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Q9R0G6 (COMP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cartilage oligomeric matrix protein

Short name=COMP
Gene names
Name:Comp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 By similarity.

Cofactor

Binds 11-14 calcium ions per subunit By similarity.

Subunit structure

Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca2+, Mg2+ or Mn2+). The greatest amount of binding is seen in the presence of Mn2+. Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response By similarity.

The TSP C-terminal domain mediates interaction with FN1 and ACAN By similarity.

Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions By similarity.

Sequence similarities

Belongs to the thrombospondin family.

Contains 4 EGF-like domains.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 8 TSP type-3 repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADAMTS12P583973EBI-9028018,EBI-9028051From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 755736Cartilage oligomeric matrix protein
PRO_0000035858

Regions

Domain85 – 12440EGF-like 1
Domain125 – 17753EGF-like 2; calcium-binding Potential
Domain178 – 22043EGF-like 3; calcium-binding Potential
Domain223 – 26543EGF-like 4
Repeat266 – 29833TSP type-3 1
Repeat299 – 33436TSP type-3 2
Repeat335 – 35723TSP type-3 3
Repeat358 – 39336TSP type-3 4
Repeat394 – 41623TSP type-3 5
Repeat417 – 45438TSP type-3 6
Repeat455 – 49036TSP type-3 7
Repeat491 – 52636TSP type-3 8
Domain530 – 744215TSP C-terminal
Region21 – 8464COMP N-terminal
Region525 – 755231Mediates cell survival and induction of the IAP family of survival proteins By similarity

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Disulfide bond68Interchain
Disulfide bond71Interchain
Disulfide bond89 ↔ 100 By similarity
Disulfide bond94 ↔ 109 By similarity
Disulfide bond112 ↔ 123 By similarity
Disulfide bond129 ↔ 140 By similarity
Disulfide bond134 ↔ 149 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond189 ↔ 204 By similarity
Disulfide bond207 ↔ 219 By similarity
Disulfide bond227 ↔ 241 By similarity
Disulfide bond235 ↔ 251 By similarity
Disulfide bond253 ↔ 264 By similarity
Disulfide bond280 ↔ 285 By similarity
Disulfide bond290 ↔ 310 By similarity
Disulfide bond326 ↔ 346 By similarity
Disulfide bond349 ↔ 369 By similarity
Disulfide bond385 ↔ 405 By similarity
Disulfide bond408 ↔ 428 By similarity
Disulfide bond446 ↔ 466 By similarity
Disulfide bond482 ↔ 502 By similarity
Disulfide bond518 ↔ 739 By similarity

Experimental info

Sequence conflict53 – 542QQ → HE in AAD01972. Ref.1

Secondary structure

... 755
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R0G6 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 24C2F113E7945C0F

FASTA75582,342
        10         20         30         40         50         60 
MGPTACVLVL ALAILRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL LRQQVKEITF 

        70         80         90        100        110        120 
LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC SETATGARCG PCPPGYTGNG 

       130        140        150        160        170        180 
SHCTDVNECN AHPCFPRVRC INTSPGFHCE ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN 

       190        200        210        220        230        240 
ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN 

       250        260        270        280        290        300 
CVLERDGSRS CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 

       310        320        330        340        350        360 
VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR SKKNDDQKDT 

       370        380        390        400        410        420 
DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG VGDACDNCPQ KDNPDQRDVD 

       430        440        450        460        470        480 
HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP NSAQQDSDHD GKGDACDDDD DNDGVPDSRD 

       490        500        510        520        530        540 
NCRLVPNPGQ EDNDRDGVGD ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE 

       550        560        570        580        590        600 
GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG 

       610        620        630        640        650        660 
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN ALWHTGDTAS 

       670        680        690        700        710        720 
QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG PELVADSNVV LDTAMRGGRL 

       730        740        750 
GVFCFSQENI IWANLRYRCN DTIPEDYESH RLQRV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, sequencing, and tissue and developmental expression of mouse cartilage oligomeric matrix protein (COMP)."
Fang C., Carlson C.S., Leslie M.P., Tulli H., Stolerman E., Perris R., Ni L., Di Cesare P.E.
J. Orthop. Res. 18:593-603(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cartilage.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Storage function of cartilage oligomeric matrix protein: the crystal structure of the coiled-coil domain in complex with vitamin D(3)."
Ozbek S., Engel J., Stetefeld J.
EMBO J. 21:5960-5968(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-71.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF033530 mRNA. Translation: AAD01972.1.
AC158553 Genomic DNA. No translation available.
CH466569 Genomic DNA. Translation: EDL28815.1.
CCDSCCDS22367.1.
RefSeqNP_057894.2. NM_016685.2.
UniGeneMm.45071.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZ9X-ray1.70A/B/C/D/E28-71[»]
3V2NX-ray1.80A/B/C/D/E28-71[»]
3V2PX-ray1.87A/B/C/D/E28-71[»]
3V2QX-ray2.20A/B/C/D/E28-71[»]
3V2RX-ray2.75A/B/C/D/E28-71[»]
ProteinModelPortalQ9R0G6.
SMRQ9R0G6. Positions 28-71, 89-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0G6. 2 interactions.
STRING10090.ENSMUSP00000003659.

PTM databases

PhosphoSiteQ9R0G6.

Proteomic databases

PaxDbQ9R0G6.
PRIDEQ9R0G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003659; ENSMUSP00000003659; ENSMUSG00000031849.
GeneID12845.
KEGGmmu:12845.
UCSCuc009mad.2. mouse.

Organism-specific databases

CTD1311.
MGIMGI:88469. Comp.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00550000074507.
HOVERGENHBG000636.
InParanoidQ9R0G6.
KOK04659.
OMAPEDYETQ.
OrthoDBEOG76QFGD.
TreeFamTF324917.

Gene expression databases

CleanExMM_COMP.
GenevestigatorQ9R0G6.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProIPR028492. Comp.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PANTHERPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9R0G6.
NextBio282384.
PROQ9R0G6.
SOURCESearch...

Entry information

Entry nameCOMP_MOUSE
AccessionPrimary (citable) accession number: Q9R0G6
Secondary accession number(s): G3X8Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot