COMP_BOVIN
ID COMP_BOVIN Reviewed; 756 AA.
AC P35445;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cartilage oligomeric matrix protein;
DE Short=COMP;
DE Flags: Precursor;
GN Name=COMP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-756.
RC TISSUE=Cartilage;
RX PubMed=1429587; DOI=10.1016/s0021-9258(18)41677-8;
RA Oldberg A., Antonsson P., Lindblom K., Heinegaard D.;
RT "COMP (cartilage oligomeric matrix protein) is structurally related to the
RT thrombospondins.";
RL J. Biol. Chem. 267:22346-22350(1992).
RN [3]
RP INTERACTION WITH MATN1.
RX PubMed=15075323; DOI=10.1074/jbc.m403778200;
RA Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.;
RT "Interactions between the cartilage oligomeric matrix protein and
RT matrilins. Implications for matrix assembly and the pathogenesis of
RT chondrodysplasias.";
RL J. Biol. Chem. 279:25294-25298(2004).
CC -!- FUNCTION: Plays a role in the structural integrity of cartilage via its
CC interaction with other extracellular matrix proteins such as the
CC collagens and fibronectin. Can mediate the interaction of chondrocytes
CC with the cartilage extracellular matrix through interaction with cell
CC surface integrin receptors. Could play a role in the pathogenesis of
CC osteoarthritis. Potent suppressor of apoptosis in both primary
CC chondrocytes and transformed cells. Suppresses apoptosis by blocking
CC the activation of caspase-3 and by inducing the IAP family of survival
CC proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity). Essential for
CC maintaining a vascular smooth muscle cells (VSMCs)
CC contractile/differentiated phenotype under physiological and
CC pathological stimuli. Maintains this phenotype of VSMCs by interacting
CC with ITGA7 (By similarity). {ECO:0000250|UniProtKB:P35444,
CC ECO:0000250|UniProtKB:P49747}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P49747};
CC Note=Binds 11-14 calcium ions per subunit.
CC {ECO:0000250|UniProtKB:P49747};
CC -!- SUBUNIT: Pentamer; disulfide-linked. Exists in a more compact
CC conformation in the presence of calcium and shows a more extended
CC conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and
CC FN1. Binding to FN1 requires the presence of divalent cations (Ca(2+),
CC Mg(2+) or Mn(2+)). The greatest amount of binding is seen in the
CC presence of Mn(2+). Interacts with MATN1, MATN3, MATN4 and ACAN (By
CC similarity) (PubMed:15075323). Binds heparin, heparan sulfate and
CC chondroitin sulfate. EDTA dimishes significantly its binding to ACAN
CC and abolishes its binding to MATN3, MATN4 and chondroitin sulfate.
CC Interacts with collagen I, II and IX, and interaction with these
CC collagens is dependent on the presence of zinc ions. Interacts with
CC ADAMTS12 (By similarity). Interacts with ITGA7 (By similarity).
CC {ECO:0000250|UniProtKB:P35444, ECO:0000250|UniProtKB:P49747,
CC ECO:0000269|PubMed:15075323}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P49747}.
CC -!- DOMAIN: The cell attachment motif mediates the attachment to
CC chondrocytes. It mediates the induction of both the IAP family of
CC survival proteins and the antiapoptotic response.
CC {ECO:0000250|UniProtKB:P49747}.
CC -!- DOMAIN: The TSP C-terminal domain mediates interaction with FN1 and
CC ACAN. {ECO:0000250|UniProtKB:P49747}.
CC -!- DOMAIN: Each of the eight TSP type-3 repeats binds two calcium ions.
CC The TSP C-terminal domain binds three calcium ions.
CC {ECO:0000250|UniProtKB:P49747}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; X74326; CAA52374.1; -; mRNA.
DR PIR; B44315; B44315.
DR AlphaFoldDB; P35445; -.
DR SMR; P35445; -.
DR IntAct; P35445; 1.
DR MINT; P35445; -.
DR STRING; 9913.ENSBTAP00000006074; -.
DR PeptideAtlas; P35445; -.
DR PRIDE; P35445; -.
