RAP1_DROME
ID RAP1_DROME Reviewed; 184 AA.
AC P08645; Q2XYB6; Q540V3; Q9V3N0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ras-related protein Rap1 {ECO:0000312|FlyBase:FBgn0004636};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE AltName: Full=Rap1 GTPase {ECO:0000312|FlyBase:FBgn0004636};
DE AltName: Full=Ras-like protein 3 {ECO:0000303|PubMed:3926484};
DE Flags: Precursor;
GN Name=Rap1 {ECO:0000312|FlyBase:FBgn0004636};
GN Synonyms=R {ECO:0000312|FlyBase:FBgn0004636},
GN RAP {ECO:0000303|PubMed:1934069}, ras3 {ECO:0000303|PubMed:3926484};
GN ORFNames=CG1956 {ECO:0000312|FlyBase:FBgn0004636};
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 [GENOMIC DNA].
RX PubMed=3926484; DOI=10.1002/j.1460-2075.1985.tb03643.x;
RA Schejter E.D., Shilo B.-Z.;
RT "Characterization of functional domains of p21 ras by use of chimeric
RT genes.";
RL EMBO J. 4:407-412(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1934069; DOI=10.1016/0092-8674(91)90066-8;
RA Hariharan I.K., Carthew R.W., Rubin G.M.;
RT "The Drosophila roughened mutation: activation of a rap homolog disrupts
RT eye development and interferes with cell determination.";
RL Cell 67:717-722(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A1;
RX PubMed=10552039; DOI=10.1007/pl00006579;
RA Gasperini R., Gibson G.;
RT "Absence of protein polymorphism in the Ras genes of Drosophila
RT melanogaster.";
RL J. Mol. Evol. 49:583-590(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178.
RC STRAIN=Ral1;
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. Plays a role in photoreceptor cell determination.
CC {ECO:0000269|PubMed:1934069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61224};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit disruption of the early stages of
CC photoreceptor cell determination, adult eyes lack the R7 cell.
CC {ECO:0000269|PubMed:1934069}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26131.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X02200; CAA26131.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M80535; AAA28845.1; -; Genomic_DNA.
DR EMBL; AF186654; AAF15520.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47583.1; -; Genomic_DNA.
DR EMBL; AY121688; AAM52015.1; -; mRNA.
DR EMBL; DQ138746; ABA86352.1; -; Genomic_DNA.
DR PIR; A41217; A41217.
DR PIR; S07187; TVFFR3.
DR RefSeq; NP_001189023.1; NM_001202094.2.
DR RefSeq; NP_001261295.1; NM_001274366.1.
DR RefSeq; NP_476857.1; NM_057509.5.
DR AlphaFoldDB; P08645; -.
DR SMR; P08645; -.
DR BioGRID; 63773; 48.
DR IntAct; P08645; 1.
DR STRING; 7227.FBpp0072746; -.
DR PaxDb; P08645; -.
DR PRIDE; P08645; -.
DR EnsemblMetazoa; FBtr0072867; FBpp0072746; FBgn0004636.
DR EnsemblMetazoa; FBtr0303154; FBpp0292253; FBgn0004636.
DR EnsemblMetazoa; FBtr0332671; FBpp0304917; FBgn0004636.
DR GeneID; 38244; -.
DR KEGG; dme:Dmel_CG1956; -.
DR CTD; 38244; -.
DR FlyBase; FBgn0004636; Rap1.
DR VEuPathDB; VectorBase:FBgn0004636; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000164058; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P08645; -.
DR OMA; NVPMVIV; -.
DR OrthoDB; 1353024at2759; -.
DR PhylomeDB; P08645; -.
DR BRENDA; 3.6.5.2; 1994.
DR Reactome; R-DME-170968; Frs2-mediated activation.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; P08645; -.
DR BioGRID-ORCS; 38244; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rap1; fly.
DR GenomeRNAi; 38244; -.
DR PRO; PR:P08645; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004636; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR ExpressionAtlas; P08645; baseline and differential.
DR Genevisible; P08645; DM.
DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IDA:FlyBase.
DR GO; GO:0034333; P:adherens junction assembly; IGI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0071320; P:cellular response to cAMP; IBA:GO_Central.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IGI:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IDA:FlyBase.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0032486; P:Rap protein signal transduction; IDA:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd04175; Rap1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038851; Rap1.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome; Sensory transduction;
KW Vision.
FT CHAIN 1..181
FT /note="Ras-related protein Rap1"
FT /id="PRO_0000030191"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030192"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 181
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 157
FT /note="F -> L (in roughened mutants)"
FT CONFLICT 45..49
FT /note="EVDGQ -> KVNER (in Ref. 1; CAA26131)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="LD -> VN (in Ref. 1; CAA26131)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="D -> N (in Ref. 1; CAA26131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 20863 MW; 9A55889B61FEDE13 CRC64;
MREYKIVVLG SGGVGKSALT VQFVQCIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MVLVGNKCDL
EEERVVGKEL GKNLATQFNC AFMETSAKAK VNVNDIFYDL VRQINKKSPE KKQKKPKKSL
CVLL
