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MGP002572

UniProt Annotations

Entry Information

Gene Name	v-ral simian leukemia viral oncogene homolog A (ras related)
Protein Entry	RALA_HUMAN
UniProt ID	P11233
Species	Human

Comments

Comment type	Description
Enzyme Regulation	Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase- activating protein (GAP).
Function	Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin- dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. {ECO:0000269\|PubMed:18756269, ECO:0000269\|PubMed:19306925, ECO:0000269\|PubMed:20005108}.
Induction	Activated in an LPA-dependent manner by LPAR1 and in an LPA-independent manner by LPAR2. {ECO:0000269\|PubMed:19306925}.
Interaction	O54921:Exoc2 (xeno); NbExp=2; IntAct=EBI-1036803, EBI-1036795; P30154:PPP2R1B; NbExp=6; IntAct=EBI-1036803, EBI-357094;
Ptm	Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). {ECO:0000269\|PubMed:17875936, ECO:0000269\|PubMed:1903399}.
Similarity	Belongs to the small GTPase superfamily. Ras family. {ECO:0000305}.
Subcellular Location	Cell surface. Cell membrane; Lipid-anchor; Cytoplasmic side. Cleavage furrow. Midbody. Note=Prior to LPA treatment found predominantly at the cell surface and in the presence of LPA colocalizes with LPAR1 and LPAR2 in the endocytic vesicles. During early cytokinesis localizes at the cleavage furrow membrane. Colocalizes with EXOC2 at the early midbody ring and persists there till maturation of the midbody.
Subunit	Interacts with RALBP1 via its effector domain. Interacts with EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites and compete for RALA binding. Interacts with Clostridium exoenzyme C3. Interacts with RALGPS1. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in response to LPAR1 activation. RALA and ADRBK1 mutually inhibit each other's binding to LPAR1. {ECO:0000269\|PubMed:10747847, ECO:0000269\|PubMed:14525976, ECO:0000269\|PubMed:15809419, ECO:0000269\|PubMed:15920473, ECO:0000269\|PubMed:16177825, ECO:0000269\|PubMed:19306925, ECO:0000269\|PubMed:7673236}.