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Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding
Biological processApoptosis, Cell adhesion
LigandCalcium

Enzyme and pathway databases

ReactomeiR-MMU-216083 Integrin cell surface interactions
R-MMU-3000178 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88469 Comp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000003585820 – 755Cartilage oligomeric matrix proteinAdd BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68Interchain (with C-71)Combined sources1 Publication
Disulfide bondi71Interchain (with C-68)Combined sources1 Publication
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi94 ↔ 109PROSITE-ProRule annotation
Disulfide bondi112 ↔ 123PROSITE-ProRule annotation
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
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
Modified residuei394PhosphoserineCombined sources1
Disulfide bondi408 ↔ 428PROSITE-ProRule annotation
Disulfide bondi446 ↔ 466PROSITE-ProRule annotation
Disulfide bondi482 ↔ 502PROSITE-ProRule annotation
Disulfide bondi518 ↔ 739PROSITE-ProRule annotation
Glycosylationi740N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9R0G6
PaxDbiQ9R0G6
PRIDEiQ9R0G6

PTM databases

iPTMnetiQ9R0G6
PhosphoSitePlusiQ9R0G6

Expressioni

Tissue specificityi

Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues.1 Publication

Developmental stagei

In knee epiphyseal cartilage, expression is detected from E12.5 onwards, with significant up-regulation at E16.5 and again at postnatal day 5. Expressed at least until 10 months of age.1 Publication

Gene expression databases

BgeeiENSMUSG00000031849
CleanExiMM_COMP
ExpressionAtlasiQ9R0G6 baseline and differential
GenevisibleiQ9R0G6 MM

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 Homo sapiens.

GO - Molecular functioni

  • fibronectin binding Source: MGI
  • heparan sulfate proteoglycan binding Source: MGI
  • protease binding Source: BHF-UCL

Protein-protein interaction databases

ComplexPortaliCPX-3026 Thrombospondin 5 complex
IntActiQ9R0G6, 2 interactors
STRINGi10090.ENSMUSP00000003659

Structurei

Secondary structure

1755
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 66Combined sources37

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R0G6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 124EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini125 – 177EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST53
Domaini178 – 220EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini223 – 265EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Repeati266 – 298TSP type-3 1Add BLAST33
Repeati299 – 334TSP type-3 2Add BLAST36
Repeati335 – 357TSP type-3 3Add BLAST23
Repeati358 – 393TSP type-3 4Add BLAST36
Repeati394 – 416TSP type-3 5Add BLAST23
Repeati417 – 454TSP type-3 6Add BLAST38
Repeati455 – 490TSP type-3 7Add BLAST36
Repeati491 – 526TSP type-3 8Add BLAST36
Domaini530 – 744TSP C-terminalPROSITE-ProRule annotationAdd BLAST215

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 84COMP N-terminalAdd BLAST64
Regioni525 – 755Mediates cell survival and induction of the IAP family of survival proteinsBy similarityAdd BLAST231

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

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IFQQ Eukaryota
ENOG410XQKE LUCA
GeneTreeiENSGT00850000132273
HOVERGENiHBG000636
InParanoidiQ9R0G6
KOiK04659
OMAiDVDHDFV
OrthoDBiEOG091G00TV
TreeFamiTF324917

Family and domain databases

Gene3Di4.10.1080.10, 3 hits
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR024665 Thbs/COMP_coiled-coil
IPR037349 Thrombospondin
IPR003367 Thrombospondin_3-like_rpt
IPR017897 Thrombospondin_3_rpt
IPR008859 Thrombospondin_C
IPR028492 TSP-5
IPR028974 TSP_type-3_rpt
PANTHERiPTHR10199 PTHR10199, 1 hit
PTHR10199:SF88 PTHR10199:SF88, 1 hit
PfamiView protein in Pfam
PF11598 COMP, 1 hit
PF07645 EGF_CA, 2 hits
PF02412 TSP_3, 6 hits
PF05735 TSP_C, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 4 hits
SM00179 EGF_CA, 2 hits
SUPFAMiSSF103647 SSF103647, 3 hits
SSF49899 SSF49899, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00018 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

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 3, 2012 - v2
Checksum:i24C2F113E7945C0F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53 – 54QQ → HE in AAD01972 (PubMed:11052496).Curated2

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

Similar proteinsi

Entry informationi

Entry nameiCOMP_MOUSE
AccessioniPrimary (citable) accession number: Q9R0G6
Secondary accession number(s): G3X8Q4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 3, 2012
Last modified: June 20, 2018
This is version 146 of the entry and version 2 of the sequence. See 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

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