triple functional domain protein (PTPRF-interacting protein, TRIO)

Function: 1) promotes the exchange of GDP by GTP 2) coordinates cell-matrix & cytoskeletal rearrangements for cell migration & growth in association with LAR 3) forms complex with leukocyte antigen related protein (LAR) 4) N-terminal DBL domain specifically catalyzes nucleotide exchange for RAC1, leading to the activation of Jun kinase & production of membrane ruffles 5) the 2nd DBL domain is an exchange factor for RhoA & induces formation of stress fibers 6) phosphorylated on serine residue(s) Structure: - contains 1 CRAL-TRIO domain - contains 2 DBL domains - contains 1 Ig-like C2-type domain (immunoglobulin-like domain) - contains 2 PH domains - contains 1 protein kinase domain - contains 2 SH3 domains - contains 4 spectrin repeats Alternative splicing: named isoforms=2 Expression: - expressed in heart, skeletal muscle, brain, pancreas, placenta, liver, kidney, lung

General

guanine nucleotide exchange factor (GDP/GTP dissociation stimulator, guanine nucleotide-releasing factor/protein, GNEF, GNDS, GDS) protein kinase

Properties

SIZE: MW = 342 kD entity length = 3038 aa STATE: active state MOTIF: CRAL-TRIO lipid binding domain {6-151} Spectrin {252-359} Spectrin {479-585} glutamine-rich region {656-659} MOTIF: glutamine residue (SEVERAL) Spectrin {819-925} Spectrin {1050-1157} DH 1 {1233-1408} PH domain {1421-1532} MOTIF: Thr phosphorylation site {T1486} src homology 3 [SH3] domain SITE: 1597-1653 serine-rich region {1786-1791} MOTIF: serine residue (SEVERAL) DH 2 {1910-2086} PH domain {2098-2212} glycine-rich region {2233-2253} serine-rich region {2486-2492} MOTIF: serine residue (SEVERAL) src homology 3 [SH3] domain SITE: 2492-2557 immunoglobulin superfamily domain {2626-2716} MOTIF: cysteine residue {C2637} MODIFICATION: cysteine residue {C2700} cysteine residue {C2700} MODIFICATION: cysteine residue {C2637} kinase domain SITE: 2737-2993 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 2743-2751 ATP-binding site NAME: ATP-binding site SITE: 2766-2766 aspartate residue {D2856}

Database Correlations

OMIM 601893 UniProt O75962 PFAM correlations

References

UniProt :accession O75962