multimerin-1; emilin-4; elastin microfibril interface located protein 4; elastin microfibril interfacer 4; endothelial cell multimerin; contains: platelet glycoprotein Ia*; contains: 155 kD platelet multimerin; p-155; p155 (MMRN1, ECM, EMILIN4, GPIA* MMRN)

Function: 1) carrier protein for platelet factor V/Va* 2) storage & stabilization of factor V in platelets 3) upon release following platelet activation, may limit platelet & plasma factor Va-dependent thrombin generation 4) ligand for integrin alpha-IIb/beta-3 & integrin alpha-V/beta-3 on activated platelets, & may function as an extracellular matrix or adhesive protein 5) interacts with factor V/factor Va * not for plasma factor V/Va Structure: - the N-terminus is blocked - extensively N-glycosylated - multimeric - composed of varying sized, disulfide-linked multimers; the smallest is a homotrimer - proteolysis of the promultimerin in the N-terminal region, leads to the mature p155 form that is stored in platelets - contains 1 C1q domain - contains 1 EGF-like domain - contains 1 EMI domain Compartment: secreted (putative) Alternative splicing: named isoforms=2 Expression: - synthesized by endothelial cells & megakaryocytes - stored in platelet alpha granules & endothelial cell Weibel-Palade bodies, following activation of these cells - released & attached to megakaryocytes, platelets, endothelium & subendothelium of blood vessels - not found in plasma - found in vascular tissues such as placenta, lung, & liver Pathology: - deficiency in multimerin 1 due to proteolytic degradation within the platelet alpha granules is associated with factor V Quebec

General

emilin; elastin microfibril interface located protein multimerin

Properties

SIZE: entity length = 1228 aa MW = 138 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-19} N-glycosylation site {N21} N-glycosylation site {N97} N-glycosylation site {N114} N-glycosylation site {N120} N-glycosylation site {N136} Cell attachment site {186-188} serine-rich region {189-192} MOTIF: serine residue (SEVERAL) EMI {207-282} MOTIF: cysteine residue {C211} MODIFICATION: cysteine residue {C272} cysteine residue {C238} MODIFICATION: cysteine residue {C245} cysteine residue {C245} MODIFICATION: cysteine residue {C238} cysteine residue {C271} MODIFICATION: cysteine residue {C280} cysteine residue {C272} MODIFICATION: cysteine residue {C211} cysteine residue {C280} MODIFICATION: cysteine residue {C271} glutamine-rich region {309-313} MOTIF: glutamine residue (SEVERAL) coiled coil {333-365} MOTIF: N-glycosylation site {N344} coiled coil {400-430} N-glycosylation site {N431} coiled coil {503-523} MOTIF: N-glycosylation site {N507} N-glycosylation site {N541} N-glycosylation site {N576} coiled coil {580-650} MOTIF: N-glycosylation site {N618} coiled coil {675-726} MOTIF: N-glycosylation site {N680} N-glycosylation site {N729} N-glycosylation site {N783} N-glycosylation site {N816} coiled coil {819-869} MOTIF: N-glycosylation site {N828} N-glycosylation site {N840} N-glycosylation site {N921} N-glycosylation site {N933} N-glycosylation site {N942} N-glycosylation site {N981} N-glycosylation site {N1020} EGF domain {1041-1077} MOTIF: cysteine residue {C1045} MODIFICATION: cysteine residue {C1056} cysteine residue {C1050} MODIFICATION: cysteine residue {C1065} cysteine residue {C1056} MODIFICATION: cysteine residue {C1045} cysteine residue {C1065} MODIFICATION: cysteine residue {C1050} cysteine residue {C1067} MODIFICATION: cysteine residue {C1076} N-glycosylation site {N1075} cysteine residue {C1076} MODIFICATION: cysteine residue {C1067} C1q {1096-1228}

Database Correlations

OMIM 601456 UniProt Q13201 PFAM correlations Entrez Gene 22915 Kegg hsa:22915

References

UniProt :accession Q13201