ID A0A2K6G784_PROCO Unreviewed; 756 AA.
AC A0A2K6G784;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cartilage oligomeric matrix protein {ECO:0000313|Ensembl:ENSPCOP00000022086.1};
GN Name=COMP {ECO:0000313|Ensembl:ENSPCOP00000022086.1};
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:ENSPCOP00000022086.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000022086.1}
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 RefSeq; XP_012509543.1; XM_012654089.1.
DR AlphaFoldDB; A0A2K6G784; -.
DR STRING; 379532.ENSPCOP00000022086; -.
DR Ensembl; ENSPCOT00000032757.1; ENSPCOP00000022086.1; ENSPCOG00000023117.1.
DR GeneID; 105818166; -.
DR CTD; 1311; -.
DR GeneTree; ENSGT00940000162169; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0036122; F:BMP binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:1990079; P:cartilage homeostasis; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0050881; P:musculoskeletal movement; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1900047; P:negative regulation of hemostasis; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0035989; P:tendon development; IEA:Ensembl.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16077; TSP-5cc; 1.
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; IPR039081; TSP-5_cc.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; CARTILAGE OLIGOMERIC MATRIX PROTEIN; 1.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR Pfam; PF11598; COMP; 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; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
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; 4.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..756
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014437356"
FT DOMAIN 126..163
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 179..218
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 300..335
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 359..394
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 456..491
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 492..527
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 531..745
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 297..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..65
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 82550 MW; 7D6E3BFF7C6B4FA5 CRC64;
MAPAAACLLL LTLTALGASG QGQMALGSDL APQMLRELQE TNAALQDVRE LLRQQVKEIT
FLKNTVMECD ACGMQPARTP GLSVRPLLHC APGFCFPGVA CTQTASGARC GPCPEGFTGN
GSHCTDINEC NAHPCFPRVR CINTSPGFRC EACPPGYSGP THEGVGLAFA KANKQVCTDI
NECETGQHNC VPNSVCINTR GSFQCSPCQP GFVGDQASGC HRREQRLCPD GSPSQCHEKA
DCVLERDGSR SCVCAVGWAG NGILCGRDTD LDGFPDEKLR CPERQCRKDN CVTVPNSGQE
DVDRDGIGDA CDPDADGDGV PNEGDNCPLV RNPDQRNTDG DKWGDACDNC RSQKNDDQKD
TDRDGRGDAC DDDIDGDRIR NPVDNCPRTP NSDQKDTDGD GIGDACDNCP RKSNPDQSDV
DQDFVGDACD SDQDQDGDGH QDSMDNCPTV PNSAQQDSDH DGQGDACDDD DDNDGVPDSR
DNCRLVANPG QEDADRDGVG DVCQGDFDAD KVVDKIDVCP ENAEVTLTDF RAFQTVVLDP
EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD FEGTFHVNTA TDDDYAGFIF
GYQDSSSFYV VMWKQMEQTY WQANPFRAVA EPGIQLKAVK SSTGPGEQLR NALWHTGDTE
SQVRLLWKDP RNVGWKDKTS YRWFLQHRPQ VGYIRVRFYE GPELVADSNV ILDTTMRGGR
LGVFCFSQEN IIWANLRYRC NDTIPEDYEM QRLRRA
//
