ID:GRDN_HUMAN DESCRIPTION: RecName: Full=Girdin; AltName: Full=Akt phosphorylation enhancer; Short=APE; AltName: Full=Coiled-coil domain-containing protein 88A; AltName: Full=G alpha-interacting vesicle-associated protein; Short=GIV; AltName: Full=Girders of actin filament; AltName: Full=Hook-related protein 1; Short=HkRP1; FUNCTION: Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB, but does not possess kinase activity itself. Phosphorylation of AKT1/PKB thereby induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Essential for the integrity of the actin cytoskeleton and for cell migration. Required for formation of actin stress fibers and lamellipodia. May be involved in membrane sorting in the early endosome. SUBUNIT: Interacts (via C-terminus) with DISC1; the interaction is direct. Interacts with AKT proteins; the interaction is inhibited in presence of DISC1 (By similarity). Homodimer. The non- phosphorylated form interacts with phosphatidylinositol 4- phosphate [PI(4)P] and weakly with phosphatidylinositol 3- phosphate [PI(3)P]. Interacts with microtubules. Interacts with actin through its C-terminal domain. Interacts with the C-terminus of AKT1/PKB. SUBCELLULAR LOCATION: Membrane. Cell membrane. Cytoplasm, cytosol. Cytoplasmic vesicle. Cell projection, lamellipodium. Note=Localizes to the cell membrane through interaction with phosphoinositides. TISSUE SPECIFICITY: Expressed ubiquitously. PTM: Phosphorylation is induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner. Phosphorylation by AKT1/PKB is necessary for the delocalization from the cell membrane and for cell migration. SIMILARITY: Belongs to the CCDC88 family. SEQUENCE CAUTION: Sequence=AAY14932.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=CAD97945.1; Type=Miscellaneous discrepancy; Note=Intron retention at the C-terminus; Sequence=CAI46020.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q3V6T2
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0003779 actin binding GO:0008017 microtubule binding GO:0035091 phosphatidylinositol binding GO:0042803 protein homodimerization activity GO:0043422 protein kinase B binding GO:0051959 dynein light intermediate chain binding
Biological Process: GO:0001932 regulation of protein phosphorylation GO:0006260 DNA replication GO:0006275 regulation of DNA replication GO:0007399 nervous system development GO:0010975 regulation of neuron projection development GO:0016477 cell migration GO:0030030 cell projection organization GO:0030032 lamellipodium assembly GO:0030705 cytoskeleton-dependent intracellular transport GO:0031122 cytoplasmic microtubule organization GO:0031929 TOR signaling GO:0032148 activation of protein kinase B activity GO:0032956 regulation of actin cytoskeleton organization GO:0042127 regulation of cell proliferation GO:0045724 positive regulation of cilium assembly GO:0061024 membrane organization GO:1903566 positive regulation of protein localization to cilium