RAB2B_MOUSE
ID RAB2B_MOUSE Reviewed; 216 AA.
AC P59279; Q3TV67;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ras-related protein Rab-2B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:Q8WUD1};
GN Name=Rab2b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Hypothalamus, Stomach, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [4]
RP FUNCTION, INTERACTION WITH GARIN5A, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP SER-20 AND GLN-65, AND CATALYTIC ACTIVITY.
RX PubMed=28930687; DOI=10.1016/j.celrep.2017.08.085;
RA Takahama M., Fukuda M., Ohbayashi N., Kozaki T., Misawa T., Okamoto T.,
RA Matsuura Y., Akira S., Saitoh T.;
RT "The RAB2B-GARIL5 Complex Promotes Cytosolic DNA-Induced Innate Immune
RT Responses.";
RL Cell Rep. 20:2944-2954(2017).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH GARIN1B, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-20 AND GLN-65.
RX PubMed=34714330; DOI=10.1242/dev.199644;
RA Morohoshi A., Miyata H., Oyama Y., Oura S., Noda T., Ikawa M.;
RT "FAM71F1 binds to RAB2A and RAB2B and is essential for acrosome formation
RT and male fertility in mice.";
RL Development 148:0-0(2021).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between active GTP-bound and inactive
CC GDP-bound states (PubMed:28930687). In their active state, drive
CC transport of vesicular carriers from donor organelles to acceptor
CC organelles to regulate the membrane traffic that maintains organelle
CC identity and morphology (PubMed:28930687). Regulates the compacted
CC morphology of the Golgi (By similarity). Promotes cytosolic DNA-induced
CC innate immune responses. Regulates IFN responses against DNA viruses by
CC regulating the CGAS-STING signaling axis (PubMed:28930687).
CC {ECO:0000250|UniProtKB:Q8WUD1, ECO:0000269|PubMed:28930687}.
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|PubMed:28930687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:28930687};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. {ECO:0000305}.
CC -!- SUBUNIT: Interacts (in GTP-bound form) with GARIN4 (via N-terminus) (By
CC similarity). Interacts (in GTP-bound form) with GARIN5A
CC (PubMed:28930687). Interacts (in GTP-bound form) with GARIN1B
CC (PubMed:34714330). {ECO:0000250|UniProtKB:Q8WUD1,
CC ECO:0000269|PubMed:28930687, ECO:0000269|PubMed:34714330}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:28930687, ECO:0000269|PubMed:34714330};
CC Lipid-anchor {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:34714330}. Note=Localized in the Golgi
CC apparatus in the round spermatids and in the acrosome in the elongating
CC spermatid. {ECO:0000269|PubMed:34714330}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK038393; BAC29983.1; -; mRNA.
DR EMBL; AK044202; BAC31814.1; -; mRNA.
DR EMBL; AK160249; BAE35713.1; -; mRNA.
DR EMBL; AK160351; BAE35753.1; -; mRNA.
DR EMBL; BC046334; AAH46334.1; -; mRNA.
DR CCDS; CCDS27052.1; -.
DR RefSeq; NP_766189.1; NM_172601.3.
DR AlphaFoldDB; P59279; -.
DR SMR; P59279; -.
DR BioGRID; 218074; 2.
DR IntAct; P59279; 6.
DR STRING; 10090.ENSMUSP00000022765; -.
DR iPTMnet; P59279; -.
DR PhosphoSitePlus; P59279; -.
DR SwissPalm; P59279; -.
DR EPD; P59279; -.
DR jPOST; P59279; -.
DR PaxDb; P59279; -.
DR PeptideAtlas; P59279; -.
DR PRIDE; P59279; -.
DR ProteomicsDB; 300375; -.
DR Antibodypedia; 22150; 212 antibodies from 31 providers.
DR DNASU; 76338; -.
DR Ensembl; ENSMUST00000022765; ENSMUSP00000022765; ENSMUSG00000022159.
DR Ensembl; ENSMUST00000167116; ENSMUSP00000131145; ENSMUSG00000022159.
DR GeneID; 76338; -.
DR KEGG; mmu:76338; -.
DR UCSC; uc007tox.2; mouse.
DR CTD; 84932; -.
DR MGI; MGI:1923588; Rab2b.
DR VEuPathDB; HostDB:ENSMUSG00000022159; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000153886; -.
DR InParanoid; P59279; -.
DR OMA; VEEAFMI; -.
DR OrthoDB; 1271975at2759; -.
DR PhylomeDB; P59279; -.
DR TreeFam; TF300032; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 76338; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Rab2b; mouse.
DR PRO; PR:P59279; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P59279; protein.
DR Bgee; ENSMUSG00000022159; Expressed in bone fossa and 239 other tissues.
DR ExpressionAtlas; P59279; baseline and differential.
DR Genevisible; P59279; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..216
FT /note="Ras-related protein Rab-2B"
FT /id="PRO_0000121072"
FT REGION 189..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 189..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT BINDING 149..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 20
FT /note="S->N: Constitutively inactive. Loss of Golgi
FT apparatus location. Loss of interaction with GARIN1B."
FT /evidence="ECO:0000269|PubMed:28930687,
FT ECO:0000269|PubMed:34714330"
FT MUTAGEN 65
FT /note="Q->L: Constitutively active. Interacts with
FT GARIN1B."
FT /evidence="ECO:0000269|PubMed:28930687,
FT ECO:0000269|PubMed:34714330"
SQ SEQUENCE 216 AA; 24198 MW; 54EE7E2337BFD751 CRC64;
MTYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMVNI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLTSW LEDARQHSSS NMVIMLIGNK
SDLESRRDVK REEGEAFARE HGLIFMETSA KTACNVEEAY INTAKEIYRK IQQGLFDVHN
EANGIKIGPQ QSITSSVGPC SPQQNVSDIG PDSGCC
