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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