DR Ensembl; ENSBTAT00000006074; ENSBTAP00000006074; ENSBTAG00000004630.
DR VEuPathDB; HostDB:ENSBTAG00000004630; -.
DR VGNC; VGNC:27590; COMP.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000162169; -.
DR InParanoid; P35445; -.
DR OMA; RSQRFCP; -.
DR OrthoDB; 120983at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000004630; Expressed in laryngeal cartilage and 52 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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:Ensembl.
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:UniProtKB-KW.
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:UniProtKB-KW.
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; ISS:UniProtKB.
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:0010259; P:multicellular organism aging; 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; ISS:UniProtKB.
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; cd16077; TSP-5cc; 1.
DR Gene3D; 4.10.1080.10; -; 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; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028492; TSP-5.
DR InterPro; IPR039081; TSP-5_cc.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; PTHR10199:SF88; 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; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Heparin-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..756
FT /note="Cartilage oligomeric matrix protein"
FT /id="PRO_0000186460"
FT DOMAIN 86..125
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 126..178
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 179..218
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 224..266
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 267..299
FT /note="TSP type-3 1"
FT REPEAT 300..335
FT /note="TSP type-3 2"
FT REPEAT 336..358
FT /note="TSP type-3 3"
FT REPEAT 359..394
FT /note="TSP type-3 4"
FT REPEAT 395..417
FT /note="TSP type-3 5"
FT REPEAT 418..455
FT /note="TSP type-3 6"
FT REPEAT 456..491
FT /note="TSP type-3 7"
FT REPEAT 492..527
FT /note="TSP type-3 8"
FT DOMAIN 531..745
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 22..85
FT /note="COMP N-terminal"
FT REGION 322..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..756
FT /note="Mediates cell survival and induction of the IAP
FT family of survival proteins"
FT /evidence="ECO:0000250"
FT MOTIF 366..368
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 335..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..443
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"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 72
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 90..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 95..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 113..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 130..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 135..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 190..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 228..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 254..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 570
FT /note="A -> C (in Ref. 2; CAA52374)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="T -> P (in Ref. 2; CAA52374)"
FT /evidence="ECO:0000305"
FT CONFLICT 603..604
FT /note="QD -> HH (in Ref. 2; CAA52374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 82362 MW; DC2D84FE1C18FCA2 CRC64;
MVLAAARVLL LTLAALGASG QGQMPLGGDL GPQMLRELQE TNAALQDVRD LLRQQVKEIT
FLKNTVMECD ACGMQPARTP KLTVRPLSQC SPGFCFPGVA CTETANGARC GPCPEGFTGN
GSHCADVNEC TAHPCFPRVR CINTSPGFRC EACPPGFSGP THEGVGLAFA KANKQVCTDI
NECETGQHNC VPNSVCVNTV GSFQCGPCQP GFVGDQASGC RRRPQRFCPD GTPSPCHEKA
DCVLERDGSR SCVCAVGWAG NGLICGRDTD LDGFPDEKLR CSERQCRKDN CVTVPNSGQE
DVDQDGIGDA CDPDADGDGV LNEKDNCPLV RNPDQRNTDG DKWGDACDNC RSQKNDDQKD
TDKDGRGDAC DDDIDGDRIR NPVDNCPKVP NSDQKDTDGD GVGDACDNCP QKSNADQRDV
DHDFVGDACD SDQDQDGDGH QDSKDNCPTV PNSAQQDSDH DGQGDACDDD DDNDGVPDSR
DNCRLVPNPG QEDMDRDGVG DACQGDFDAD KVVDKIDVCP ENAEVTLTDF RAFQTVVLDP
EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD FEGTFHVNTA TDDDYAGFIF
GYQDSSSFYV VMWKQMEQTY WQANPFRAVA EPGIQLKAVK SSTGPGEQLR NALWHTGDTA
SQVRLLWKDP RNVGWKDKTS YRWFLQHRPQ VGYIRVRFYE GPELVADSNV ILDTTMRGGR
LGVFCFSQEN IIWANLRYRC NDTIPEDYEA QRLLQA
