RALB_MOUSE
ID RALB_MOUSE Reviewed; 206 AA.
AC Q9JIW9; Q3TVS5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Ral-B;
DE EC=3.6.5.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=Ralb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11025226; DOI=10.1016/s0925-4773(00)00427-5;
RA Zhao Z., Rivkees S.A.;
RT "Tissue-specific expression of GTPas RalA and RalB during embryogenesis and
RT regulation by epithelial-mesenchymal interaction.";
RL Mech. Dev. 97:201-204(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). Involved in ligand-dependent receptor
CC mediated endocytosis of the EGF and insulin receptors (By similarity).
CC {ECO:0000250|UniProtKB:P11234, ECO:0000250|UniProtKB:P36860}.
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 -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Interacts with EXOC2/Sec5 and EXOC8/Exo84 (By similarity).
CC Interacts (via effector domain) with RALBP1 (By similarity).
CC {ECO:0000250|UniProtKB:P11234}.
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 -!- PTM: Prenylation is essential for membrane localization.
CC {ECO:0000250|UniProtKB:P11234}.
CC -!- PTM: The farnesylated form confers resistance to the proapoptotic and
CC anti-anchorage-dependent growth effects of some
CC geranylgeranyltransferase I inhibitors. {ECO:0000250|UniProtKB:P11234}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF174296; AAF89875.1; -; mRNA.
DR EMBL; AK017698; BAB30881.1; -; mRNA.
DR EMBL; AK159993; BAE35543.1; -; mRNA.
DR EMBL; BC006907; AAH06907.1; -; mRNA.
DR CCDS; CCDS15225.1; -.
DR RefSeq; NP_071722.1; NM_022327.5.
DR RefSeq; XP_006529845.1; XM_006529782.1.
DR AlphaFoldDB; Q9JIW9; -.
DR SMR; Q9JIW9; -.
DR BioGRID; 211033; 2.
DR IntAct; Q9JIW9; 3.
DR STRING; 10090.ENSMUSP00000004565; -.
DR iPTMnet; Q9JIW9; -.
DR PhosphoSitePlus; Q9JIW9; -.
DR SwissPalm; Q9JIW9; -.
DR EPD; Q9JIW9; -.
DR jPOST; Q9JIW9; -.
DR MaxQB; Q9JIW9; -.
DR PaxDb; Q9JIW9; -.
DR PeptideAtlas; Q9JIW9; -.
DR PRIDE; Q9JIW9; -.
DR ProteomicsDB; 300348; -.
DR Antibodypedia; 33389; 373 antibodies from 36 providers.
DR DNASU; 64143; -.
DR Ensembl; ENSMUST00000004565; ENSMUSP00000004565; ENSMUSG00000004451.
DR GeneID; 64143; -.
DR KEGG; mmu:64143; -.
DR UCSC; uc007cis.2; mouse.
DR CTD; 5899; -.
DR MGI; MGI:1927244; Ralb.
DR VEuPathDB; HostDB:ENSMUSG00000004451; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155984; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q9JIW9; -.
DR OMA; QNITEMF; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q9JIW9; -.
DR TreeFam; TF312796; -.
DR BioGRID-ORCS; 64143; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ralb; mouse.
DR PRO; PR:Q9JIW9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JIW9; protein.
DR Bgee; ENSMUSG00000004451; Expressed in granulocyte and 257 other tissues.
DR ExpressionAtlas; Q9JIW9; baseline and differential.
DR Genevisible; Q9JIW9; MM.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0001928; P:regulation of exocyst assembly; ISS:UniProtKB.
DR GO; GO:0060178; P:regulation of exocyst localization; 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 1: Evidence at protein level;
KW Apoptosis; Cell cycle; Cell division; Cell membrane; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome.
FT CHAIN 1..203
FT /note="Ras-related protein Ral-B"
FT /id="PRO_0000082699"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281351"
FT REGION 181..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..51
FT /note="Effector region"
FT BINDING 21..29
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 BINDING 158..160
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"
SQ SEQUENCE 206 AA; 23349 MW; 6CA5994C74221232 CRC64;
MAANKGKSQG SLVLHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKSEEDK
IPLLVVGNKS DLEERRQVPV DEARGKAEEW GVQYVETSAK TRANVDKVFF DLMREIRAKK
MSENKDKNGR KSSKSKKSFK ERCCLL
