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FLASH GENE
Symbol COMP contributors: mct/npt/pgu - updated : 22-06-2015
HGNC name cartilage oligomeric matrix protein
HGNC id 2227
EXPRESSION
Type widely
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Cardiovascularvessel     Homo sapiensAdult
Skeletonappendicular skeletonjointsynovia highly
Visualeyeanterior segmentcornea  
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connectivebone   
Connectivecartilage    Homo sapiensAdult
Connectivedensetendon highly
Connectivedenseligament highly
cells
SystemCellPubmedSpeciesStageRna symbol
 chondrocyte
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal aliphatic residues dictate the structure, stability, assembly, and small molecule binding of the coiled-coil region
  • a signal peptide
  • thrombospondin type 2 and 3 repeats, lacking the procollagen homology domain and seven type III repeats (TSP) of THBS1
  • four coiled-coil type II (EGF-like)
  • type III calmodulin-like (Ca++ binding) repeats, including a very short triplet repeat, encoding five Asp (GAC5) slightly expanded in some patients
  • conjugated GlycoP
    mono polymer homomer , pentamer
    HOMOLOGY
    interspecies homolog to murine Comp
    Homologene
    FAMILY
  • thrombospondin family
  • noncollagenous extracellular matrix family
  • CATEGORY adhesion , structural protein
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text
  • in the extracellular matrix (ECM) of developing and mature cartilage, within and around the tendon, in ligament, synovium and the vitreous of the eye
  • COMP and ECM1 colocalize in the growth plates
  • basic FUNCTION
  • structural protein with modified conformation when calcium is removed
  • playing with MATN3 an important role in matrix assembly
  • may function to stabilize the articular cartilage extracellular matrix by specific cation-dependent interactions with matrix components, including collagen types II and IX, fibronectin, aggrecan, and matrilin-1, -3, and -4
  • may act as the co-factor of the GRN cell surface receptor and may present GRN to its receptor, followed by the activations of GRN-mediated signal transduction and gene regulation pathways
  • playing a role in catalyzing the assembly of collagen, promoting formation of well defined fibrils
  • promotes cell attachment via two independent mechanisms involving cell surface CD47 and alphaVbeta3 integrin (and consequence of cell attachment to COMP is the specific induction of fascin-stabilized actin microspikes) (Rock 2010)
  • pivotal for maintaining the homeostasis of vascular smooth muscle cells (VSMCs)
  • potential novel inhibitor of vascular calcificationand the imbalance between the effects of COMP and BMP2 may provide new insights into the pathophysiology of vascular calcification
  • functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS development
    text human limb development
    PATHWAY
    metabolism
    signaling
    a component
  • pentameric approximately 524 kDa multidomain extracellular matrix protein (R
  • INTERACTION
    DNA
    RNA
    small molecule metal binding,
  • Ca2+
  • protein
  • interacting with GRN (required for GRN-mediated chondrocyte proliferation, since chondrocyte proliferation induced by GRN is dramatically inhibited by an anti-COMP antibody)
  • ADAMTS12 is a new COMP-interacting and -degrading enzyme and thus may play an important role in the COMP degradation in the initiation and progression of arthritis
  • binding to collagens I and II is enhanced in the presence of Zn2+
  • ADAMTS7 facilitated intimal hyperplasia through degradation of inhibitory matrix protein COMP
  • ECM1 novel COMP-associated partner (EGF domain of COMP and the C-terminus of ECM1 mediate the interaction between them)
  • bound directly to BMP2 through the C-terminus, inhibited BMP2 receptor binding, and blocked BMP2 osteogenic signaling
  • COMP binds to COL12A1 and COL14A1 via their C-terminal collagenous domains, and three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin
  • ADAMTS7 facilitated vascular smooth muscle cell (VSMC) migration by degrading the extracellular matrix protein COMP and thereby promoted neointima formation following vascular mechanical injury
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) EDM1 , PSACH
    Susceptibility putative susceptibility gene for rheumatoid arthritis
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS