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    COMP cartilage oligomeric matrix protein [ Bos taurus (domestic cattle) ]

    Gene ID: 281088, updated on 1-Jan-2025

    Summary

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    Official Symbol
    COMPprovided by VGNC
    Official Full Name
    cartilage oligomeric matrix proteinprovided by VGNC
    Primary source
    VGNC:VGNC:27590
    See related
    BGD:BT11103; Ensembl:ENSBTAG00000004630
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Bos taurus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
    Orthologs
    human mouse all
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    Genomic context

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    See COMP in Genome Data Viewer
    Location:
    chromosome: 7
    Exon count:
    20
    Annotation release Status Assembly Chr Location
    RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 7 NC_037334.1 (4422721..4430541)

    Chromosome 7 - NC_037334.1Genomic Context describing neighboring genes Neighboring gene growth differentiation factor 1 Neighboring gene UPF1 RNA helicase and ATPase Neighboring gene uncharacterized LOC112447321 Neighboring gene CREB regulated transcription coactivator 1 Neighboring gene U6 spliceosomal RNA Neighboring gene kelch like family member 26 Neighboring gene uncharacterized LOC112447594

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_037334.1 Chromosome 7 Reference ARS-UCD2.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Dominette sequence data
    • BioProject: PRJNA294306
    • Analysis date: Tue Dec 17 08:57:05 2024

    Bibliography

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    Related articles in PubMed

    1. Differential response of cartilage oligomeric matrix protein (COMP) to morphogens of bone morphogenetic protein/transforming growth factor-β family in the surface, middle and deep zones of articular cartilage. Motaung SC, et al. J Tissue Eng Regen Med, 2011 Jun. PMID 21604381
    2. COMP acts as a catalyst in collagen fibrillogenesis. Halász K, et al. J Biol Chem, 2007 Oct 26. PMID 17716974
    3. Expression of PSACH-associated mutant COMP in tendon fibroblasts leads to increased apoptotic cell death irrespective of the secretory characteristics of mutant COMP. Weirich C, et al. Matrix Biol, 2007 May. PMID 17307347
    4. Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs. Dickinson SC, et al. Matrix Biol, 2003 May. PMID 12853037
    5. COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. Oldberg A, et al. J Biol Chem, 1992 Nov 5. PMID 1429587

    See all (11) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. COMP regulation of BMPR2 appears to have an important role in controlling hypoxia-elicited changes in pulmonary artery superoxide and its potential regulation of contractile phenotype proteins.
      Title: Potential role of cartilage oligomeric matrix protein in the modulation of pulmonary arterial smooth muscle superoxide by hypoxia.
    2. COMP synthesis is differentially regulated by TGFbeta1 in the surface and middle zones of bovine articular cartilage.
      Title: Differential response of cartilage oligomeric matrix protein (COMP) to morphogens of bone morphogenetic protein/transforming growth factor-β family in the surface, middle and deep zones of articular cartilage.
    3. COMP acts as a catalyst in collagen fibrillogenesis.
      Title: COMP acts as a catalyst in collagen fibrillogenesis.
    4. COMP mutant expression in tendon fibroblasts leads to increased apoptotic cell death irrespective of the secretory characteristics of mutant COMP
      Title: Expression of PSACH-associated mutant COMP in tendon fibroblasts leads to increased apoptotic cell death irrespective of the secretory characteristics of mutant COMP.
    5. COMP mRNA expression level was markedly increased by ball oscillation.
      Title: Effects of simple and complex motion patterns on gene expression of chondrocytes seeded in 3D scaffolds.
    6. role for proteinases other than MMPs in the degradation of COMP in cartilage
      Title: Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables calcium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cell adhesion IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in collagen-containing extracellular matrix IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    cartilage oligomeric matrix protein

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001166517.2 → NP_001159989.2  cartilage oligomeric matrix protein precursor

      Status: PROVISIONAL

      Source sequence(s)
      NKLS02000007
      UniProtKB/Swiss-Prot
      P35445
      UniProtKB/TrEMBL
      A0AAA9TYT9
      Related
      ENSBTAP00000006074.6, ENSBTAT00000006074.6
      Conserved Domains (6) summary
      cd00054
      Location:179 → 215
      EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...
      sd00001
      Location:395 → 417
      TSP3; TSP3 repeat_short [structural motif]
      sd00002
      Location:300 → 335
      TSP3; TSP3 repeat_long [structural motif]
      cd16077
      Location:30 → 72
      TSP-5cc; Coiled coil region of thrombospondin-5 (TSP-5)
      pfam02412
      Location:300 → 335
      TSP_3; Thrombospondin type 3 repeat
      pfam05735
      Location:545 → 742
      TSP_C; Thrombospondin C-terminal region

    RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference ARS-UCD2.0 Primary Assembly

    Genomic

    1. NC_037334.1 Reference ARS-UCD2.0 Primary Assembly

      Range
      4422721..4430541
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_059887922.1 → XP_059743905.1  cartilage oligomeric matrix protein isoform X1

      UniProtKB/TrEMBL
      A0AAA9TYT9
      Related
      ENSBTAP00000097813.1, ENSBTAT00000122756.1
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P35445.2 GenPept UniProtKB/Swiss-Prot:P35445

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Molecular Biology Databases
    Research Materials