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Database: UniProt
Entry: A0A2K5Y0L4_MANLE
LinkDB: A0A2K5Y0L4_MANLE
Original site: A0A2K5Y0L4_MANLE 
ID   A0A2K5Y0L4_MANLE        Unreviewed;       757 AA.
AC   A0A2K5Y0L4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cartilage oligomeric matrix protein {ECO:0000313|Ensembl:ENSMLEP00000009108.1};
GN   Name=COMP {ECO:0000313|Ensembl:ENSMLEP00000009108.1};
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:ENSMLEP00000009108.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000009108.1}
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_011845905.1; XM_011990515.1.
DR   AlphaFoldDB; A0A2K5Y0L4; -.
DR   STRING; 9568.ENSMLEP00000009108; -.
DR   Ensembl; ENSMLET00000032507.1; ENSMLEP00000009108.1; ENSMLEG00000028753.1.
DR   GeneID; 105547095; -.
DR   KEGG; mleu:105547095; -.
DR   CTD; 1311; -.
DR   GeneTree; ENSGT00940000162169; -.
DR   OMA; DQTSGCQ; -.
DR   OrthoDB; 5345349at2759; -.
DR   Proteomes; UP000233140; 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; 3.
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; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..757
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014459908"
FT   DOMAIN          127..164
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          301..336
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          360..395
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          457..492
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          493..528
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          532..746
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          298..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          35..65
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        303..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  82916 MW;  ACDD8A35282F6936 CRC64;
     MAPDTACVLL LTLAALGASG QSQIPLGSDL GPQMLRELQE TNAALQDVRE LLRQQVREIT
     FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV ACIQTESGAR CGPCPAGFTG
     NGSHCTDVNE CNAHPCFPRV RCINTSPGFR CEACPPGYSG PTHEGVGLAF AKANKQVCTD
     INECETGQHN CVPNSVCINT RGSFQCGPCQ PGFVGDQESG CQRRAQRFCP DGSPSECHEH
     ADCVLERDGS RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ
     EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN CRTQKNDDQK
     DTDQDGRGDA CDDDIDGDRI RNQADNCPRI PNSDQKDSDG DGIGDACDNC PQKSNPDQGD
     VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT VPNSAQQDSD HDGQGDACDN DDDNDGVPDS
     RDNCRLVPNP GQEDADRDGV GDVCQGDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD
     PEGDAQIDPN WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI
     FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL RNALWHTGDT
     DSQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY EGPELVADSN VVLDTTMRGG
     RLGVFCFSQE NIIWANLRYR CNDTIPEDYE THQLRRA
//
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