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 27-MAR-2024, entry version 184. 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}. 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; 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; 26. DR CORUM; P63011; -. DR DIP; DIP-31051N; -. DR IntAct; P63011; 51. DR MINT; P63011; -. DR STRING; 10090.ENSMUSP00000105719; -. DR GlyGen; P63011; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P63011; -. DR MetOSite; P63011; -. DR PhosphoSitePlus; P63011; -. DR SwissPalm; P63011; -. DR EPD; P63011; -. DR jPOST; P63011; -. DR PaxDb; 10090-ENSMUSP00000105719; -. DR PeptideAtlas; P63011; -. DR ProteomicsDB; 300290; -. DR Pumba; P63011; -. DR Antibodypedia; 1005; 471 antibodies from 39 providers. DR DNASU; 19339; -. DR Ensembl; ENSMUST00000034301.12; ENSMUSP00000034301.6; ENSMUSG00000031840.15. DR Ensembl; ENSMUST00000110090.8; ENSMUSP00000105717.2; ENSMUSG00000031840.15. DR Ensembl; ENSMUST00000110092.6; ENSMUSP00000105719.5; ENSMUSG00000031840.15. DR Ensembl; ENSMUST00000110093.9; ENSMUSP00000105720.3; ENSMUSG00000031840.15. DR GeneID; 19339; -. DR KEGG; mmu:19339; -. DR UCSC; uc009mbi.2; mouse. DR AGR; MGI:97843; -. 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; QAITCPP; -. DR OrthoDB; 8685at2759; -. 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 78 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 153 other cell types or tissues. DR ExpressionAtlas; P63011; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI. 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; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. 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:0030672; C:synaptic vesicle membrane; IDA:SynGO. 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:0030674; F:protein-macromolecule adaptor activity; IDA: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:0051649; P:establishment of localization in cell; IPI:MGI. DR GO; GO:0061670; P:evoked neurotransmitter secretion; IMP:ParkinsonsUK-UCL. DR GO; GO:0006887; P:exocytosis; ISO:MGI. DR GO; GO:0030073; P:insulin secretion; IPI: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:0099161; P:regulation of presynaptic dense core granule exocytosis; IDA:SynGO. 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; IDA:SynGO. 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; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR037872; Rab3. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47980; LD44762P; 1. DR PANTHER; PTHR47980:SF9; RAS-RELATED PROTEIN RAB-3A; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; P63011; MM. 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 //