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Database: UniProt
Entry: P35444
LinkDB: P35444
Original site: P35444 
ID   COMP_RAT                Reviewed;         755 AA.
AC   P35444;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Cartilage oligomeric matrix protein;
DE            Short=COMP;
DE   Flags: Precursor;
GN   Name=Comp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ITGA7.
RX   PubMed=20019333; DOI=10.1161/CIRCRESAHA.109.202762;
RA   Wang L., Zheng J., Du Y., Huang Y., Li J., Liu B., Liu C.J., Zhu Y.,
RA   Gao Y., Xu Q., Kong W., Wang X.;
RT   "Cartilage oligomeric matrix protein maintains the contractile
RT   phenotype of vascular smooth muscle cells by interacting with
RT   alpha(7)beta(1) integrin.";
RL   Circ. Res. 106:514-525(2010).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 27-72, AND DISULFIDE BONDS.
RX   PubMed=8864111; DOI=10.1126/science.274.5288.761;
RA   Malashkevich V.N., Kammerer R.A., Efimov V.P., Schulthess T.,
RA   Engel J.;
RT   "The crystal structure of a five-stranded coiled coil in COMP: a
RT   prototype ion channel?";
RL   Science 274:761-765(1996).
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) (By similarity). Essential for maintaining a
CC       vascular smooth muscle cells (VSMCs) contractile/differentiated
CC       phenotype under physiological and pathological stimuli. Maintains
CC       this phenotype of VSMCs by interacting with ITGA7. {ECO:0000250,
CC       ECO:0000269|PubMed:20019333}.
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 MATN1, MATN3,
CC       MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin
CC       sulfate. EDTA dimishes significantly its binding to ACAN and
CC       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 (By
CC       similarity). Interacts with ADAMTS12 (By similarity). Interacts
CC       with ITGA7. {ECO:0000250, ECO:0000269|PubMed:20019333}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in differentiated and de-
CC       differentiated vascular smooth muscle cells (VSMCs) (at protein
CC       level). {ECO:0000269|PubMed:20019333}.
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; X72914; CAA51419.1; -; mRNA.
DR   PIR; A44315; A44315.
DR   RefSeq; NP_036966.1; NM_012834.1.
DR   UniGene; Rn.10343; -.
DR   PDB; 1FBM; X-ray; 2.70 A; A/B/C/D/E=28-72.
DR   PDB; 1VDF; X-ray; 2.05 A; A/B/C/D/E=28-72.
DR   PDBsum; 1FBM; -.
DR   PDBsum; 1VDF; -.
DR   ProteinModelPortal; P35444; -.
DR   SMR; P35444; -.
DR   STRING; 10116.ENSRNOP00000067037; -.
DR   PaxDb; P35444; -.
DR   PRIDE; P35444; -.
DR   GeneID; 25304; -.
DR   KEGG; rno:25304; -.
DR   CTD; 1311; -.
DR   RGD; 2378; Comp.
DR   eggNOG; ENOG410IFQQ; Eukaryota.
DR   eggNOG; ENOG410XQKE; LUCA.
DR   HOVERGEN; HBG000636; -.
DR   InParanoid; P35444; -.
DR   KO; K04659; -.
DR   OrthoDB; 120983at2759; -.
DR   PhylomeDB; P35444; -.
DR   EvolutionaryTrace; P35444; -.
DR   PRO; PR:P35444; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IDA:RGD.
DR   GO; GO:0001968; F:fibronectin binding; IDA:RGD.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005499; F:vitamin D binding; IMP:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IBA:GO_Central.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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   SUPFAM; SSF57184; SSF57184; 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   3D-structure; Apoptosis; Calcium; Cell adhesion; Complete proteome;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Heparin-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    755       Cartilage oligomeric matrix protein.
FT                                /FTId=PRO_0000035859.
FT   DOMAIN       85    124       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      125    177       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      178    220       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      223    265       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      266    298       TSP type-3 1.
FT   REPEAT      299    334       TSP type-3 2.
FT   REPEAT      335    357       TSP type-3 3.
FT   REPEAT      358    393       TSP type-3 4.
FT   REPEAT      394    416       TSP type-3 5.
FT   REPEAT      417    454       TSP type-3 6.
FT   REPEAT      455    490       TSP type-3 7.
FT   REPEAT      491    526       TSP type-3 8.
FT   DOMAIN      530    744       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION       21     84       COMP N-terminal.
FT   REGION      525    755       Mediates cell survival and induction of
FT                                the IAP family of survival proteins.
FT                                {ECO:0000250}.
FT   MOD_RES     394    394       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G6}.
FT   CARBOHYD    119    119       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    740    740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     68     68       Interchain (with C-71).
FT                                {ECO:0000244|PDB:1FBM,
FT                                ECO:0000244|PDB:1VDF,
FT                                ECO:0000269|PubMed:8864111}.
FT   DISULFID     71     71       Interchain (with C-68).
FT                                {ECO:0000244|PDB:1FBM,
FT                                ECO:0000244|PDB:1VDF,
FT                                ECO:0000269|PubMed:8864111}.
FT   DISULFID     89    100       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     94    109       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    112    123       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    129    140       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    134    149       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    152    176       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    182    195       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    189    204       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    207    219       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    227    241       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    235    251       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    253    264       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    280    285       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    290    310       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    326    346       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    349    369       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    385    405       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    408    428       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    446    466       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    482    502       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    518    739       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   HELIX        30     66       {ECO:0000244|PDB:1VDF}.
SQ   SEQUENCE   755 AA;  82664 MW;  AB48888FE093C598 CRC64;
     MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL LRHRVKEITF
     LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC TETATGARCG PCPPGYTGNG
     SHCTDVNECN AHPCFPRVRC INTSPGFHCE ACPPGFSGPT HEGVGLTFAK TNKQVCTDIN
     ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD
     CILERDGSRS CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED
     VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR SQKNDDQKDT
     DRDGQGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG VGDACDNCPQ KDNPDQRDVD
     HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP NSAQQDSDHD GKGDACDDDD DNDGVPDSRD
     NCRLVPNPGQ EDNDRDGVGD ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE
     GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG
     YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN ALWHTGDTAS
     QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG PELVADSNVV LDTAMRGGRL
     GVFCFSQENI IWANLRYRCN DTIPEDYERH RLRRA
//
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