RB3GP_DROME
ID RB3GP_DROME Reviewed; 916 AA.
AC Q9VQ26;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Rab3 GTPase-activating protein catalytic subunit;
GN ORFNames=CG31935;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-544, AND
RP IDENTIFICATION BY 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 catalytic 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. Specifically
CC converts active Rab3-GTP to the inactive form Rab3-GDP (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer composed
CC of CG31935 and rab3-GAP/CG7061. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF51356.2; -; Genomic_DNA.
DR RefSeq; NP_608608.2; NM_134764.3.
DR AlphaFoldDB; Q9VQ26; -.
DR SMR; Q9VQ26; -.
DR BioGRID; 59582; 2.
DR IntAct; Q9VQ26; 1.
DR STRING; 7227.FBpp0077582; -.
DR iPTMnet; Q9VQ26; -.
DR PaxDb; Q9VQ26; -.
DR PRIDE; Q9VQ26; -.
DR EnsemblMetazoa; FBtr0077916; FBpp0077582; FBgn0051935.
DR GeneID; 33338; -.
DR KEGG; dme:Dmel_CG31935; -.
DR UCSC; CG31935-RA; d. melanogaster.
DR FlyBase; FBgn0051935; CG31935.
DR VEuPathDB; VectorBase:FBgn0051935; -.
DR eggNOG; KOG2390; Eukaryota.
DR GeneTree; ENSGT00390000006705; -.
DR HOGENOM; CLU_012561_1_0_1; -.
DR InParanoid; Q9VQ26; -.
DR OMA; IMTEDMH; -.
DR OrthoDB; 536022at2759; -.
DR PhylomeDB; Q9VQ26; -.
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; 33338; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33338; -.
DR PRO; PR:Q9VQ26; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051935; Expressed in saliva-secreting gland and 26 other tissues.
DR ExpressionAtlas; Q9VQ26; baseline and differential.
DR Genevisible; Q9VQ26; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0034389; P:lipid droplet organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016236; P:macroautophagy; IMP:FlyBase.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061646; P:positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:ParkinsonsUK-UCL.
DR InterPro; IPR045700; Rab3GAP1.
DR InterPro; IPR026147; Rab3GAP1_conserved.
DR PANTHER; PTHR21422; PTHR21422; 1.
DR Pfam; PF13890; Rab3-GTPase_cat; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..916
FT /note="Rab3 GTPase-activating protein catalytic subunit"
FT /id="PRO_0000191661"
FT REGION 530..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 916 AA; 104431 MW; 7625F4D48BA54F1A CRC64;
MAEEIDDNEF YRENFSADSD WEVFNAQLGE ILQKWDVSSD SETRNLKSEE IFSCNWKVER
EKLDMLRNGI EVEYHQAILE DEELVRAEAK EITCLQRTSC HHDLMSTGNS FGPPIRSSQE
LHILARIYGL RRFIVLHPVN PTLNYMRSTS EFNFFLSAVA VVSAEVQSLV PIFVQIYDPK
WNYYTGVALA PALRTNFRLI GLEKAPPECR FLMGLLTLFR EKVPTSYTQA AMISVCTTYA
LDTMRIRMPM YVPFDHGLSS EDIVVDGEVS HLEVQQFCAL PHGYKPESRT EIYLVYTWPE
LSEHVAFDSE QRSDFVPAKA PLGKIYLSVE ASSYLSCCLR DYQSVAEVTR SLESFVGRNF
SGTSSGAEAA SNPLDRITEH KLTKRRERSF ELPSQAGLTK RLPGPMTESE LSELLAYLFP
DMHPEMALFP YAKKNFTDKF DPMRIKSAVP DSLVCRLSCL LATCHAHLGS VEGMAQVWAA
FTRQLRLLWD NSLMVPGISA GFPDTRTCLL HQKLQMLNVC VERRVQREAN SKRKSEGMVG
KASSEEEEDE DDDEGEFFDC DDLTAGAGSP TKAVLSLKPE GRLRRLNNER LLEEPDEYLY
IPDTQEPVPK TEDQLQDDAE VMLKLGPGSG LTTQMMCTSL LSDMEAFKAA NPRGIMEDFI
RWYSPKDWEE VTDELGQVKH QLSIRMTTEG NTWQKVWEQA QAVPVSRQKR LFDDTNEALK
VLHYLETRKM HEIYNLTVIP LLHSAILKLA DILSNAELED LFSSQIEKLL SDLCRLSRSH
SDELPSIKPL LDDLAELERR FYQFKCFERL SGYPKRSSLQ QVKLQFEEIL RNDNCCTIVN
RRLTAAGDGT LYDILIPKLE EDMADRLISK DYIIRLDGDT KTTEKGLYLG PQFMRAIVTG
EKLRLCGAFT ESTAFV
