SMART: Pfam domain GAPT

The domain within your query sequence starts at position 1 and ends at position 155; the E-value for the GAPT domain shown below is 2.5e-77.

MLECFESSPVAVAVGVSLLVLLLLCGIGCAWHWNRRESTPFTLPKFMQRRSSRQKDVTKT
VSSSAYVISPSMKASVESKGHKSTAKRNKMHGNYENVEVCPPCTEGTTEKALYENTQPSN
LEEHVYGNQTDPLYYNFQKPSPPPPQDDDIYILPD

GAPT

PFAM accession number:	PF11770
Interpro abstract (IPR021082):	Protein GAPT (also known as Growth-factor Receptor-Bound protein 2 (GRB2)-binding adaptor protein, transmembrane) belongs to a class of transmembrane (TM) adaptor proteins that couple antigen receptor engagement to downstream signalling cascades in lymphocytes [ (PUBMED:18559951) ]. Expressed in B cells and myeloid cells, GAPT negatively regulates B-cell proliferation following stimulation through the B-cell receptor; it may also play an important role in the proper maintenance of marginal zone B-cells [ (PUBMED:18559951) ]. GAPT has an extracellular domain, a TM domain, and a cytoplasmic tail with multiple GRB2-binding motifs; it constitutively associates with GRB2 SH3 domains via a proline-rich region [ (PUBMED:18559951) ]. Its cytosolic domain contains 7 tyrosine residues (4 of them within GRB2-binding motifs), and 2 cysteines in the juxta-membrane region, which may be palmitoylated [ (PUBMED:18559951) ].
GO component:	integral component of membrane (GO:0016021)

PFAM accession number:

PF11770

Interpro abstract (IPR021082):

Protein GAPT (also known as Growth-factor Receptor-Bound protein 2 (GRB2)-binding adaptor protein, transmembrane) belongs to a class of transmembrane (TM) adaptor proteins that couple antigen receptor engagement to downstream signalling cascades in lymphocytes [ (PUBMED:18559951) ]. Expressed in B cells and myeloid cells, GAPT negatively regulates B-cell proliferation following stimulation through the B-cell receptor; it may also play an important role in the proper maintenance of marginal zone B-cells [ (PUBMED:18559951) ].

GAPT has an extracellular domain, a TM domain, and a cytoplasmic tail with multiple GRB2-binding motifs; it constitutively associates with GRB2 SH3 domains via a proline-rich region [ (PUBMED:18559951) ]. Its cytosolic domain contains 7 tyrosine residues (4 of them within GRB2-binding motifs), and 2 cysteines in the juxta-membrane region, which may be palmitoylated [ (PUBMED:18559951) ].

GO component:

integral component of membrane (GO:0016021)

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