The domain within your query sequence starts at position 1836 and ends at position 2102; the E-value for the Laminin_I domain shown below is 2.7e-93.
ELRLVKSKLQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHL NREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEG TDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVENN GLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKN DFTKYLATADSSLLQTNNLLQQMDKSQ
Laminin_I |
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PFAM accession number: | PF06008 |
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Interpro abstract (IPR009254): | Laminins are glycoproteins that are major constituents of the basement membrane of cells. Laminins are trimeric molecules; laminin-1 is an alpha1 beta1 gamma1 trimer. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure [ (PUBMED:3182802) ]. Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components. |
GO process: | regulation of cell adhesion (GO:0030155), regulation of embryonic development (GO:0045995), regulation of cell migration (GO:0030334) |
GO function: | signaling receptor binding (GO:0005102) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Laminin_I