RAB3A_MOUSE
ID RAB3A_MOUSE Reviewed; 220 AA.
AC P63011; P05713; Q3TSL4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ras-related protein Rab-3A;
GN Name=Rab3a;
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 [GENOMIC DNA].
RX PubMed=7687127; DOI=10.1042/bj2930157;
RA Baumert M., Fischer von Mollard G., Jahn R., Suedhof T.C.;
RT "Structure of the murine rab3A gene: correlation of genomic organization
RT with antibody epitopes.";
RL Biochem. J. 293:157-163(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Visual cortex;
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].
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF 13-35; 42-60; 73-83; 122-136; 152-167 AND 179-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH RIMS1 AND RIMS2.
RX PubMed=11056535; DOI=10.1038/35041046;
RA Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H.,
RA Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.;
RT "cAMP-GEFII is a direct target of cAMP in regulated exocytosis.";
RL Nat. Cell Biol. 2:805-811(2000).
RN [6]
RP INTERACTION WITH RIMS1.
RX PubMed=11431472; DOI=10.1074/jbc.m103337200;
RA Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially
RT related through N-terminal alpha-helix motifs.";
RL J. Biol. Chem. 276:32480-32488(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11598194; DOI=10.1091/mbc.12.10.3095;
RA Leenders A.G., Lopes da Silva F.H., Ghijsen W.E., Verhage M.;
RT "Rab3a is involved in transport of synaptic vesicles to the active zone in
RT mouse brain nerve terminals.";
RL Mol. Biol. Cell 12:3095-3102(2001).
RN [8]
RP INTERACTION WITH RIMS2.
RX PubMed=12401793; DOI=10.1074/jbc.m210146200;
RA Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M., Sasaki T.,
RA Tajima N., Iwanaga T., Seino S.;
RT "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL J. Biol. Chem. 277:50497-50502(2002).
RN [9]
RP INTERACTION WITH RIMS1; RIMS2; RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [10]
RP INTERACTION WITH SYTL4.
RX PubMed=12590134; DOI=10.1074/jbc.m213090200;
RA Fukuda M.;
RT "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL J. Biol. Chem. 278:15390-15396(2003).
RN [11]
RP FUNCTION.
RX PubMed=15159548; DOI=10.1073/pnas.0306709101;
RA Matsumoto M., Miki T., Shibasaki T., Kawaguchi M., Shinozaki H., Nio J.,
RA Saraya A., Koseki H., Miyazaki M., Iwanaga T., Seino S.;
RT "Noc2 is essential in normal regulation of exocytosis in endocrine and
RT exocrine cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8313-8318(2004).
RN [12]
RP INTERACTION WITH SGSM1 AND SGSM3.
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [13]
RP INTERACTION WITH MADD, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-36 AND
RP GLN-81.
RX PubMed=18849981; DOI=10.1038/ncb1785;
RA Niwa S., Tanaka Y., Hirokawa N.;
RT "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL Nat. Cell Biol. 10:1269-1279(2008).
RN [14]
RP FUNCTION, AND INTERACTION WITH RIMS2.
RX PubMed=20674857; DOI=10.1016/j.cmet.2010.05.017;
RA Yasuda T., Shibasaki T., Minami K., Takahashi H., Mizoguchi A., Uriu Y.,
RA Numata T., Mori Y., Miyazaki J., Miki T., Seino S.;
RT "Rim2alpha determines docking and priming states in insulin granule
RT exocytosis.";
RL Cell Metab. 12:117-129(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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 [16]
RP PHOSPHORYLATION AT THR-86.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31651360; DOI=10.1186/s40478-019-0812-5;
RA Xiao S., McKeever P.M., Lau A., Robertson J.;
RT "Synaptic localization of C9orf72 regulates post-synaptic glutamate
RT receptor 1 levels.";
RL Acta Neuropathol. Commun. 7:161-161(2019).
