RHEB_DROME
ID RHEB_DROME Reviewed; 182 AA.
AC Q9VND8; Q0KIB7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=GTP-binding protein Rheb homolog;
DE Flags: Precursor;
GN Name=Rheb; ORFNames=CG1081;
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=Head;
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 [4]
RP FUNCTION.
RX PubMed=22493059; DOI=10.1128/mcb.06474-11;
RA Wang T., Blumhagen R., Lao U., Kuo Y., Edgar B.A.;
RT "LST8 regulates cell growth via target-of-rapamycin complex 2 (TORC2).";
RL Mol. Cell. Biol. 32:2203-2213(2012).
CC -!- FUNCTION: Binds GTP and exhibits intrinsic GTPase activity (By
CC similarity). Activates the protein kinase activity of TORC1, and
CC thereby plays a role in the regulation of apoptosis (PubMed:22493059).
CC Stimulates the phosphorylation of S6K through activation of TORC1
CC signaling (PubMed:22493059). May also have a role in activating TORC2
CC signaling (PubMed:22493059). {ECO:0000250|UniProtKB:Q15382,
CC ECO:0000269|PubMed:22493059}.
CC -!- INTERACTION:
CC Q9VND8; Q9VS51: Cln7; NbExp=3; IntAct=EBI-4372932, EBI-180370;
CC Q9VND8; Q9VGS2: Tctp; NbExp=3; IntAct=EBI-4372932, EBI-100452;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15382}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF52004.3; -; Genomic_DNA.
DR EMBL; AY094697; AAM11050.1; -; mRNA.
DR RefSeq; NP_730950.2; NM_169068.3.
DR RefSeq; NP_730951.2; NM_169069.3.
DR AlphaFoldDB; Q9VND8; -.
DR SMR; Q9VND8; -.
DR BioGRID; 72870; 112.
DR DIP; DIP-60269N; -.
DR IntAct; Q9VND8; 4.
DR MINT; Q9VND8; -.
DR STRING; 7227.FBpp0078342; -.
DR PaxDb; Q9VND8; -.
DR PRIDE; Q9VND8; -.
DR DNASU; 117332; -.
DR EnsemblMetazoa; FBtr0078693; FBpp0078342; FBgn0041191.
DR EnsemblMetazoa; FBtr0078694; FBpp0078343; FBgn0041191.
DR GeneID; 117332; -.
DR KEGG; dme:Dmel_CG1081; -.
DR CTD; 6009; -.
DR FlyBase; FBgn0041191; Rheb.
DR VEuPathDB; VectorBase:FBgn0041191; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000165909; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q9VND8; -.
DR OMA; SARHNEN; -.
DR OrthoDB; 1320427at2759; -.
DR PhylomeDB; Q9VND8; -.
DR Reactome; R-DME-110523; TOR signaling pathway.
DR Reactome; R-DME-1632852; Macroautophagy.
DR Reactome; R-DME-165159; MTOR signalling.
DR Reactome; R-DME-166208; mTORC1-mediated signalling.
DR Reactome; R-DME-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9VND8; -.
DR BioGRID-ORCS; 117332; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 117332; -.
DR PRO; PR:Q9VND8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0041191; Expressed in oviduct (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VND8; baseline and differential.
DR Genevisible; Q9VND8; DM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:FlyBase.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:FlyBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
DR GO; GO:1904503; P:negative regulation of lipophagy; IMP:FlyBase.
DR GO; GO:1903940; P:negative regulation of TORC2 signaling; IDA:UniProtKB.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IDA:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0090070; P:positive regulation of ribosome biogenesis; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:FlyBase.
DR GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IEP:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
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 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..179
FT /note="GTP-binding protein Rheb homolog"
FT /id="PRO_0000082711"
FT PROPEP 180..182
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281368"
FT MOTIF 34..42
FT /note="Effector region"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 31..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8TAI7"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 148..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT MOD_RES 179
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 179
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 182 AA; 20731 MW; CAB8AE2A988A0179 CRC64;
MPTKERHIAM MGYRSVGKSS LCIQFVEGQF VDSYDPTIEN TFTKIERVKS QDYIVKLIDT
AGQDEYSIFP VQYSMDYHGY VLVYSITSQK SFEVVKIIYE KLLDVMGKKY VPVVLVGNKI
DLHQERTVST EEGKKLAESW RAAFLETSAK QNESVGDIFH QLLILIENEN GNPQEKSGCL
VS
