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agrin (AGRN)

Function: - component of the basal lamina - causes aggregation of acetylcholine receptors & acetylcholine-esterase on the surface of muscle fibers of the neuromuscular junction - binds to laminin Structure: - contains heparan sulfate chains as well as N-linked oligosaccharides & O-linked oligosaccharides (putative) - contains 4 EGF-like domains - contains 9 Kazal-like domains - contains 2 laminin EGF-like domains - contains 3 laminin G-like domains - contains 1 NtA (N-terminal agrin) domain - contains 1 SEA domain Compartment: - secreted, extracellular space, extracellular matrix - synaptic basal lamina at the neuromuscular junction

General

glycoprotein matrix protein

Properties

SIZE: MW = 215 kD entity length = 2045 aa COMPARTMENT: extracellular matrix MOTIF: NTA {30-157} MOTIF: N-glycosylation site {N135} Kazal-type serine protease inhibitor domain {170-750} (8) MOTIF: cysteine residue {X+0} MODIFICATION: cysteine residue {X+X4} cysteine residue {X+X1} MODIFICATION: cysteine residue {X+X3} cysteine residue {X+X2} MODIFICATION: cysteine residue {X+X5} cysteine residue {X+X3} MODIFICATION: cysteine residue {X+X1} cysteine residue {X+X4} MODIFICATION: cysteine residue {X+0} cysteine residue {X+X5} MODIFICATION: cysteine residue {X+X2} FOR-BINDING-OF: serine protease N-glycosylation site {N777} threonine-rich region {974-1099} MOTIF: threonine residue (SEVERAL) SEA {1130-1252} EGF domain {1329-1367} MOTIF: cysteine residue {C1333} MODIFICATION: cysteine residue {C1344} cysteine residue {C1338} MODIFICATION: cysteine residue {C1355} cysteine residue {C1344} MODIFICATION: cysteine residue {C1333} cysteine residue {C1355} MODIFICATION: cysteine residue {C1338} LAMININ G-LIKE {1372-2042} (3) MOTIF: cysteine residue {C1519} MODIFICATION: cysteine residue {C1548} cysteine residue {C1548} MODIFICATION: cysteine residue {C1519}

Database Correlations

OMIM 103320 UniProt O00468 PFAM correlations Entrez Gene 375790 Kegg hsa:375790

References

UniProt :accession O00468