CC -!- FUNCTION: Small GTP-binding protein that plays a central role in
CC regulated exocytosis and secretion. Controls the recruitment, tethering
CC and docking of secretory vesicles to the plasma membrane
CC (PubMed:11598194). Upon stimulation, switches to its active GTP-bound
CC form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2,
CC Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules
CC onto the plasma membrane (By similarity). Upon GTP hydrolysis by
CC GTPase-activating protein, dissociates from the vesicle membrane
CC allowing the exocytosis to proceed (By similarity). Stimulates insulin
CC secretion through interaction with RIMS2 isoform RIMS2 and RPH3AL
CC effectors in pancreatic beta cells (PubMed:15159548, PubMed:20674857).
CC Regulates calcium-dependent lysosome exocytosis and plasma membrane
CC repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-
CC 9/MYH9 (By similarity). Acts as a positive regulator of acrosome
CC content secretion in sperm cells by interacting with RIMS1 (By
CC similarity). Plays a role in the regulation of dopamine release by
CC interacting with synaptotagmin I/SYT (By similarity).
CC {ECO:0000250|UniProtKB:P20336, ECO:0000250|UniProtKB:P63012,
CC ECO:0000269|PubMed:11598194, ECO:0000269|PubMed:15159548,
CC ECO:0000269|PubMed:20674857}.
CC -!- SUBUNIT: Interacts with RIMS1 and RIMS2 (PubMed:11056535,
CC PubMed:11431472, PubMed:12401793, PubMed:12578829). Interacts with
CC Rabphilin-3A/RPH3A and Rab effector Noc2/RPH3AL (PubMed:12578829).
CC Interacts with SYTL4 (PubMed:12590134). Interacts with RAB3IP.
CC Interacts with SGSM1 and SGSM3 (PubMed:17509819). Interacts with SYT1
CC (By similarity). Interacts with MYH9; this interaction is essential for
CC lysosome exocytosis and plasma membrane repair (By similarity).
CC Interacts with STXBP1; this interaction promotes RAB3A dissociation
CC from the vesicle membrane (By similarity). Interacts with SNCA (By
CC similarity). Interacts with GDI1, GDI2, CHM and CHML; phosphorylation
CC at Thr-86 disrupts these interactions (By similarity). Interacts with
CC MADD (via uDENN domain); the GTP-bound form is preferred for
CC interaction (PubMed:18849981). {ECO:0000250|UniProtKB:P20336,
CC ECO:0000250|UniProtKB:P63012, ECO:0000269|PubMed:11056535,
CC ECO:0000269|PubMed:11431472, ECO:0000269|PubMed:12401793,
CC ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:12590134,
CC ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:18849981}.
CC -!- INTERACTION:
CC P63011; P47708: Rph3a; NbExp=2; IntAct=EBI-398393, EBI-398376;
CC P63011; Q8TDW5: SYTL5; Xeno; NbExp=2; IntAct=EBI-398393, EBI-2939487;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P63012}. Lysosome
CC {ECO:0000250|UniProtKB:P20336}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:P63012}. Cell projection, axon
CC {ECO:0000269|PubMed:18849981}. Cell membrane {ECO:0000305}; Lipid-
CC anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse
CC {ECO:0000269|PubMed:31651360}. Postsynapse
CC {ECO:0000269|PubMed:31651360}. Note=Cycles between a vesicle-associated
CC GTP-bound form and a cytosolic GDP-bound form.
CC {ECO:0000250|UniProtKB:P63012}.
CC -!- TISSUE SPECIFICITY: Expressed in the forebrain and hippocampus (at
CC protein level) (PubMed:31651360). Found in active zone in brain nerve
CC terminals (PubMed:11598194). {ECO:0000269|PubMed:11598194,
CC ECO:0000269|PubMed:31651360}.
CC -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:P20336}.
CC -!- DISRUPTION PHENOTYPE: RAB3-deficient mice show an incomplete and slow
CC secretion response in brain nerve terminals after exhaustive
CC stimulation. The replenishment of docked vesicles after exhaustive
CC stimulation is also impaired. {ECO:0000269|PubMed:11598194}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X72966; CAA51470.1; -; Genomic_DNA.
