The domain within your query sequence starts at position 32 and ends at position 159; the E-value for the NtA domain shown below is 5.1e-91.



PFAM accession number:PF03146
Interpro abstract (IPR004850):

Agrin is a multidomain heparan sulphate proteoglycan, that is a key organiser for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain [ (PUBMED:9321698) ]. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The NtA domain forms the most N-terminal part, followed by 9 Kazal-like domains and 2 LE domains. The C-terminal part consists of a SEA domain, 4 EGF-like domains and 3 Laminin G domains, responsible for the clustering of acetylcholine receptors [ (PUBMED:11473262) ].

Tertiairy structures show that the NtA domain folds as a beta-barrel core flanked by N- and C-terminal helical regions. The core of the domain consists of 5 beta-strands that form 2 beta-sheets. The structure belongs to the OB fold family and shows similarity with the protease inhibition domain of TIMP-1, suggesting alternative functions for agrin in addition to synaptogenic activity [ (PUBMED:11473262) ]. Residues Leu 117 and Val 124 in helix 3 of the NtA domain are essential for binding to the laminin gamma1 chain [ (PUBMED:12554653) ].

GO process:receptor clustering (GO:0043113), G protein-coupled acetylcholine receptor signaling pathway (GO:0007213)
GO function:laminin binding (GO:0043236)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NtA