ID RABEP_DROME Reviewed; 511 AA.
AC Q9V8W3; O97142;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 148.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A;
DE AltName: Full=Rab escort protein homolog;
DE Short=REP;
GN Name=Rep {ECO:0000312|FlyBase:FBgn0026378}; ORFNames=CG8432;
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] {ECO:0000305, ECO:0000312|EMBL:AAD16891.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10082978; DOI=10.1016/s0167-4889(99)00004-x;
RA Dong H., Jin Y., Johansen J., Johansen K.M.;
RT "Antibody identification, chromosome map assignment, and sequence analysis
RT of a Rab escort protein homolog in Drosophila.";
RL Biochim. Biophys. Acta 1449:194-198(1999).
RN [2] {ECO:0000312|EMBL:AAF57544.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF57544.1}
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 [4] {ECO:0000312|EMBL:AAL28600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28600.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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: Binds unprenylated Rab proteins, presents it to the catalytic
CC component B, and remains bound to it after the geranylgeranyl transfer
CC reaction. The component A is thought to be regenerated by transferring
CC its prenylated Rab to a protein acceptor (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9V8W3; Q9VN77: RabGGTa; NbExp=2; IntAct=EBI-186105, EBI-139441;
CC Q9V8W3; Q9W501: temp; NbExp=6; IntAct=EBI-186105, EBI-119928;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10082978}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:10082978}. Note=Coordinated with the cell cycle,
CC located around nuclei during prophase and telophase. Located to spindle
CC poles during metaphase.
CC -!- DEVELOPMENTAL STAGE: Expressed in the syncytial embryo.
CC {ECO:0000269|PubMed:10082978}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000255}.
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DR EMBL; AF105063; AAD16891.1; -; mRNA.
DR EMBL; AE013599; AAF57544.1; -; Genomic_DNA.
DR EMBL; AY061052; AAL28600.1; -; mRNA.
DR RefSeq; NP_477420.1; NM_058072.4.
DR AlphaFoldDB; Q9V8W3; -.
DR SMR; Q9V8W3; -.
DR BioGRID; 62904; 5.
DR IntAct; Q9V8W3; 3.
DR STRING; 7227.FBpp0085658; -.
DR PaxDb; 7227-FBpp0085658; -.
DR EnsemblMetazoa; FBtr0086462; FBpp0085658; FBgn0026378.
DR GeneID; 37246; -.
DR KEGG; dme:Dmel_CG8432; -.
DR AGR; FB:FBgn0026378; -.
DR CTD; 37246; -.
DR FlyBase; FBgn0026378; Rep.
DR VEuPathDB; VectorBase:FBgn0026378; -.
DR eggNOG; KOG4405; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_4_1_1; -.
DR InParanoid; Q9V8W3; -.
DR OMA; LMKFLTA; -.
DR OrthoDB; 197300at2759; -.
DR PhylomeDB; Q9V8W3; -.
DR Reactome; R-DME-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-DME-8873719; RAB geranylgeranylation.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 37246; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37246; -.
DR PRO; PR:Q9V8W3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026378; Expressed in oviduct (Drosophila) and 24 other cell types or tissues.
DR Genevisible; Q9V8W3; DM.
DR GO; GO:0005818; C:aster; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; NAS:FlyBase.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; IMP:FlyBase.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Cytoskeleton; GTPase activation; Reference proteome.
FT CHAIN 1..511
FT /note="Rab proteins geranylgeranyltransferase component A"
FT /id="PRO_0000056691"
FT CONFLICT 356
FT /note="N -> D (in Ref. 1; AAD16891)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> V (in Ref. 1; AAD16891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56827 MW; D613DF8C784490DC CRC64;
MLDDLPEQFD LVVIGTGFTE SCIAAAGSRI GKSVLHLDSN EYYGDVWSSF SMDALCARLD
QEVEPHSALR NARYTWHSME KESETDAQSW NRDSVLAKSR RFSLDLCPRI LYAAGELVQL
LIKSNICRYA EFRAVDHVCM RHNGEIVSVP CSRSDVFNTK TLTIVEKRLL MKFLTACNDY
GEDKCNEDSL EFRGRTFLEY LQAQRVTEKI SSCVMQAIAM CGPSTSFEEG MQRTQRFLGS
LGRYGNTPFL FPMYGCGELP QCFCRLCAVY GGIYCLKRAV DDIALDSNSN EFLLSSAGKT
LRAKNVVSAP GYTPVSKGIE LKPHISRGLF ISSSPLGNEE LNKGGGGVNL LRLLDNEGGR
EAFLIQLSHY TGACPEGLYI FHLTTPALSE DPASDLAIFT SQLFDQSDAQ IIFSSYFTIA
AQSSKSPAAE HIYYTDPPTY ELDYDAAIAN ARDIFGKMFP DADFLPRAPD PEEIVVDGED
PSALNEHTLP EDLRAQLHDM QQATQEMDIQ E
//
