ID RAB3A_HUMAN Reviewed; 220 AA. AC P20336; A8K0J4; Q9NYE1; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 27-MAR-2024, entry version 233. DE RecName: Full=Ras-related protein Rab-3A; GN Name=RAB3A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2501306; DOI=10.1016/s0021-9258(18)63872-4; RA Zahraoui A., Touchot N., Chardin P., Tavitian A.; RT "The human Rab genes encode a family of GTP-binding proteins related to RT yeast YPT1 and SEC4 products involved in secretion."; RL J. Biol. Chem. 264:12394-12401(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10574328; DOI=10.1016/s0898-6568(99)00037-6; RA Sullivan M., Olsen A.S., Houslay M.D.; RT "Genomic organisation of the human cyclic AMP-specific phosphodiesterase RT PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and RT JUND."; RL Cell. Signal. 11:735-742(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RA Liu Y., Li J., He J.J.; RT "Functional cloning and characterization of human fetal brain cDNAs."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [9] RP ISOPRENYLATION AT CYS-218 AND CYS-220, AND METHYLATION AT CYS-220. RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264; RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., RA Balch W.E., Buss J.E., Der C.J.; RT "Isoprenoid modification of rab proteins terminating in CC or CXC motifs."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991). RN [10] RP ISOPRENYLATION AT CYS-218 AND CYS-220, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=7991565; DOI=10.1073/pnas.91.25.11963; RA Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.; RT "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of RT adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."; RL Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994). RN [11] RP INTERACTION WITH RPH3A AND SNCA. RX PubMed=15207266; DOI=10.1016/j.nbd.2004.01.001; RA Dalfo E., Barrachina M., Rosa J.L., Ambrosio S., Ferrer I.; RT "Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse RT Lewy body disease."; RL Neurobiol. Dis. 16:92-97(2004). RN [12] RP FUNCTION. RX PubMed=22248876; DOI=10.1016/j.yexcr.2012.01.002; RA Bello O.D., Zanetti M.N., Mayorga L.S., Michaut M.A.; RT "RIM, Munc13, and Rab3A interplay in acrosomal exocytosis."; RL Exp. Cell Res. 318:478-488(2012). RN [13] RP PHOSPHORYLATION AT THR-86. RX PubMed=26824392; DOI=10.7554/elife.12813; RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S., RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J., RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.; RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates RT a subset of Rab GTPases."; RL Elife 5:0-0(2016). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYH9. RX PubMed=27325790; DOI=10.1083/jcb.201511093; RA Encarnacao M., Espada L., Escrevente C., Mateus D., Ramalho J., RA Michelet X., Santarino I., Hsu V.W., Brenner M.B., Barral D.C., RA Vieira O.V.; RT "A Rab3a-dependent complex essential for lysosome positioning and plasma RT membrane repair."; RL J. Cell Biol. 213:631-640(2016). RN [15] RP INTERACTION WITH GDI1; GDI2; CHML AND CHM, PHOSPHORYLATION AT THR-86, AND RP MUTAGENESIS OF 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 [16] RP FUNCTION. RX PubMed=30599141; DOI=10.1016/j.bbamcr.2018.12.005; RA Quevedo M.F., Bustos M.A., Masone D., Roggero C.M., Bustos D.M., RA Tomes C.N.; RT "Grab recruitment by Rab27A-Rabphilin3a triggers Rab3A activation in human RT sperm exocytosis."; RL Biochim. Biophys. Acta 1866:612-622(2018). 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 (By CC similarity). Upon stimulation, switches to its active GTP-bound form, CC 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 or RPH3AL effectors in CC pancreatic beta cells (By similarity). Regulates calcium-dependent CC lysosome exocytosis and plasma membrane repair (PMR) via the CC interaction with 2 effectors, SYTL4 and myosin-9/MYH9 CC (PubMed:27325790). Acts as a positive regulator of acrosome content CC secretion in sperm cells by interacting with RIMS1 (PubMed:22248876, CC PubMed:30599141). Also plays a role in the regulation of dopamine CC release by interacting with synaptotagmin I/SYT (By similarity). CC Interacts with MADD (via uDENN domain); the GTP-bound form is preferred CC for interaction (By similarity). {ECO:0000250|UniProtKB:P63011, CC ECO:0000250|UniProtKB:P63012, ECO:0000269|PubMed:22248876, CC ECO:0000269|PubMed:27325790, ECO:0000269|PubMed:30599141}. CC -!