RAB3A_HUMAN
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 03-AUG-2022, entry version 224.
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}.
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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; 57.
DR CORUM; P20336; -.
DR IntAct; P20336; 32.
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; P20336; -.
DR PeptideAtlas; P20336; -.
DR PRIDE; P20336; -.
DR ProteomicsDB; 53748; -.
DR Antibodypedia; 1005; 392 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 CTD; 5864; -.
DR DisGeNET; 5864; -.
DR GeneCards; RAB3A; -.
DR HGNC; HGNC:9777; RAB3A.
DR HPA; ENSG00000105649; Group enriched (brain, retina).
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; KECTDNI; -.
DR OrthoDB; 1426655at2759; -.
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; 14 hits in 1081 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 159 other tissues.
DR ExpressionAtlas; P20336; baseline and differential.
DR Genevisible; P20336; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0051021; F:GDP-dissociation inhibitor binding; IEA:Ensembl.
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:0008022; F:protein C-terminus binding; 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: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:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
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:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IEA:Ensembl.
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; -; 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; 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
