The domain within your query sequence starts at position 50 and ends at position 102; the E-value for the Laminin_N domain shown below is 6.2e-16.



PFAM accession number:PF00055
Interpro abstract (IPR008211):

Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. It is thought to mediate the attachment, migration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components [ (PUBMED:1975589) ]. Each laminin is a heterotrimer assembled from alpha, beta and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices [ (PUBMED:10842354) ].

Basement membrane assembly is a cooperative process in which laminins polymerise through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains. Netrins may also associate with this network through heterotypic LN domain interactions [ (PUBMED:8349613) ]. This leads to cell signalling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the alpha 2 laminin chain [ (PUBMED:7874173) ]. The laminin N-terminal domain is found in all laminin and netrin subunits except laminin alpha 3A, alpha 4 and gamma 2.

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