RHO1_DROME
ID RHO1_DROME Reviewed; 192 AA.
AC P48148; A4UZI6; Q0E958; Q9V3J0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Ras-like GTP-binding protein Rho1;
DE Flags: Precursor;
GN Name=Rho1 {ECO:0000312|FlyBase:FBgn0014020};
GN ORFNames=CG8416 {ECO:0000312|FlyBase:FBgn0014020};
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 FUNCTION.
RX PubMed=7835340; DOI=10.1002/j.1460-2075.1995.tb07003.x;
RA Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M.,
RA Settleman J.;
RT "Characterization of rho GTPase family homologues in Drosophila
RT melanogaster: overexpressing Rho1 in retinal cells causes a late
RT developmental defect.";
RL EMBO J. 14:292-302(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH CAPU,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=10556060; DOI=10.1242/dev.126.23.5353;
RA Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M.;
RT "Mutations in the Rho1 small GTPase disrupt morphogenesis and segmentation
RT during early Drosophila development.";
RL Development 126:5353-5364(1999).
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=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 [6]
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH PKN.
RX PubMed=10323867; DOI=10.1101/gad.13.9.1168;
RA Lu Y., Settleman J.;
RT "The Drosophila Pkn protein kinase is a Rho/Rac effector target required
RT for dorsal closure during embryogenesis.";
RL Genes Dev. 13:1168-1180(1999).
RN [8]
RP INTERACTION WITH PKN.
RX PubMed=17507675; DOI=10.1534/genetics.107.072967;
RA Betson M., Settleman J.;
RT "A rho-binding protein kinase C-like activity is required for the function
RT of protein kinase N in Drosophila development.";
RL Genetics 176:2201-2212(2007).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24535826; DOI=10.1083/jcb.201307070;
RA Simoes S., Mainieri A., Zallen J.A.;
RT "Rho GTPase and Shroom direct planar polarized actomyosin contractility
RT during convergent extension.";
RL J. Cell Biol. 204:575-589(2014).
RN [10]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND MUTAGENESIS OF 27-LYS--GLN-29;
RP PHE-39 AND 51-LYS--GLU-54.
RX PubMed=25739458; DOI=10.1091/mbc.e14-08-1266;
RA Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
RT "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune
RT cell developmental migrations.";
RL Mol. Biol. Cell 26:1665-1674(2015).
CC -!- FUNCTION: Has a role in regulating actin cytoskeletal organization:
CC required during early development for proper execution of morphogenetic
CC movements of individual cells and groups of cells important for the
CC formation of the embryonic body plan (PubMed:10556060, PubMed:24535826,
CC PubMed:25739458). Plays a role in regulating dorsal closure during
CC embryogenesis (PubMed:10556060, PubMed:10323867). During axis
CC elongation, required for Rho-kinase Rok planar polarity and adherens
CC junction localization as well as for generating a planar polarized
CC distribution of the actin-binding protein Shrm (PubMed:24535826).
CC During embryogenesis, acts upstream of wash to regulate the
CC developmental migration of tail hemocytes anteriorly along the ventral
CC midline (PubMed:25739458). May have a role in eye development
CC (PubMed:7835340). {ECO:0000269|PubMed:10323867,
CC ECO:0000269|PubMed:10556060, ECO:0000269|PubMed:24535826,
CC ECO:0000269|PubMed:25739458, ECO:0000269|PubMed:7835340}.
CC -!- SUBUNIT: Interacts with capu (PubMed:10556060). Interacts (via REM
CC repeats) with Pkn (via N-terminus) (PubMed:10323867, PubMed:17507675).
CC Interacts (via N-terminus) with wash (via N-terminus)
CC (PubMed:25739458). {ECO:0000269|PubMed:10323867,
CC ECO:0000269|PubMed:10556060, ECO:0000269|PubMed:17507675}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton.
CC Apical cell membrane {ECO:0000269|PubMed:24535826}. Lateral cell
CC membrane {ECO:0000269|PubMed:24535826}.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes (at protein level).
CC {ECO:0000269|PubMed:25739458}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Embryos exhibit severe defects
CC in head involution and imperfect dorsal closure. During head
CC involution, the head structures fail to internalize resulting in holes
CC in the dorsal anterior region of the cuticle. The disruption in the
CC dorsal surface stretches the ventral surface, causing the cuticle to
CC bow. {ECO:0000269|PubMed:10556060}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; L38311; AAA67042.1; -; mRNA.
DR EMBL; AF177871; AAF01183.1; -; Genomic_DNA.
DR EMBL; AF177872; AAF01184.1; -; mRNA.
DR EMBL; AF177873; AAF01185.1; -; mRNA.
