RHOL_DROME
ID RHOL_DROME Reviewed; 190 AA.
AC Q24192; Q541G3; Q9U5D4; Q9VHC9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ras-like GTP-binding protein RhoL;
DE Flags: Precursor;
GN Name=RhoL; Synonyms=Drac3; ORFNames=CG9366;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=8636236; DOI=10.1083/jcb.133.3.617;
RA Murphy A.M., Montell D.J.;
RT "Cell type-specific roles for Cdc42, Rac, and RhoL in Drosophila
RT oogenesis.";
RL J. Cell Biol. 133:617-630(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=9197407; DOI=10.1007/s004380050443;
RA Sasamura T., Kobayashi T., Kojima S., Qadota H., Ohya Y., Masai I.,
RA Hotta Y.;
RT "Molecular cloning and characterization of Drosophila genes encoding small
RT GTPases of the rab and rho families.";
RL Mol. Gen. Genet. 254:486-494(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the maturation of hemocytes.
CC {ECO:0000269|PubMed:9197407}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the embryonic cephalic mesoderm
CC starting from stage 6 and fading by stage 11. Hemocyte precursor cells.
CC {ECO:0000269|PubMed:9197407}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC {ECO:0000269|PubMed:8636236}.
CC -!- DISRUPTION PHENOTYPE: Hemocyte precursor cells start to differentiate
CC normally, but never develop into mature hemocytes.
CC {ECO:0000269|PubMed:9197407}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U50314; AAB05666.1; -; mRNA.
DR EMBL; AB035355; BAA87881.1; -; mRNA.
DR EMBL; AE014297; AAF54385.1; -; Genomic_DNA.
DR EMBL; AY069811; AAL39956.1; -; mRNA.
DR RefSeq; NP_524292.1; NM_079568.3.
DR AlphaFoldDB; Q24192; -.
DR SMR; Q24192; -.
DR BioGRID; 66297; 4.
DR IntAct; Q24192; 1.
DR STRING; 7227.FBpp0293883; -.
DR PaxDb; Q24192; -.
DR DNASU; 41136; -.
DR EnsemblMetazoa; FBtr0082124; FBpp0081602; FBgn0014380.
DR GeneID; 41136; -.
DR KEGG; dme:Dmel_CG9366; -.
DR UCSC; CG9366-RA; d. melanogaster.
DR CTD; 562845; -.
DR FlyBase; FBgn0014380; RhoL.
DR VEuPathDB; VectorBase:FBgn0014380; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q24192; -.
DR OMA; NHACNIV; -.
DR PhylomeDB; Q24192; -.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9706019; RHOBTB3 ATPase cycle.
DR SignaLink; Q24192; -.
DR BioGRID-ORCS; 41136; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41136; -.
DR PRO; PR:Q24192; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0014380; Expressed in adult midgut (Drosophila) and 32 other tissues.
DR ExpressionAtlas; Q24192; baseline and differential.
DR Genevisible; Q24192; DM.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007516; P:hemocyte development; IMP:UniProtKB.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..187
FT /note="Ras-like GTP-binding protein RhoL"
FT /id="PRO_0000198886"
FT PROPEP 188..190
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281239"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 187
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 187
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 131
FT /note="N -> S (in Ref. 2; BAA87881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21880 MW; 9E35F487F7445184 CRC64;
MTANITKSPR PLKITIVGDG MVGKTCMLIT YTRNEFPEEY IPTVFDNHAC NIAVDDRDYN
LTLWDTAGQE DYERLRPLSY PSTNCFLLCY SISSRTSFEN VKSKWWPEIR HFSAHVPVVL
VGTKLDLRIP NSEKFVTTQE GKKMRKEIHA FNLVECSAKK KQNLQQVFEE AVRAVERKPK
TTSKQSCKIL
