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Q9R0G6

- COMP_MOUSE

UniProt

Q9R0G6 - COMP_MOUSE

Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    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

    Binds 11-14 calcium ions per subunit.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. extracellular matrix structural constituent Source: InterPro
    3. heparin binding Source: UniProtKB-KW
    4. protease binding Source: BHF-UCL
    5. protein binding Source: IntAct

    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: Ensembl
    6. negative regulation of apoptotic process Source: Ensembl

    Keywords - Biological processi

    Apoptosis, Cell adhesion

    Keywords - Ligandi

    Calcium, Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_216309. Integrin cell surface interactions.

    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: Chromosome 8

    Organism-specific databases

    MGIiMGI:88469. Comp.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    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

    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 – 6637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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]
    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

    MGPTACVLVL ALAILRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL    50
    LRQQVKEITF LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC 100
    SETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE 150
    ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN ECETGQHNCV PNSVCVNTRG 200
    SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN CVLERDGSRS 250
    CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 300
    VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR 350
    SKKNDDQKDT DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG 400
    VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP 450
    NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD 500
    ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV 550
    VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG 600
    YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN 650
    ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG 700
    PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYESH 750
    RLQRV 755
    Length:755
    Mass (Da):82,342
    Last modified:October 3, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033530 mRNA. Translation: AAD01972.1 .
    AC158553 Genomic DNA. No translation available.
    CH466569 Genomic DNA. Translation: EDL28815.1 .
    CCDSi CCDS22367.1.
    RefSeqi NP_057894.2. NM_016685.2.
    UniGenei Mm.45071.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MZ9 X-ray 1.70 A/B/C/D/E 28-71 [» ]
    3V2N X-ray 1.80 A/B/C/D/E 28-71 [» ]
    3V2P X-ray 1.87 A/B/C/D/E 28-71 [» ]
    3V2Q X-ray 2.20 A/B/C/D/E 28-71 [» ]
    3V2R X-ray 2.75 A/B/C/D/E 28-71 [» ]
    ProteinModelPortali Q9R0G6.
    SMRi Q9R0G6. Positions 28-71, 89-754.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9R0G6. 2 interactions.
    STRINGi 10090.ENSMUSP00000003659.

    PTM databases

    PhosphoSitei Q9R0G6.

    Proteomic databases

    PaxDbi Q9R0G6.
    PRIDEi Q9R0G6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003659 ; ENSMUSP00000003659 ; ENSMUSG00000031849 .
    GeneIDi 12845.
    KEGGi mmu:12845.
    UCSCi uc009mad.2. mouse.

    Organism-specific databases

    CTDi 1311.
    MGIi MGI:88469. Comp.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00550000074507.
    HOVERGENi HBG000636.
    InParanoidi Q9R0G6.
    KOi K04659.
    OMAi PEDYETQ.
    OrthoDBi EOG76QFGD.
    TreeFami TF324917.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    EvolutionaryTracei Q9R0G6.
    NextBioi 282384.
    PROi Q9R0G6.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_COMP.
    Genevestigatori Q9R0G6.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    4.10.1080.10. 2 hits.
    InterProi IPR028492. 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 ]
    PANTHERi PTHR10199:SF81. PTHR10199:SF81. 1 hit.
    Pfami PF11598. COMP. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF02412. TSP_3. 6 hits.
    PF05735. TSP_C. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 2 hits.
    SM00179. EGF_CA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF103647. SSF103647. 3 hits.
    SSF49899. SSF49899. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiCOMP_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0G6
    Secondary accession number(s): G3X8Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 120 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