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Database: UniProt
Entry: P35445
LinkDB: P35445
Original site: P35445 
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   10-APR-2019, entry version 135.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   and evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 318-756.
RC   TISSUE=Cartilage;
RX   PubMed=1429587;
RA   Oldberg A., Antonsson P., Lindblom K., Heinegaard D.;
RT   "COMP (cartilage oligomeric matrix protein) is structurally related to
RT   the 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: May play a role in the structural integrity of cartilage
CC       via its interaction with other extracellular matrix proteins such
CC       as the collagens and fibronectin. Can mediate the interaction of
CC       chondrocytes with the cartilage extracellular matrix through
CC       interaction with cell surface integrin receptors. Could play a
CC       role in the pathogenesis of osteoarthritis. Potent suppressor of
CC       apoptosis in both primary chondrocytes and transformed cells.
CC       Suppresses apoptosis by blocking the activation of caspase-3 and
CC       by inducing the IAP family of survival proteins (BIRC3, BIRC2,
CC       BIRC5 and XIAP). Essential for maintaining a vascular smooth
CC       muscle cells (VSMCs) contractile/differentiated phenotype under
CC       physiological and pathological stimuli. Maintains this phenotype
CC       of VSMCs by interacting with ITGA7 (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 11-14 calcium ions per subunit. {ECO:0000250};
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,
CC       ITGA5 and FN1. Binding to FN1 requires the presence of divalent
CC       cations (Ca(2+), Mg(2+) or Mn(2+)). The greatest amount of binding
CC       is seen in the presence of Mn(2+). Interacts with MATN3, MATN4 and
CC       ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA
CC       dimishes significantly its binding to ACAN and abolishes its
CC       binding to MATN3, MATN4 and chondroitin sulfate. Interacts with
CC       collagen I, II and IX and interaction with these collagens is
CC       dependent on the presence of zinc ions (By similarity). Interacts
CC       with MATN1. Interacts with ADAMTS12. Interacts with ITGA7 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The TSP C-terminal domain mediates interaction with FN1
CC       and ACAN. {ECO:0000250}.
CC   -!- DOMAIN: Each of the eight TSP type-3 repeats binds two calcium
CC       ions. The TSP C-terminal domain binds three calcium ions (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
DR   EMBL; X74326; CAA52374.1; -; mRNA.
DR   PIR; B44315; B44315.
DR   UniGene; Bt.3034; -.
DR   ProteinModelPortal; 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   GeneTree; ENSGT00940000162169; -.
DR   HOGENOM; HOG000007542; -.
DR   HOVERGEN; HBG000636; -.
DR   InParanoid; P35445; -.
DR   OrthoDB; 120983at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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:0010260; P:animal organ senescence; 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: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:0048747; P:muscle fiber development; 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:0050905; P:neuromuscular process; IEA:Ensembl.
DR   GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR   GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IBA:GO_Central.
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: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 smooth muscle cell development; IEA:Ensembl.
DR   GO; GO:0014829; P:vascular 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR   InterPro; IPR037349; Thrombospondin.
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; PTHR10199; 1.
DR   PANTHER; PTHR10199:SF88; PTHR10199:SF88; 1.
DR   Pfam; PF11598; COMP; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF02412; TSP_3; 6.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    756       Cartilage oligomeric matrix protein.
FT                                /FTId=PRO_0000186460.
FT   DOMAIN       86    125       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      126    178       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      179    218       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      224    266       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      267    299       TSP type-3 1.
FT   REPEAT      300    335       TSP type-3 2.
FT   REPEAT      336    358       TSP type-3 3.
FT   REPEAT      359    394       TSP type-3 4.
FT   REPEAT      395    417       TSP type-3 5.
FT   REPEAT      418    455       TSP type-3 6.
FT   REPEAT      456    491       TSP type-3 7.
FT   REPEAT      492    527       TSP type-3 8.
FT   DOMAIN      531    745       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION       22     85       COMP N-terminal.
FT   REGION      526    756       Mediates cell survival and induction of
FT                                the IAP family of survival proteins.
FT                                {ECO:0000250}.
FT   MOTIF       366    368       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    120    120       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    741    741       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     69     69       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID     72     72       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID     90    101       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     95    110       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    113    124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    130    141       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    135    150       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    183    196       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    190    205       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    228    242       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    236    252       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    254    265       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT    570    570       A -> C (in Ref. 2; CAA52374).
FT                                {ECO:0000305}.
FT   CONFLICT    584    584       T -> P (in Ref. 2; CAA52374).
FT                                {ECO:0000305}.
FT   CONFLICT    603    604       QD -> HH (in Ref. 2; CAA52374).
FT                                {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
//
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