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Ras-related protein ralB-A (XRalB-A)

 RALBA_XENLA             Reviewed;         206 AA.
Q9YH09; Q32N67;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 111.
RecName: Full=Ras-related protein ralB-A;
AltName: Full=XRalB-A;
Flags: Precursor;
Name=ralb-a;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-23; SER-28 AND ASP-49.
TISSUE=Oocyte;
PubMed=10328920; DOI=10.1006/dbio.1999.9254;
Moreau J., Lebreton S., Iouzalen N., Mechali M.;
"Characterization of Xenopus Ral B and its involvement in F-actin
control during early development.";
Dev. Biol. 209:268-281(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Oocyte;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH RALBP1 AND RAP1GDS1.
PubMed=9753634; DOI=10.1006/bbrc.1998.9336;
Iouzalen N., Camonis J., Moreau J.;
"Identification and characterization in Xenopus of XsmgGDS, a RalB-
binding protein.";
Biochem. Biophys. Res. Commun. 250:359-363(1998).
[4]
FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-23 AND SER-28.
PubMed=14576358; DOI=10.1242/jcs.00763;
Lebreton S., Boissel L., Moreau J.;
"Control of embryonic Xenopus morphogenesis by a Ral-GDS/Xral branch
of the Ras signalling pathway.";
J. Cell Sci. 116:4651-4662(2003).
[5]
FUNCTION, INTERACTION WITH RALBP1, AND MUTAGENESIS OF GLY-23; SER-28;
ASP-49 AND CYS-203.
TISSUE=Oocyte;
PubMed=15511640; DOI=10.1016/j.mod.2004.07.008;
Lebreton S., Boissel L., Iouzalen N., Moreau J.;
"RLIP mediates downstream signalling from RalB to the actin
cytoskeleton during Xenopus early development.";
Mech. Dev. 121:1481-1494(2004).
-!- 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 (By similarity). Required both
to stabilize the assembly of the exocyst complex and to localize
functional exocyst complexes to the leading edge of migrating
cells (By similarity). Required for suppression of apoptosis (By
similarity). In late stages of cytokinesis, upon completion of the
bridge formation between dividing cells, mediates exocyst
recruitment to the midbody to drive abscission (By similarity).
Regulates the actin cytoskeleton to play a role in gastrulation or
neurulation. During the cleavage stages, the GTP-bound form
induces a cortical reaction that affects the localization of
pigment granules. Activated by the FGF pathway via ras and ral-
GDS, but independently of raf. Directs ralbp1 to the plasma
membrane (PubMed:10328920, PubMed:14576358, PubMed:15511640).
{ECO:0000250|UniProtKB:P11234, ECO:0000250|UniProtKB:P36860,
ECO:0000269|PubMed:10328920, ECO:0000269|PubMed:14576358,
ECO:0000269|PubMed:15511640}.
-!- SUBUNIT: Interacts with ralbp1 and rap1gds1.
{ECO:0000269|PubMed:15511640, ECO:0000269|PubMed:9753634}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P11234}; Lipid-anchor
{ECO:0000250|UniProtKB:P11234}; Cytoplasmic side
{ECO:0000250|UniProtKB:P11234}. Midbody
{ECO:0000250|UniProtKB:P11234}. Note=During late cytokinesis,
enriched at the midbody. {ECO:0000250|UniProtKB:P11234}.
-!- TISSUE SPECIFICITY: Weakly expressed in adult tissues and highest
levels were found in heart, brain and testes.
{ECO:0000269|PubMed:10328920}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Detected from stage I oocyte up to the tadpole stage. Present at a
relatively high level until the gastrula stage, after which
expression levels decrease. During gastrulation, levels of protein
activation are highest in the embryonic mesodermal region.
{ECO:0000269|PubMed:10328920, ECO:0000269|PubMed:14576358}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y16259; CAA76143.1; -; mRNA.
EMBL; BC108805; AAI08806.1; -; mRNA.
RefSeq; NP_001084154.1; NM_001090685.1.
UniGene; Xl.5659; -.
ProteinModelPortal; Q9YH09; -.
SMR; Q9YH09; -.
IntAct; Q9YH09; 1.
GeneID; 399338; -.
KEGG; xla:399338; -.
CTD; 399338; -.
Xenbase; XB-GENE-6254042; ralb.
HOVERGEN; HBG009351; -.
KO; K07835; -.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0048070; P:regulation of developmental pigmentation; IMP:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR028412; Ral.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
PANTHER; PTHR24070:SF199; PTHR24070:SF199; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Prenylation.
CHAIN 1 203 Ras-related protein ralB-A.
/FTId=PRO_0000082701.
PROPEP 204 206 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281354.
NP_BIND 21 28 GTP. {ECO:0000250}.
NP_BIND 68 72 GTP. {ECO:0000250}.
NP_BIND 128 131 GTP. {ECO:0000250}.
MOTIF 43 51 Effector region.
MOD_RES 203 203 Cysteine methyl ester. {ECO:0000250}.
LIPID 203 203 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 23 23 G->V: Constitutively active. Displays
defective GTPase activity and fails to
respond to ral-GAP. Still able to bind
ralbp1. Injection into embryos disrupts
the actin cytoskeleton and the
localization of pigment granules.
{ECO:0000269|PubMed:10328920,
ECO:0000269|PubMed:14576358,
ECO:0000269|PubMed:15511640}.
MUTAGEN 28 28 S->N: Dominant negative. Shows decreased
GTP affinity. Injection into embryos
disrupts gastrulation.
{ECO:0000269|PubMed:10328920,
ECO:0000269|PubMed:14576358,
ECO:0000269|PubMed:15511640}.
MUTAGEN 49 49 D->N: Results are conflicting as to
whether binding of the GTP-bound form to
ralbp1 is abolished.
{ECO:0000269|PubMed:10328920,
ECO:0000269|PubMed:15511640}.
MUTAGEN 203 203 C->S: Defective in membrane targeting.
{ECO:0000269|PubMed:15511640}.
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


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