RALBA_XENLA
ID RALBA_XENLA Reviewed; 206 AA.
AC Q9YH09; Q32N67;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ras-related protein ralB-A;
DE EC=3.6.5.2 {ECO:0000305};
DE AltName: Full=XRalB-A;
DE Flags: Precursor;
GN Name=ralb-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF GLY-23; SER-28 AND ASP-49.
RC TISSUE=Oocyte;
RX PubMed=10328920; DOI=10.1006/dbio.1999.9254;
RA Moreau J., Lebreton S., Iouzalen N., Mechali M.;
RT "Characterization of Xenopus Ral B and its involvement in F-actin control
RT during early development.";
RL Dev. Biol. 209:268-281(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH RALBP1 AND RAP1GDS1.
RX PubMed=9753634; DOI=10.1006/bbrc.1998.9336;
RA Iouzalen N., Camonis J., Moreau J.;
RT "Identification and characterization in Xenopus of XsmgGDS, a RalB-binding
RT protein.";
RL Biochem. Biophys. Res. Commun. 250:359-363(1998).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-23 AND SER-28.
RX PubMed=14576358; DOI=10.1242/jcs.00763;
RA Lebreton S., Boissel L., Moreau J.;
RT "Control of embryonic Xenopus morphogenesis by a Ral-GDS/Xral branch of the
RT Ras signalling pathway.";
RL J. Cell Sci. 116:4651-4662(2003).
RN [5]
RP FUNCTION, INTERACTION WITH RALBP1, AND MUTAGENESIS OF GLY-23; SER-28;
RP ASP-49 AND CYS-203.
RC TISSUE=Oocyte;
RX PubMed=15511640; DOI=10.1016/j.mod.2004.07.008;
RA Lebreton S., Boissel L., Iouzalen N., Moreau J.;
RT "RLIP mediates downstream signalling from RalB to the actin cytoskeleton
RT during Xenopus early development.";
RL Mech. Dev. 121:1481-1494(2004).
CC -!- FUNCTION: Multifunctional GTPase involved in a variety of cellular
CC processes including gene expression, cell migration, cell
CC proliferation, oncogenic transformation and membrane trafficking.
CC Accomplishes its multiple functions by interacting with distinct
CC downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis
CC of dense core vesicles (By similarity). Required both to stabilize the
CC assembly of the exocyst complex and to localize functional exocyst
CC complexes to the leading edge of migrating cells (By similarity).
CC Required for suppression of apoptosis (By similarity). In late stages
CC of cytokinesis, upon completion of the bridge formation between
CC dividing cells, mediates exocyst recruitment to the midbody to drive
CC abscission (By similarity). Regulates the actin cytoskeleton to play a
CC role in gastrulation or neurulation. During the cleavage stages, the
CC GTP-bound form induces a cortical reaction that affects the
CC localization of pigment granules. Activated by the FGF pathway via ras
CC and ral-GDS, but independently of raf. Directs ralbp1 to the plasma
CC membrane (PubMed:10328920, PubMed:14576358, PubMed:15511640). Involved
CC in ligand-dependent receptor mediated endocytosis of the EGF and
CC insulin receptors (By similarity). {ECO:0000250|UniProtKB:P11234,
CC ECO:0000250|UniProtKB:P36860, ECO:0000269|PubMed:10328920,
CC ECO:0000269|PubMed:14576358, ECO:0000269|PubMed:15511640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with ralbp1 and rap1gds1.
CC {ECO:0000269|PubMed:15511640, ECO:0000269|PubMed:9753634}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11234};
CC Lipid-anchor {ECO:0000250|UniProtKB:P11234}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P11234}. Midbody {ECO:0000250|UniProtKB:P11234}.
CC Note=During late cytokinesis, enriched at the midbody.
CC {ECO:0000250|UniProtKB:P11234}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in adult tissues and highest
CC levels were found in heart, brain and testes.
CC {ECO:0000269|PubMed:10328920}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Detected from stage I oocyte up to the tadpole stage. Present at a
CC relatively high level until the gastrula stage, after which expression
CC levels decrease. During gastrulation, levels of protein activation are
CC highest in the embryonic mesodermal region.
CC {ECO:0000269|PubMed:10328920, ECO:0000269|PubMed:14576358}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; Y16259; CAA76143.1; -; mRNA.
DR EMBL; BC108805; AAI08806.1; -; mRNA.
DR RefSeq; NP_001084154.1; NM_001090685.1.
DR AlphaFoldDB; Q9YH09; -.
DR SMR; Q9YH09; -.
DR IntAct; Q9YH09; 1.
DR PRIDE; Q9YH09; -.
DR DNASU; 399338; -.
DR GeneID; 399338; -.
DR KEGG; xla:399338; -.
DR CTD; 399338; -.
DR Xenbase; XB-GENE-6254042; ralb.L.
DR OMA; IIEHESF; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 399338; Expressed in egg cell and 19 other tissues.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR028412; Ral.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR PANTHER; PTHR24070:SF199; PTHR24070:SF199; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..203
FT /note="Ras-related protein ralB-A"
FT /id="PRO_0000082701"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281354"
FT REGION 180..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..51
FT /note="Effector region"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="G->V: Constitutively active. Displays defective
FT GTPase activity and fails to respond to ral-GAP. Still able
FT to bind ralbp1. Injection into embryos disrupts the actin
FT cytoskeleton and the localization of pigment granules."
FT /evidence="ECO:0000269|PubMed:10328920,
FT ECO:0000269|PubMed:14576358, ECO:0000269|PubMed:15511640"
FT MUTAGEN 28
FT /note="S->N: Dominant negative. Shows decreased GTP
FT affinity. Injection into embryos disrupts gastrulation."
FT /evidence="ECO:0000269|PubMed:10328920,
FT ECO:0000269|PubMed:14576358, ECO:0000269|PubMed:15511640"
FT MUTAGEN 49
FT /note="D->N: Results are conflicting as to whether binding
FT of the GTP-bound form to ralbp1 is abolished."
FT /evidence="ECO:0000269|PubMed:10328920,
FT ECO:0000269|PubMed:15511640"
FT MUTAGEN 203
FT /note="C->S: Defective in membrane targeting."
FT /evidence="ECO:0000269|PubMed:15511640"
SQ SEQUENCE 206 AA; 23421 MW; E35BA92D04606AF7 CRC64;
MAANKNKNQS SLVLHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK
IPLLIVGNKS DLEDRRQVPM DEARGKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK
MSENKDKNGK KSGKSKKGFK QRCCLL
