RBGPR_DROME
ID RBGPR_DROME Reviewed; 1341 AA.
AC Q9VKB9; Q7KMI4; Q7KTD8; Q9VKC0; Q9Y0Z3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Rab3 GTPase-activating protein regulatory subunit;
GN Name=Rab3-GAP {ECO:0000312|FlyBase:FBgn0027505};
GN ORFNames=CG7061 {ECO:0000312|FlyBase:FBgn0027505};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1341.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP IDENTIFICATION.
RX PubMed=10798391; DOI=10.1016/s0896-6273(00)81136-8;
RA Lloyd T.E., Verstreken P., Ostrin E.J., Phillippi A., Lichtarge O.,
RA Bellen H.J.;
RT "A genome-wide search for synaptic vesicle cycle proteins in Drosophila.";
RL Neuron 26:45-50(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-801, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Probable regulatory subunit of a GTPase activating protein
CC that has specificity for Rab3 subfamily. Rab3 proteins are involved in
CC regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-
CC activating complex specifically converts active Rab3-GTP to the
CC inactive form Rab3-GDP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed
CC of CG31935 and Rab3-GAP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Rab3-GAP regulatory subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38657.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53156.2; -; Genomic_DNA.
DR EMBL; BT016089; AAV36974.1; -; mRNA.
DR EMBL; AF145682; AAD38657.1; ALT_FRAME; mRNA.
DR RefSeq; NP_609544.2; NM_135700.5.
DR AlphaFoldDB; Q9VKB9; -.
DR SMR; Q9VKB9; -.
DR BioGRID; 60677; 4.
DR IntAct; Q9VKB9; 2.
DR STRING; 7227.FBpp0079885; -.
DR iPTMnet; Q9VKB9; -.
DR PaxDb; Q9VKB9; -.
DR PRIDE; Q9VKB9; -.
DR DNASU; 34626; -.
DR EnsemblMetazoa; FBtr0080301; FBpp0079885; FBgn0027505.
DR GeneID; 34626; -.
DR KEGG; dme:Dmel_CG7061; -.
DR UCSC; CG7061-RA; d. melanogaster.
DR CTD; 34626; -.
DR FlyBase; FBgn0027505; Rab3-GAP.
DR VEuPathDB; VectorBase:FBgn0027505; -.
DR eggNOG; KOG2727; Eukaryota.
DR GeneTree; ENSGT00390000005794; -.
DR InParanoid; Q9VKB9; -.
DR OrthoDB; 790713at2759; -.
DR PhylomeDB; Q9VKB9; -.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 34626; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Rab3-GAP; fly.
DR GenomeRNAi; 34626; -.
DR PRO; PR:Q9VKB9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027505; Expressed in testis and 26 other tissues.
DR Genevisible; Q9VKB9; DM.
DR GO; GO:0044754; C:autolysosome; IDA:FlyBase.
DR GO; GO:0005776; C:autophagosome; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; NAS:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060025; P:regulation of synaptic activity; IMP:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:FlyBase.
DR InterPro; IPR026059; Rab3GAP2.
DR InterPro; IPR029257; RAB3GAP2_C.
DR InterPro; IPR032839; RAB3GAP_N.
DR PANTHER; PTHR12472; PTHR12472; 1.
DR Pfam; PF14656; RAB3GAP2_C; 1.
DR Pfam; PF14655; RAB3GAP2_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1341
FT /note="Rab3 GTPase-activating protein regulatory subunit"
FT /id="PRO_0000191666"
FT REGION 432..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 505
FT /note="T -> I (in Ref. 4; AAD38657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1341 AA; 151008 MW; 0E07C114DEDECAF6 CRC64;
MACEVKHCGE IRDFKKVQEY FGLGHDDNWL NAINHAISPT GELIAMAQGE KLAFLSTCWS
SHGNGNTYVL GWCGELEDPN QIVTSLTCLP MTQNKSTDGA IEWTCVAVGL CSGMVTFYTD
SGVKLFSQCC QEDPVIGVKL QSAPRHSEAD SLLYIIYPRC LCFIQGQDIL PTLNNCRHNV
QRGALERSSY PTADVVPFQK YKFKQEREAV INDAAISTTQ RPPTYDYIVQ QTIGLGYFAK
VHATPPRSSQ VLAAGAEPYL GFFQAEEGYK TMSLGEVAKD VIGIAYKNLL GGIFRRAPEP
LPSPEESPLP VPTKEAPMRI RCRLYDGKRD GLTLSVAPGG RLAVVTDNLD RVMLVDTHQA
IILRVWKGYR DAQCAFVPVK EKSVRGIKTH KRKALFLVIY APRMGCLDIW ALQNGPKVAA
FNVSKSGQLM YNNHSPLGSG GSSGSGNSSS QSRKSLAINH CLFLDPSDGS LKEIHIPFHY
ALSETSSQTS RDIHMLRRLR NQLRTINHGQ AKDEALQEIG ELASELQTLE VRQQCLEMLL
KSKKLQPQVF QSIINAFIKK PLSESTGSEE FVNQIENYKR LTDLYLALSQ ANQREDNEPP
VEYLELSDAD LVTINKLVLL LDDGTEKDKP AATREVSFKL QAEHKTEEFV DYLSIFNIDS
PDGISLLPEK SDKFGAVSID LFSQFFAQGL CFGQFKQWIN QACLPSRDLL KLIIWFWLEK
PFKYNNCDEV VEDMSRIAAM VQTICDLAGE HIHDYAYNAI SPWWQEVREL LLESKQFSGL
LVAIVCKTVA TNLWRNRKEG SCDESSQNED DERWERISHD EAQWGLLTGK LEDVAVLGAI
LSKPLICRDP VGPEMSYEPP DCSLKSIVSS GKGIVTELTA KWLISAQLHP SKVLEISPPE
NELDDESKVK IKDEPTKESV DEDAESEEDL EMAKEVYAAS KEAHEPILER LALLRAHFPF
SLESGVLLSL MSWQYMVQWS KQLSSLDHLK AALLCLNQFR TPDWALKHGI CCMLWNATLK
FPLQAAAKLI QKVGRLPVDK MCQQDLEMSA GKVPEFLELS LEFLQHFTAS MEHDKRELHF
EQSLSEGALP LQFLALQQHH AMPQLLRLQT ELCSVLHFVS FFQLRIPKPL TTLFDSMSNK
ALLADINKEL PYVLPAPDLV LQQQRTEFLC RLVTATMDLI REDLEQLYIL DHVFYMGKIC
ALADSWEVDK LPILRRQVVE LYAFGYDAEA QVLLQDISDD EELGRLLLEI AGRRLNLYAQ
SSQSTFLKIA SVGHQLLAYL DNLKEPMTEN NIQIAATKPD EIDVAALDRL LSHAYKYLCR
RESKQLPIIG QMYNAVRILQ N