- SUBUNIT: Interacts with RIMS1 and RIMS2 (By similarity). Interacts with CC Rabphilin-3A/RPH3A and Rab effector Noc2/RPH3AL (By similarity). CC Interacts with SYTL4 (By similarity). Interacts with RAB3IP (By CC similarity). Interacts with SGSM1 and SGSM3 (By similarity). Interacts CC with SYT1 (By similarity). Interacts with MYH9; this interaction is CC essential for lysosome exocytosis and plasma membrane repair CC (PubMed:27325790). Interacts with STXBP1; this interaction promotes CC RAB3A dissociation from the vesicle membrane (By similarity). Interacts CC with SNCA (PubMed:15207266). Interacts with GDI1, GDI2, CHM and CHML; CC phosphorylation at Thr-86 disrupts these interactions CC (PubMed:29125462). {ECO:0000250|UniProtKB:P63011, CC ECO:0000250|UniProtKB:P63012, ECO:0000269|PubMed:15207266, CC ECO:0000269|PubMed:27325790, ECO:0000269|PubMed:29125462}. CC -!- INTERACTION: CC P20336; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1045943, EBI-10171774; CC P20336; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-1045943, EBI-743796; CC P20336; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-1045943, EBI-747844; CC P20336; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-1045943, EBI-11984839; CC P20336; P47224: RABIF; NbExp=9; IntAct=EBI-1045943, EBI-713992; CC P20336; Q9H8Y1: VRTN; NbExp=5; IntAct=EBI-1045943, EBI-12894399; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P63012}. Lysosome {ECO:0000269|PubMed:27325790}. CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P63012}. CC Cell projection, axon {ECO:0000250|UniProtKB:P63011}. Cell membrane CC {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side CC {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P63011}. Postsynapse CC {ECO:0000250|UniProtKB:P63011}. Note=Cycles between a vesicle- CC associated GTP-bound form and a cytosolic GDP-bound form. CC {ECO:0000250|UniProtKB:P63012}. CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. 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:0000269|PubMed:29125462}. 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; M28210; AAA60242.1; -; mRNA. DR EMBL; AF157809; AAD46811.1; -; Genomic_DNA. DR EMBL; AF157806; AAD46811.1; JOINED; Genomic_DNA. DR EMBL; AF157807; AAD46811.1; JOINED; Genomic_DNA. DR EMBL; AF157808; AAD46811.1; JOINED; Genomic_DNA. DR EMBL; AF254795; AAF67748.1; -; mRNA. DR EMBL; AF498931; AAM21079.1; -; mRNA. DR EMBL; AK289559; BAF82248.1; -; mRNA. DR EMBL; AC068499; AAF67385.1; -; Genomic_DNA. DR EMBL; CH471106; EAW84672.1; -; Genomic_DNA. DR EMBL; BC011782; AAH11782.1; -; mRNA. DR CCDS; CCDS12372.1; -. DR PIR; C34323; C34323. DR RefSeq; NP_002857.1; NM_002866.4. DR RefSeq; XP_011526466.1; XM_011528164.1. DR AlphaFoldDB; P20336; -. DR SMR; P20336; -. DR BioGRID; 111802; 69. DR CORUM; P20336; -. DR IntAct; P20336; 33. DR MINT; P20336; -. DR STRING; 9606.ENSP00000222256; -. DR GlyGen; P20336; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P20336; -. DR PhosphoSitePlus; P20336; -. DR SwissPalm; P20336; -. DR BioMuta; RAB3A; -. DR DMDM; 131801; -. DR EPD; P20336; -. DR jPOST; P20336; -. DR MassIVE; P20336; -. DR MaxQB; P20336; -. DR PaxDb; 9606-ENSP00000222256; -. DR PeptideAtlas; P20336; -. DR ProteomicsDB; 53748; -. DR Pumba; P20336; -. DR Antibodypedia; 1005; 471 antibodies from 39 providers. DR DNASU; 5864; -. DR Ensembl; ENST00000222256.9; ENSP00000222256.3; ENSG00000105649.10. DR GeneID; 5864; -. DR KEGG; hsa:5864; -. DR MANE-Select; ENST00000222256.9; ENSP00000222256.3; NM_002866.5; NP_002857.1. DR UCSC; uc002nie.3; human. DR AGR; HGNC:9777; -. DR CTD; 5864; -. DR DisGeNET; 5864; -. DR GeneCards; RAB3A; -. DR HGNC; HGNC:9777; RAB3A. DR HPA; ENSG00000105649; Tissue enriched (brain). DR MIM; 179490; gene. DR neXtProt; NX_P20336; -. DR OpenTargets; ENSG00000105649; -. DR PharmGKB; PA34132; -. DR VEuPathDB; HostDB:ENSG00000105649; -. DR eggNOG; KOG0093; Eukaryota. DR GeneTree; ENSGT00940000158959; -. DR