RAB2A_MOUSE
ID RAB2A_MOUSE Reviewed; 212 AA.
AC P53994; Q3UK45;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Rab-2A;
DE EC=3.6.5.2 {ECO:0000305|PubMed:34714330};
GN Name=Rab2a; Synonyms=Rab2;
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=NIH Swiss;
RA Laufer W.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Bone marrow, Diencephalon, Egg, and Muellerian duct;
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 PROTEIN SEQUENCE OF 31-46, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [5]
RP FUNCTION, INTERACTION WITH GARIN1B, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP SER-20 AND GLN-65, AND CATALYTIC ACTIVITY.
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. In their active state, drive transport of vesicular
CC carriers from donor organelles to acceptor organelles to regulate the
CC membrane traffic that maintains organelle identity and morphology.
CC Required for protein transport from the endoplasmic reticulum to the
CC Golgi complex. Regulates the compacted morphology of the Golgi.
CC {ECO:0000305|PubMed:34714330}.
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:34714330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:34714330};
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:0000250|UniProtKB:P61019}.
CC -!- SUBUNIT: Interacts with PRKCI. Interacts with TRIP11. Interacts (in
CC GTP-bound form) with GARIN1B (PubMed:34714330).
CC {ECO:0000250|UniProtKB:P61019, ECO:0000269|PubMed:34714330}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Lipid-anchor. Melanosome {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Golgi apparatus membrane {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}.
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; X95403; CAA64684.1; -; mRNA.
DR EMBL; AK079071; BAC37524.1; -; mRNA.
DR EMBL; AK135421; BAE22525.1; -; mRNA.
DR EMBL; AK146179; BAE26957.1; -; mRNA.
DR EMBL; AK150030; BAE29254.1; -; mRNA.
DR EMBL; AK159607; BAE35226.1; -; mRNA.
DR EMBL; AK160333; BAE35742.1; -; mRNA.
DR EMBL; AK163320; BAE37298.1; -; mRNA.
DR CCDS; CCDS17955.1; -.
DR RefSeq; NP_067493.1; NM_021518.3.
DR AlphaFoldDB; P53994; -.
DR SMR; P53994; -.
DR BioGRID; 208489; 11.
DR IntAct; P53994; 8.
DR MINT; P53994; -.
DR STRING; 10090.ENSMUSP00000057664; -.
DR iPTMnet; P53994; -.
DR PhosphoSitePlus; P53994; -.
DR SwissPalm; P53994; -.
DR EPD; P53994; -.
DR jPOST; P53994; -.
DR PaxDb; P53994; -.
DR PeptideAtlas; P53994; -.
DR PRIDE; P53994; -.
DR ProteomicsDB; 300224; -.
DR TopDownProteomics; P53994; -.
DR Antibodypedia; 4367; 339 antibodies from 37 providers.
DR DNASU; 59021; -.
DR Ensembl; ENSMUST00000060232; ENSMUSP00000057664; ENSMUSG00000047187.
DR GeneID; 59021; -.
DR KEGG; mmu:59021; -.
DR UCSC; uc008rxw.1; mouse.
DR CTD; 5862; -.
DR MGI; MGI:1928750; Rab2a.
DR VEuPathDB; HostDB:ENSMUSG00000047187; -.
DR eggNOG; KOG0098; Eukaryota.
DR GeneTree; ENSGT00940000153886; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P53994; -.
DR OMA; ANGVMQY; -.
DR OrthoDB; 1271975at2759; -.
DR PhylomeDB; P53994; -.
DR TreeFam; TF300032; -.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 59021; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Rab2a; mouse.
DR PRO; PR:P53994; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P53994; protein.
DR Bgee; ENSMUSG00000047187; Expressed in subparaventricular zone and 247 other tissues.
DR ExpressionAtlas; P53994; baseline and differential.
DR Genevisible; P53994; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
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 Acetylation; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT CHAIN 2..212
FT /note="Ras-related protein Rab-2A"
FT /id="PRO_0000121067"
FT REGION 2..19
FT /note="Required for interaction with PRKCI"
FT /evidence="ECO:0000250"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 193..212
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61019"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 20
FT /note="S->N: Constitutively inactive. Loss of interaction
FT with GARIN1B."
FT /evidence="ECO:0000269|PubMed:34714330"
FT MUTAGEN 65
FT /note="Q->L: Constitutively active. Interacts with
FT GARIN1B."
FT /evidence="ECO:0000269|PubMed:34714330"
SQ SEQUENCE 212 AA; 23548 MW; 58231E3F9EF007A5 CRC64;
MAYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DGKQIKLQIW
DTAGQESFRS ITRSYYRGAA GALLVYDITR RDTFNHLTTW LEDARQHSNS NMVIMLIGNK
SDLESRREVK KEEGEAFARE HGLIFMETSA KTASNVEEAF INTAKEIYEK IQEGVFDINN
EANGIKIGPQ HAATNASHGS NQGGQQAGGG CC
