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lactadherin (milk fat globule-EGF factor 8, MFG-E8, HMFG, breast epithelial antigen BA46, MFGM, [Contains: Lactadherin short form; Medin], MFGE8)

Function: 1) specific ligand for the alpha-v/beta-3 & alpha-v/beta-5 receptors 2) also binds to phosphatidylserine-enriched cell surfaces (receptor-independen) 3) binds zona pellucida, role in gamete interaction Structure: - medin has a ragged N-terminus with minor species starting at Pro-264 and Gly-273 - contains 1 EGF-like domain - contains 2 F5/8 type C domains Compartment: membrane, peripheral membrane Expression: - expressed on mammary epithelial cell surfaces & in aortic media Pathology: - binds specifically to rotavirus & inhibits its replication - medin is the main constituent of aortic medial amyloid - overexpressed in several carcinomas

General

glycoprotein membrane protein

Properties

SIZE: MW = 43 kD entity length = 387 aa COMPARTMENT: cellular membrane MOTIF: signal sequence {1-23} EGF domain {24-67} MOTIF: cysteine residue {C27} MODIFICATION: cysteine residue {C38} cysteine residue {C32} MODIFICATION: cysteine residue {C55} cysteine residue {C38} MODIFICATION: cysteine residue {C27} Cell attachment {46-48} cysteine residue {C55} MODIFICATION: cysteine residue {C32} cysteine residue {C57} MODIFICATION: cysteine residue {C66} cysteine residue {C66} MODIFICATION: cysteine residue {C57} coagulation factors 5/8 type C domain (FA58C) {70-225} MOTIF: cysteine residue {C70} MODIFICATION: cysteine residue {C225} cysteine residue {C212} MODIFICATION: cysteine residue {C216} cysteine residue {C216} MODIFICATION: cysteine residue {C212} cysteine residue {C225} MODIFICATION: cysteine residue {C70} coagulation factors 5/8 type C domain (FA58C) {230-387} MOTIF: cysteine residue {C230} MODIFICATION: cysteine residue {C387} N-glycosylation site {N238} N-glycosylation site {N325} N-glycosylation site {N329} N-glycosylation site {N350} cysteine residue {C387} MODIFICATION: cysteine residue {C230}

Database Correlations

OMIM 602281 UniProt Q08431 PFAM correlations

References

UniProt :accession Q08431