HOGENOM; CLU_041217_10_1_1; -. DR InParanoid; P20336; -. DR OMA; AQQQCNC; -. DR OrthoDB; 8685at2759; -. DR PhylomeDB; P20336; -. DR TreeFam; TF313199; -. DR PathwayCommons; P20336; -. DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle. DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR SignaLink; P20336; -. DR SIGNOR; P20336; -. DR BioGRID-ORCS; 5864; 16 hits in 1157 CRISPR screens. DR ChiTaRS; RAB3A; human. DR GeneWiki; RAB3A; -. DR GenomeRNAi; 5864; -. DR Pharos; P20336; Tbio. DR PRO; PR:P20336; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P20336; Protein. DR Bgee; ENSG00000105649; Expressed in right frontal lobe and 161 other cell types or tissues. DR ExpressionAtlas; P20336; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL. DR GO; GO:0060201; C:clathrin-sculpted acetylcholine transport vesicle membrane; TAS:Reactome. DR GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome. DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome. DR GO; GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB. DR GO; GO:0098793; C:presynapse; ISS:UniProtKB. DR GO; GO:0048786; C:presynaptic active zone; ISS:UniProtKB. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl. DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IDA:UniProtKB. DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central. DR GO; GO:0045054; P:constitutive secretory pathway; TAS:ParkinsonsUK-UCL. DR GO; GO:0061670; P:evoked neurotransmitter secretion; IEA:Ensembl. DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB. DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB. DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IBA:GO_Central. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl. DR GO; GO:0001778; P:plasma membrane repair; IDA:UniProtKB. DR GO; GO:0045921; P:positive regulation of exocytosis; TAS:ParkinsonsUK-UCL. DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; IMP:UniProtKB. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. 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; IMP:UniProtKB. DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central. DR GO; GO:1905684; P:regulation of plasma membrane repair; IMP:UniProtKB. DR GO; GO:0099161; P:regulation of presynaptic dense core granule exocytosis; IEA:Ensembl. DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL. DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0050975; P:sensory perception of touch; IEA:Ensembl. DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl. DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL. DR GO; GO:0016188; P:synaptic vesicle maturation; IEA:Ensembl. DR GO; GO:0036465; P:synaptic vesicle recycling; ISS:ParkinsonsUK-UCL. DR GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl. 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; P20336; HS. PE 1: Evidence at protein level; KW Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle; Exocytosis; KW GTP-binding; Lipoprotein; Lysosome; Membrane; Methylation; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Reference proteome; Synapse; Transport. FT CHAIN 1..220 FT /note="Ras-related protein Rab-3A" FT /id="PRO_0000121076" 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:26824392, FT ECO:0000269|PubMed:29125462" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63011" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63011" FT MOD_RES 220 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000269|PubMed:1648736" FT LIPID 218 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736, FT ECO:0000269|PubMed:7991565" FT LIPID 220 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736, FT ECO:0000269|PubMed:7991565" FT MUTAGEN 86 FT /note="T->A: Loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:29125462" FT MUTAGEN 86 FT /note="T->E: Phosphomimetic mutant. Loss of GDI1, GDI2, CHM FT and CHML binding." FT /evidence="ECO:0000269|PubMed:29125462" FT CONFLICT 70 FT /note="R -> K (in Ref. 2; AAF67748)" FT /evidence="ECO:0000305" FT CONFLICT 180 FT /note="V -> E (in Ref. 2; AAF67748)" FT /evidence="ECO:0000305" SQ SEQUENCE 220 AA; 24984 MW; 08B59F8C9BD2EB40 CRC64; MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV DVICEKMSES LDTADPAVTG AKQGPQLSDQ QVPPHQDCAC //