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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

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_000095 19 - 2471 NP_000086 - 757 - 2007 17588949

EXPRESSION

Type

widely

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Cardiovascular vessel         Homo sapiens Adult Skeleton appendicular skeleton joint synovia   highly Visual eye anterior segment cornea

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Connective bone       Connective cartilage       Homo sapiens Adult Connective dense tendon   highly Connective dense ligament   highly

cells

System Cell Pubmed Species Stage Rna 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