RAB3_DROME
ID RAB3_DROME Reviewed; 220 AA.
AC P25228; Q9V5N9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ras-related protein Rab-3;
GN Name=Rab3; ORFNames=CG7576;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1648935; DOI=10.1016/0896-6273(91)90078-e;
RA Johnston P.A., Archer B.T. III, Robinson K., Mignery G.A., Jahn R.,
RA Suedhof T.C.;
RT "Rab3A attachment to the synaptic vesicle membrane mediated by a conserved
RT polyisoprenylated carboxy-terminal sequence.";
RL Neuron 7:101-109(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE, ISOPRENYLATION AT CYS-218 AND CYS-220, AND INTERACTION
RP WITH RPH.
RX PubMed=14722103; DOI=10.1074/jbc.m306812200;
RA Fukuda M., Kanno E., Yamamoto A.;
RT "Rabphilin and Noc2 are recruited to dense-core vesicles through specific
RT interaction with Rab27A in PC12 cells.";
RL J. Biol. Chem. 279:13065-13075(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Involved in exocytosis by regulating a late step in synaptic
CC vesicle fusion. Could play a role in neurotransmitter release by
CC regulating membrane flow in the nerve terminal (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with Rph. {ECO:0000269|PubMed:14722103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M64621; AAA28843.1; -; mRNA.
DR EMBL; AB112932; BAD07037.1; -; mRNA.
DR EMBL; AE013599; AAF58762.1; -; Genomic_DNA.
DR EMBL; AY060449; AAL25488.1; -; mRNA.
DR PIR; JH0425; JH0425.
DR RefSeq; NP_523687.1; NM_078963.3.
DR PDB; 4RKF; X-ray; 1.50 A; A/B=1-188.
DR PDBsum; 4RKF; -.
DR AlphaFoldDB; P25228; -.
DR SMR; P25228; -.
DR BioGRID; 61936; 10.
DR DIP; DIP-20159N; -.
DR STRING; 7227.FBpp0087352; -.
DR PaxDb; P25228; -.
DR PRIDE; P25228; -.
DR DNASU; 36127; -.
DR EnsemblMetazoa; FBtr0088257; FBpp0087352; FBgn0005586.
DR EnsemblMetazoa; FBtr0473383; FBpp0422979; FBgn0005586.
DR GeneID; 36127; -.
DR KEGG; dme:Dmel_CG7576; -.
DR CTD; 36127; -.
DR FlyBase; FBgn0005586; Rab3.
DR VEuPathDB; VectorBase:FBgn0005586; -.
DR eggNOG; KOG0093; Eukaryota.
DR GeneTree; ENSGT00940000169270; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P25228; -.
DR OMA; WQKDASD; -.
DR OrthoDB; 1218073at2759; -.
DR PhylomeDB; P25228; -.
DR Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8873719; RAB geranylgeranylation.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 36127; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rab3; fly.
DR GenomeRNAi; 36127; -.
DR PRO; PR:P25228; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005586; Expressed in brain and 26 other tissues.
DR ExpressionAtlas; P25228; baseline and differential.
DR Genevisible; P25228; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; HDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; HDA:FlyBase.
DR GO; GO:0031982; C:vesicle; ISS:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR GO; GO:0048789; P:cytoskeletal matrix organization at active zone; IMP:FlyBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
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:0032482; P:Rab protein signal transduction; ISS:FlyBase.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
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:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IPI:FlyBase.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
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 3D-structure; Cytoplasmic vesicle; Exocytosis; GTP-binding; Lipoprotein;
KW Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..220
FT /note="Ras-related protein Rab-3"
FT /id="PRO_0000121092"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..58
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 202..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 47..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63012"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT BINDING 164..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O95716"
FT MOD_RES 220
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:14722103"
FT LIPID 220
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:14722103"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4RKF"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:4RKF"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:4RKF"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:4RKF"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:4RKF"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4RKF"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4RKF"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:4RKF"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:4RKF"
SQ SEQUENCE 220 AA; 24862 MW; B324A77DBEF847A1 CRC64;
MASGGDPKWQ KDAADQNFDY MFKLLIIGNS SVGKTSFLFR YADDSFTSAF VSTVGIDFKV
KTVFRHDKRV KLQIWDTAGQ ERYRTITTAY YRGAMGFILM YDVTNEDSFN SVQDWVTQIK
TYSWDNAQVI LVGNKCDMED QRVISFERGR QLADQLGVEF FETSAKENVN VKAVFERLVD
IICDKMSESL DADPTLVGGG QKGQRLTDQP QGTPNANCNC
