Rala
entrez
56044
canonical
uniprot
P63321
canonical
ensembl
ENSMUSG00000008859
resolver
ensp
ENSMUSP00000009003
resolver
enst
ENSMUST00000009003
resolver
genesymbol
Rala
resolver
genesymbol_syn
Ral
resolver
genesymbol_syn
Ral-a
resolver
uniprot
P05810
resolver
uniprot_entry
RALA_MOUSE
resolver
uniprot_sec
P05810
resolver
activity_regulation
ACTIVITY 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).
uniprot
proteins
amino_acid_sequence
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRADQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
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. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells (By similarity). The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling (PubMed:20005108). During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (By similarity). During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B-CDK1 (By similarity). {ECO:0000250|UniProtKB:P11233, ECO:0000269|PubMed:20005108}.
uniprot
proteins
mass_dalton
23553
uniprot
proteins
post_translational_modification
PTM: Prenylation is essential for membrane localization. {ECO:0000250|UniProtKB:P11233}.; PTM: Phosphorylated. Phosphorylation at Ser-194 by AURKA/Aurora kinase A, during mitosis, induces RALA localization to the mitochondrion where it regulates mitochondrial fission. {ECO:0000250|UniProtKB:P11233}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
11025226
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20005108
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8570186
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11233}; Lipid-anchor {ECO:0000250|UniProtKB:P11233}; Cytoplasmic side {ECO:0000250|UniProtKB:P11233}. Cleavage furrow {ECO:0000250|UniProtKB:P11233}. Midbody, Midbody ring {ECO:0000250|UniProtKB:P11233}. Mitochondrion {ECO:0000250|UniProtKB:P11233}. Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles. May colocalize with CNTRL/centriolin at the midbody ring. However, localization at the midbody at late cytokinesis was not confirmed. Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission. {ECO:0000250|UniProtKB:P11233}.
uniprot
proteins