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Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Cofactori

Ca2+By similarityNote: Binds 11-14 calcium ions per subunit.By similarity

GO - Molecular functioni

  1. calcium ion binding Source: MGI
  2. collagen binding Source: MGI
  3. extracellular matrix structural constituent Source: InterPro
  4. heparan sulfate proteoglycan binding Source: MGI
  5. heparin binding Source: MGI
  6. protease binding Source: BHF-UCL

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. extracellular matrix organization Source: InterPro
  4. growth plate cartilage development Source: MGI
  5. limb development Source: MGI
  6. negative regulation of apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_319261. Integrin cell surface interactions.
REACT_354321. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Cartilage oligomeric matrix protein
Short name:
COMP
Gene namesi
Name:Comp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88469. Comp.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 755736Cartilage oligomeric matrix proteinPRO_0000035858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 – 68Interchain
Disulfide bondi71 – 71Interchain
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi94 ↔ 109PROSITE-ProRule annotation
Disulfide bondi112 ↔ 123PROSITE-ProRule annotation
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi129 ↔ 140PROSITE-ProRule annotation
Disulfide bondi134 ↔ 149PROSITE-ProRule annotation
Disulfide bondi152 ↔ 176PROSITE-ProRule annotation
Disulfide bondi182 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 204PROSITE-ProRule annotation
Disulfide bondi207 ↔ 219PROSITE-ProRule annotation
Disulfide bondi227 ↔ 241PROSITE-ProRule annotation
Disulfide bondi235 ↔ 251PROSITE-ProRule annotation
Disulfide bondi253 ↔ 264PROSITE-ProRule annotation
Disulfide bondi280 ↔ 285PROSITE-ProRule annotation
Disulfide bondi290 ↔ 310PROSITE-ProRule annotation
Disulfide bondi326 ↔ 346PROSITE-ProRule annotation
Disulfide bondi349 ↔ 369PROSITE-ProRule annotation
Disulfide bondi385 ↔ 405PROSITE-ProRule annotation
Disulfide bondi408 ↔ 428PROSITE-ProRule annotation
Disulfide bondi446 ↔ 466PROSITE-ProRule annotation
Disulfide bondi482 ↔ 502PROSITE-ProRule annotation
Disulfide bondi518 ↔ 739PROSITE-ProRule annotation
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9R0G6.
PaxDbiQ9R0G6.
PRIDEiQ9R0G6.

PTM databases

PhosphoSiteiQ9R0G6.

Expressioni

Gene expression databases

CleanExiMM_COMP.
GenevestigatoriQ9R0G6.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAMTS12P583973EBI-9028018,EBI-9028051From a different organism.

Protein-protein interaction databases

IntActiQ9R0G6. 2 interactions.
STRINGi10090.ENSMUSP00000003659.

Structurei

Secondary structure

1
755
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 6637Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9R0G6.
SMRiQ9R0G6. Positions 28-71, 89-754.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R0G6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 12440EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 17753EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini178 – 22043EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini223 – 26543EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati266 – 29833TSP type-3 1Add
BLAST
Repeati299 – 33436TSP type-3 2Add
BLAST
Repeati335 – 35723TSP type-3 3Add
BLAST
Repeati358 – 39336TSP type-3 4Add
BLAST
Repeati394 – 41623TSP type-3 5Add
BLAST
Repeati417 – 45438TSP type-3 6Add
BLAST
Repeati455 – 49036TSP type-3 7Add
BLAST
Repeati491 – 52636TSP type-3 8Add
BLAST
Domaini530 – 744215TSP C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 8464COMP N-terminalAdd
BLAST
Regioni525 – 755231Mediates cell survival and induction of the IAP family of survival proteinsBy similarityAdd
BLAST

Domaini

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).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).By similarity

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOVERGENiHBG000636.
InParanoidiQ9R0G6.
KOiK04659.
OMAiPEDYETQ.
OrthoDBiEOG76QFGD.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR028492. Comp.
IPR013320. ConA-like_dom.
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]
PANTHERiPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00018. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0G6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPTACVLVL ALAILRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL
60 70 80 90 100
LRQQVKEITF LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC
110 120 130 140 150
SETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE
160 170 180 190 200
ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN ECETGQHNCV PNSVCVNTRG
210 220 230 240 250
SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN CVLERDGSRS
260 270 280 290 300
CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED
310 320 330 340 350
VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR
360 370 380 390 400
SKKNDDQKDT DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG
410 420 430 440 450
VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP
460 470 480 490 500
NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD
510 520 530 540 550
ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV
560 570 580 590 600
VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG
610 620 630 640 650
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN
660 670 680 690 700
ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG
710 720 730 740 750
PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYESH

RLQRV
Length:755
Mass (Da):82,342
Last modified:October 2, 2012 - v2
Checksum:i24C2F113E7945C0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 542QQ → HE in AAD01972 (PubMed:11052496).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033530 mRNA. Translation: AAD01972.1.
AC158553 Genomic DNA. No translation available.
CH466569 Genomic DNA. Translation: EDL28815.1.
CCDSiCCDS22367.1.
RefSeqiNP_057894.2. NM_016685.2.
UniGeneiMm.45071.

Genome annotation databases

EnsembliENSMUST00000003659; ENSMUSP00000003659; ENSMUSG00000031849.
GeneIDi12845.
KEGGimmu:12845.
UCSCiuc009mad.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033530 mRNA. Translation: AAD01972.1.
AC158553 Genomic DNA. No translation available.
CH466569 Genomic DNA. Translation: EDL28815.1.
CCDSiCCDS22367.1.
RefSeqiNP_057894.2. NM_016685.2.
UniGeneiMm.45071.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9R0G6.
SMRiQ9R0G6. Positions 28-71, 89-754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0G6. 2 interactions.
STRINGi10090.ENSMUSP00000003659.

PTM databases

PhosphoSiteiQ9R0G6.

Proteomic databases

MaxQBiQ9R0G6.
PaxDbiQ9R0G6.
PRIDEiQ9R0G6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003659; ENSMUSP00000003659; ENSMUSG00000031849.
GeneIDi12845.
KEGGimmu:12845.
UCSCiuc009mad.2. mouse.

Organism-specific databases

CTDi1311.
MGIiMGI:88469. Comp.

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOVERGENiHBG000636.
InParanoidiQ9R0G6.
KOiK04659.
OMAiPEDYETQ.
OrthoDBiEOG76QFGD.
TreeFamiTF324917.

Enzyme and pathway databases

ReactomeiREACT_319261. Integrin cell surface interactions.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

EvolutionaryTraceiQ9R0G6.
NextBioi282384.
PROiQ9R0G6.
SOURCEiSearch...

Gene expression databases

CleanExiMM_COMP.
GenevestigatoriQ9R0G6.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR028492. Comp.
IPR013320. ConA-like_dom.
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]
PANTHERiPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00018. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cartilage.
  2. 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 (JUN-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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-71.

Entry informationi

Entry nameiCOMP_MOUSE
AccessioniPrimary (citable) accession number: Q9R0G6
Secondary accession number(s): G3X8Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 9, 2003
Last sequence update: October 2, 2012
Last modified: March 31, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.