ID A0A2K5Y0S3_MANLE Unreviewed; 704 AA.
AC A0A2K5Y0S3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cartilage oligomeric matrix protein {ECO:0000313|Ensembl:ENSMLEP00000009120.1};
GN Name=COMP {ECO:0000313|Ensembl:ENSMLEP00000009120.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000009120.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000009120.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011845914.1; XM_011990524.1.
DR AlphaFoldDB; A0A2K5Y0S3; -.
DR Ensembl; ENSMLET00000032519.1; ENSMLEP00000009120.1; ENSMLEG00000028753.1.
DR GeneID; 105547095; -.
DR CTD; 1311; -.
DR GeneTree; ENSGT00940000162169; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008201; F:heparin binding; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
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; 2.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 3.
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; 1.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 3.
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; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..704
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014447426"
FT REPEAT 248..283
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 307..342
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 404..439
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 440..475
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 479..693
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 245..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..65
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 250..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77268 MW; DF912712018B721F CRC64;
MAPDTACVLL LTLAALGASG QSQIPLGSDL GPQMLRELQE TNAALQDVRE LLRQQVREIT
FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV ACIQTESGAR CGPCPAGFTG
NGSHCTDVNE CETGQHNCVP NSVCINTRGS FQCGPCQPGF VGDQESGCQR RAQRFCPDGS
PSECHEHADC VLERDGSRSC VCAVGWAGNG ILCGRDTDLD GFPDEKLRCP ERQCRKDNCV
TVPNSGQEDV DRDGIGDACD PDADGDGVPN EKDNCPLVRN PDQRNTDEDK WGDACDNCRT
QKNDDQKDTD QDGRGDACDD DIDGDRIRNQ ADNCPRIPNS DQKDSDGDGI GDACDNCPQK
SNPDQGDVDH DFVGDACDSD QDQDGDGHQD SRDNCPTVPN SAQQDSDHDG QGDACDNDDD
NDGVPDSRDN CRLVPNPGQE DADRDGVGDV CQGDFDADKV VDKIDVCPEN AEVTLTDFRA
FQTVVLDPEG DAQIDPNWVV LNQGREIVQT MNSDPGLAVG YTAFNGVDFE GTFHVNTVTD
DDYAGFIFGY QDSSSFYVVM WKQMEQTYWQ ANPFRAVAEP GIQLKAVKSS TGPGEQLRNA
LWHTGDTDSQ VRLLWKDPRN VGWKDKKSYR WFLQHRPQVG YIRVRFYEGP ELVADSNVVL
DTTMRGGRLG VFCFSQENII WANLRYRCND TIPEDYETHQ LRRA
//