DR EMBL; AF177874; AAF01186.1; -; mRNA.
DR EMBL; AE013599; AAM70944.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70945.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70946.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64843.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64844.1; -; Genomic_DNA.
DR EMBL; AY119536; AAM50190.1; -; mRNA.
DR EMBL; BT010085; AAQ22554.1; -; mRNA.
DR PIR; S54294; S54294.
DR RefSeq; NP_477098.1; NM_057750.4.
DR RefSeq; NP_599135.1; NM_134308.3.
DR RefSeq; NP_599136.1; NM_134309.2.
DR RefSeq; NP_725524.1; NM_166139.3.
DR RefSeq; NP_995849.1; NM_206127.2.
DR RefSeq; NP_995850.1; NM_206128.2.
DR AlphaFoldDB; P48148; -.
DR SMR; P48148; -.
DR BioGRID; 62500; 94.
DR DIP; DIP-22676N; -.
DR IntAct; P48148; 1.
DR STRING; 7227.FBpp0086354; -.
DR PaxDb; P48148; -.
DR PRIDE; P48148; -.
DR DNASU; 36775; -.
DR EnsemblMetazoa; FBtr0087211; FBpp0086353; FBgn0014020.
DR EnsemblMetazoa; FBtr0087212; FBpp0086354; FBgn0014020.
DR EnsemblMetazoa; FBtr0087213; FBpp0086355; FBgn0014020.
DR EnsemblMetazoa; FBtr0087214; FBpp0086356; FBgn0014020.
DR EnsemblMetazoa; FBtr0087216; FBpp0089129; FBgn0014020.
DR EnsemblMetazoa; FBtr0087217; FBpp0089130; FBgn0014020.
DR GeneID; 36775; -.
DR KEGG; dme:Dmel_CG8416; -.
DR UCSC; CG8416-RC; d. melanogaster.
DR CTD; 36775; -.
DR FlyBase; FBgn0014020; Rho1.
DR VEuPathDB; VectorBase:FBgn0014020; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P48148; -.
DR OMA; KINACAY; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P48148; -.
DR Reactome; R-DME-114604; GPVI-mediated activation cascade.
DR Reactome; R-DME-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-DME-198203; PI3K/AKT activation.
DR Reactome; R-DME-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-DME-350368; Activation of RHO1 by FZ:DSH complex.
DR Reactome; R-DME-350407; RHO1 GTPase cycle.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DME-4086400; PCP/CE pathway.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DME-450728; Inhibition of actin polymerisation.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5625900; RHO GTPases activate CIT.
DR Reactome; R-DME-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-DME-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DME-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR Reactome; R-DME-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 36775; 3 hits in 3 CRISPR screens.
DR ChiTaRS; Rho1; fly.
DR GenomeRNAi; 36775; -.
DR PRO; PR:P48148; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0014020; Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues.
DR Genevisible; P48148; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0070451; C:cell hair; IDA:FlyBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0019900; F:kinase binding; IPI:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; TAS:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IGI:FlyBase.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0046663; P:dorsal closure, leading edge cell differentiation; IMP:FlyBase.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0045184; P:establishment of protein localization; IMP:FlyBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:FlyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:FlyBase.
DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IDA:FlyBase.
DR GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0110020; P:regulation of actomyosin structure organization; IGI:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IMP:FlyBase.
DR GO; GO:0035298; P:regulation of Malpighian tubule size; IMP:FlyBase.
DR GO; GO:1901739; P:regulation of myoblast fusion; IGI:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IGI:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; 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; 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 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome; Sensory transduction;
KW Vision.
FT CHAIN 1..189
FT /note="Ras-like GTP-binding protein Rho1"
FT /id="PRO_0000198885"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281238"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 27..29
FT /note="KDQ->AAA: Reduces binding to wash. Reduces the
FT number of hemocytes migrating anteriorly from the tail
FT during embryogenesis."
FT /evidence="ECO:0000269|PubMed:25739458"
FT MUTAGEN 39
FT /note="F->V: No effect on binding to wash and no effect on
FT tail hemocyte developmental migration from the tail."
FT /evidence="ECO:0000269|PubMed:25739458"
FT MUTAGEN 51..54
FT /note="KQVE->AAAA: No effect on binding to wash."
FT /evidence="ECO:0000269|PubMed:25739458"
SQ SEQUENCE 192 AA; 21723 MW; B89C7D884E1743CF CRC64;
MTTIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRNDPNTIRD LAKMKQEPVK PQEGRAMAEK INAFAYLECS AKSKEGVRDV FETATRAALQ
VKKRKKTRCL LL
