RALA

V-ral simian leukemia viral oncogene homolog A (ras related)
PDB rendering based on 1u8y.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1UAD, 1ZC3, 1ZC4, 2A78, 2A9K, 2BOV
Identifiers
Symbols	RALA ; RAL
External IDs	OMIM: 179550 MGI: 1927243 HomoloGene: 3942 GeneCards: RALA Gene
Gene ontology Molecular function • GTPase activity • protein binding • GTP binding • Edg-2 lysophosphatidic acid receptor binding Cellular component • plasma membrane • cell surface • endocytic vesicle • midbody • cytoplasmic vesicle membrane • cleavage furrow • extracellular vesicular exosome Biological process • cytokinesis • GTP catabolic process • exocytosis • chemotaxis • signal transduction • Ras protein signal transduction • viral process • regulation of exocytosis • actin cytoskeleton reorganization • neurotrophin TRK receptor signaling pathway • positive regulation of filopodium assembly • membrane raft localization • membrane organization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5898	56044
Ensembl	ENSG00000006451	ENSMUSG00000008859
UniProt	P11233	P63321
RefSeq (mRNA)	NM_005402	NM_019491
RefSeq (protein)	NP_005393	NP_062364
Location (UCSC)	Chr 7: 39.66 – 39.75 Mb	Chr 13: 17.88 – 17.94 Mb
PubMed search

Ras-related protein Ral-A is a protein that in humans is encoded by the RALA gene.^[1][2]

Function

The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins.^[2]

The direct effects of RalA are uncertain, but it has been shown to play a significant role in filopodia formation^[3] and activity-dependent growth of postsynaptic membranes^[4] through its interactions with several downstream mediators including the exocyst complex.

Interactions

RALA has been shown to interact with:

• Filamin,^[5]
• PLD1,^[6][7] and
• RALBP1.^{[8][9][10][11]}

References

Further reading

PDB gallery 1u8y: CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap  1u8z: Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap  1u90: Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap  1uad: Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex  1zc3: Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA  1zc4: Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA  2a78: Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme  2a9k: Crystal structure of the C3bot-NAD-RalA complex reveals a novel type of action of a bacterial exoenzyme  2bov: MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE