3RXQ2_9TELE Unreviewed; 723 AA.
AC A0A3B3RXQ2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cartilage oligomeric matrix protein {ECO:0000313|Ensembl:ENSPKIP00000023232.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000023232.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000023232.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
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; A0A3B3RXQ2; -.
DR Ensembl; ENSPKIT00000003911.1; ENSPKIP00000023232.1; ENSPKIG00000006912.1.
DR GeneTree; ENSGT00940000166148; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; CARTILAGE OLIGOMERIC MATRIX PROTEIN; 1.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 87..124
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 184..224
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 258..293
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 317..352
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 454..489
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 493..707
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 339..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 78781 MW; 90C41692140AA79D CRC64;
MYCLVCTIVL IELTNHPAVF FQIKEIIFLK NTVMECESCG MRNDRPPQPS CVPSPCHPGV
PCMETGGGVK CGPCPEGMVG NGTHCTDVDE CIMKPCHKGA LCTNTAPGFH CGPCPAGYTG
PQVQGAGLSY ATANKQVCKD INECEGDTNG GCVANSICTN TPGSFRCGPC KLGYVGDQQR
GCKLEKSCGE SNPCHRNADC IVHRDGTIQC VCGVGWAGDG YVCGPDIDID GVPDQQLDCP
QKSCVKDNCL TVPNSGQEDA DRDGIGDACD EDADGDGIFN VEDNCVLVAN VNQRNVDQDD
FGDACDNCRL MTNNDQKDTD GDGNGDACDD DIDGDGIPNN IDNCKVVPNT DQKDRDGDKV
GDACDSCPYV RNPDQMDIDN DLIGDPCDTN KDSDGDGHQD SRDNCPAVIN SSQLDTDRDG
LGDECDDDDD NDGIPDLLPP GPDNCRLVPN PLQEDSDGDG IGNLCENDFD NDTFVDTIDV
CPENAEVTLT DFRAFQTVVL DPEGDAQIDP NWVVLNQGRE IVQTMNSDPG LAVGYTAFNG
VDFEGTFHVN TMTDDDYAGF IFGYQDSSSF YVVMWKQVEQ IYWQANPFRA VAEPGIQLKA
VKSGTGPGEH LRNSLWHTGD TGGQVRLLWK DSRNVGWKDK TSYRWFLQHR PHDGYIRVRF
YEGPKMVADS GIIIDTTMRG GRLGVFCFSQ ENIIWADLRY RCNDTTPEDF ETYRIQQIQL
SPQ
//
