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P35444

- COMP_RAT

UniProt

P35444 - COMP_RAT

Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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) By similarity. 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 similarity1 Publication

    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: RGD
    3. fibronectin binding Source: RGD
    4. heparin binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. vitamin D binding Source: RGD

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. extracellular matrix organization Source: RGD

    Keywords - Biological processi

    Apoptosis, Cell adhesion

    Keywords - Ligandi

    Calcium, Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cartilage oligomeric matrix protein
    Short name:
    COMP
    Gene namesi
    Name:Comp
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2378. Comp.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: RGD
    2. proteinaceous extracellular matrix Source: RGD

    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_0000035859Add
    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

    PRIDEiP35444.

    Expressioni

    Tissue specificityi

    Expressed in differentiated and de-differentiated vascular smooth muscle cells (VSMCs) (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP35444.

    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 By similarity. Interacts with ADAMTS12 By similarity. Interacts with ITGA7.By similarity1 Publication

    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
    1FBMX-ray2.70A/B/C/D/E28-72[»]
    1VDFX-ray2.05A/B/C/D/E28-72[»]
    ProteinModelPortaliP35444.
    SMRiP35444. Positions 28-72, 406-741.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35444.

    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

    HOVERGENiHBG000636.
    KOiK04659.
    PhylomeDBiP35444.

    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.
    PROSITEiPS01186. 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.

    P35444-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL    50
    LRHRVKEITF LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC 100
    TETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE 150
    ACPPGFSGPT HEGVGLTFAK TNKQVCTDIN ECETGQHNCV PNSVCVNTRG 200
    SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD CILERDGSRS 250
    CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 300
    VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR 350
    SQKNDDQKDT DRDGQGDACD 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 DTIPEDYERH 750
    RLRRA 755
    Length:755
    Mass (Da):82,664
    Last modified:June 1, 1994 - v1
    Checksum:iAB48888FE093C598
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72914 mRNA. Translation: CAA51419.1.
    PIRiA44315.
    RefSeqiNP_036966.1. NM_012834.1.
    UniGeneiRn.10343.

    Genome annotation databases

    GeneIDi25304.
    KEGGirno:25304.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72914 mRNA. Translation: CAA51419.1 .
    PIRi A44315.
    RefSeqi NP_036966.1. NM_012834.1.
    UniGenei Rn.10343.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FBM X-ray 2.70 A/B/C/D/E 28-72 [» ]
    1VDF X-ray 2.05 A/B/C/D/E 28-72 [» ]
    ProteinModelPortali P35444.
    SMRi P35444. Positions 28-72, 406-741.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P35444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25304.
    KEGGi rno:25304.

    Organism-specific databases

    CTDi 1311.
    RGDi 2378. Comp.

    Phylogenomic databases

    HOVERGENi HBG000636.
    KOi K04659.
    PhylomeDBi P35444.

    Miscellaneous databases

    EvolutionaryTracei P35444.
    NextBioi 606093.
    PROi P35444.

    Gene expression databases

    Genevestigatori P35444.

    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 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. "COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins."
      Oldberg A., Antonsson P., Lindblom K., Heinegaard D.
      J. Biol. Chem. 267:22346-22350(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cartilage.
    2. "Cartilage oligomeric matrix protein maintains the contractile phenotype of vascular smooth muscle cells by interacting with alpha(7)beta(1) integrin."
      Wang L., Zheng J., Du Y., Huang Y., Li J., Liu B., Liu C.J., Zhu Y., Gao Y., Xu Q., Kong W., Wang X.
      Circ. Res. 106:514-525(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ITGA7.
    3. "The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?"
      Malashkevich V.N., Kammerer R.A., Efimov V.P., Schulthess T., Engel J.
      Science 274:761-765(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 27-72.

    Entry informationi

    Entry nameiCOMP_RAT
    AccessioniPrimary (citable) accession number: P35444
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3