DR EMBL; AK005362; BAB23976.1; -; mRNA.
DR EMBL; AK158727; BAE34630.1; -; mRNA.
DR EMBL; AK161975; BAE36661.1; -; mRNA.
DR EMBL; BC053519; AAH53519.1; -; mRNA.
DR CCDS; CCDS22379.1; -.
DR PIR; S34070; S34070.
DR RefSeq; NP_001159871.1; NM_001166399.2.
DR RefSeq; NP_001314976.1; NM_001328047.1.
DR RefSeq; NP_033027.1; NM_009001.6.
DR RefSeq; XP_006509666.1; XM_006509603.3.
DR AlphaFoldDB; P63011; -.
DR SMR; P63011; -.
DR BioGRID; 202544; 24.
DR CORUM; P63011; -.
DR DIP; DIP-31051N; -.
DR IntAct; P63011; 51.
DR MINT; P63011; -.
DR STRING; 10090.ENSMUSP00000105719; -.
DR iPTMnet; P63011; -.
DR PhosphoSitePlus; P63011; -.
DR SwissPalm; P63011; -.
DR EPD; P63011; -.
DR jPOST; P63011; -.
DR PaxDb; P63011; -.
DR PeptideAtlas; P63011; -.
DR PRIDE; P63011; -.
DR ProteomicsDB; 300290; -.
DR Antibodypedia; 1005; 392 antibodies from 39 providers.
DR DNASU; 19339; -.
DR Ensembl; ENSMUST00000034301; ENSMUSP00000034301; ENSMUSG00000031840.
DR Ensembl; ENSMUST00000110090; ENSMUSP00000105717; ENSMUSG00000031840.
DR Ensembl; ENSMUST00000110092; ENSMUSP00000105719; ENSMUSG00000031840.
DR Ensembl; ENSMUST00000110093; ENSMUSP00000105720; ENSMUSG00000031840.
DR GeneID; 19339; -.
DR KEGG; mmu:19339; -.
DR UCSC; uc009mbi.2; mouse.
DR CTD; 5864; -.
DR MGI; MGI:97843; Rab3a.
DR VEuPathDB; HostDB:ENSMUSG00000031840; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000158959; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P63011; -.
DR OMA; MERYCED; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P63011; -.
DR TreeFam; TF313199; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 19339; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rab3a; mouse.
DR PRO; PR:P63011; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P63011; protein.
DR Bgee; ENSMUSG00000031840; Expressed in primary visual cortex and 150 other tissues.
DR ExpressionAtlas; P63011; baseline and differential.
DR Genevisible; P63011; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0051021; F:GDP-dissociation inhibitor binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0061670; P:evoked neurotransmitter secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0045055; P:regulated exocytosis; ISO:MGI.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:1905684; P:regulation of plasma membrane repair; ISO:MGI.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISO:MGI.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
DR GO; GO:0050975; P:sensory perception of touch; IMP:MGI.
DR GO; GO:0097091; P:synaptic vesicle clustering; IMP:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR GO; GO:0036465; P:synaptic vesicle recycling; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048489; P:synaptic vesicle transport; IDA:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR CDD; cd01865; Rab3; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037872; Rab3.
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; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Exocytosis; GTP-binding; Lipoprotein; Lysosome;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..220
FT /note="Ras-related protein Rab-3A"
FT /id="PRO_0000121078"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..59
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 29..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 48..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 165..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 86
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 36
FT /note="T->N: Reduced axon localization and aggregation in
FT neuronal cell bodies."
FT /evidence="ECO:0000269|PubMed:18849981"
FT MUTAGEN 81
FT /note="Q->L: No effect on neurite transport. Reduced axonal
FT transport in a Madd RNAi-mediated knockdown or a Kif1b
FT knockout background."
FT /evidence="ECO:0000269|PubMed:18849981"
SQ SEQUENCE 220 AA; 24970 MW; 1A3E9F8C9D09EB40 CRC64;
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI
KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV
DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC
