RALBB_XENLA
ID RALBB_XENLA Reviewed; 206 AA.
AC Q6IP71;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ras-related protein ralB-B;
DE EC=3.6.5.2 {ECO:0000305};
DE AltName: Full=XRalB-B;
DE Flags: Precursor;
GN Name=ralb-b;
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] {ECO:0000312|EMBL:AAH72046.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH72046.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. Required both to stabilize the assembly of the
CC exocyst complex and to localize functional exocyst complexes to the
CC leading edge of migrating cells (By similarity). Required for
CC suppression of apoptosis. In late stages of cytokinesis, upon
CC completion of the bridge formation between dividing cells, mediates
CC exocyst recruitment to the midbody to drive abscission (By similarity).
CC Regulates the actin cytoskeleton to play a role in gastrulation or
CC neurulation. During the cleavage stages, the GTP-bound form induces a
CC cortical reaction that affects the localization of pigment granules.
CC Activated by the FGF pathway via ras and ral-GDS, but independently of
CC raf. Directs ralbp1 to the plasma membrane (By similarity). Involved in
CC ligand-dependent receptor mediated endocytosis of the EGF and insulin
CC receptors (By similarity). {ECO:0000250|UniProtKB:P11234,
CC ECO:0000250|UniProtKB:P36860, ECO:0000250|UniProtKB:Q9YH09}.
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:0000250|UniProtKB:Q9YH09}.
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000255}.
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DR EMBL; BC072046; AAH72046.1; -; mRNA.
DR RefSeq; NP_001085234.1; NM_001091765.1.
DR AlphaFoldDB; Q6IP71; -.
DR SMR; Q6IP71; -.
DR IntAct; Q6IP71; 2.
DR DNASU; 432329; -.
DR GeneID; 432329; -.
DR KEGG; xla:432329; -.
DR CTD; 432329; -.
DR Xenbase; XB-GENE-6255413; ralb.S.
DR OMA; QNITEMF; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 432329; Expressed in internal ear and 19 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0048070; P:regulation of developmental pigmentation; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS: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 2: Evidence at transcript 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-B"
FT /id="PRO_0000228813"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281355"
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|UniProtKB:P01112"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
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|UniProtKB:P48555"
SQ SEQUENCE 206 AA; 23393 MW; 68DDD391C21AC8D6 CRC64;
MAANKNKNQS SLVLHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK
IPLLVVGNKS DLEDRRQVPM DEARGKAEEW GVQYVETSAK TRANVDKVFF DLMREVRTKK
MSENKDKNGK KSGKSKKGFK QRCCLL
