RAC1_DROME
ID RAC1_DROME Reviewed; 192 AA.
AC P40792; Q9W0H7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Ras-related protein Rac1;
DE Flags: Precursor;
GN Name=Rac1; Synonyms=RacA; ORFNames=CG2248;
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.
RC STRAIN=Oregon-R;
RX PubMed=7958857; DOI=10.1101/gad.8.15.1787;
RA Luo L., Liao Y.J., Jan L.Y., Jan Y.;
RT "Distinct morphogenetic functions of similar small GTPases: Drosophila
RT Drac1 is involved in axonal outgrowth and myoblast fusion.";
RL Genes Dev. 8:1787-1802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=7720592; DOI=10.1242/dev.121.3.903;
RA Harden N., Loh H., Chia W., Lim L.;
RT "A dominant inhibitory version of the small GTP-binding protein Rac
RT disrupts cytoskeletal structures and inhibits developmental cell shape
RT changes in Drosophila.";
RL Development 121:903-914(1995).
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 INTERACTION WITH PAK.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=8628256; DOI=10.1128/mcb.16.5.1896;
RA Harden N., Lee J., Loh H.Y., Ong Y.M., Tan I., Leung T., Manser E., Lim L.;
RT "A Drosophila homolog of the Rac- and Cdc42-activated serine/threonine
RT kinase PAK is a potential focal adhesion and focal complex protein that
RT colocalizes with dynamic actin structures.";
RL Mol. Cell. Biol. 16:1896-1908(1996).
RN [8]
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 [9]
RP INTERACTION WITH SRA-1.
RX PubMed=12818175; DOI=10.1016/s0896-6273(03)00354-4;
RA Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L.,
RA Giangrande A.;
RT "CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the
RT Rac1 GTPase pathway to the fragile X protein.";
RL Neuron 38:887-898(2003).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=22547074; DOI=10.1074/jbc.m111.333807;
RA Shiratsuchi A., Mori T., Sakurai K., Nagaosa K., Sekimizu K., Lee B.L.,
RA Nakanishi Y.;
RT "Independent recognition of Staphylococcus aureus by two receptors for
RT phagocytosis in Drosophila.";
RL J. Biol. Chem. 287:21663-21672(2012).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24855950; DOI=10.1016/j.cell.2014.03.045;
RA Cai D., Chen S.C., Prasad M., He L., Wang X., Choesmel-Cadamuro V.,
RA Sawyer J.K., Danuser G., Montell D.J.;
RT "Mechanical feedback through E-cadherin promotes direction sensing during
RT collective cell migration.";
RL Cell 157:1146-1159(2014).
CC -!- FUNCTION: During various developmental processes, regulates changes in
CC cell morphology in response to extracellular signals (PubMed:7958857,
CC PubMed:10323867, PubMed:24855950). During oogenesis, mediates signaling
CC from the tyrosine kinase (RTK) chemoattractant receptors (Egfr and Pvr)
CC to the guidance pathway that control the directional persistent
CC collective migration of the border cell (BC) cluster through the nurse
CC cells to the oocyte. Once activating by Pvr and Egfr, promotes the
CC formation of forward-directed actin protrusions which stabilize the DE-
CC cadherin (shg)-mediated adhesions. In turn, DE-mediated adhesion
CC between the leader border cells and nurse cells further promotes Rac1
CC signaling creating a positive feedback loop that amplifies the output
CC of RTK activity and leads to higher Rac activity at the front, thus
CC promoting polarization of the border cell cluster and directionally
CC persistent migration (PubMed:24855950). Involved in axon outgrowth and
CC myoblast fusion (PubMed:7958857). Plays a role in regulating dorsal
CC closure during embryogenesis (PubMed:10323867). Involved in integrin
CC alpha-PS3/beta-nu-mediated phagocytosis of Gram-positive S.aureus by
CC hemocytes (PubMed:22547074). {ECO:0000269|PubMed:10323867,
CC ECO:0000269|PubMed:22547074, ECO:0000269|PubMed:24855950,
CC ECO:0000269|PubMed:7958857}.
CC -!- SUBUNIT: Interacts with Sra-1. Interacts (via REM 1 repeats) with Pkn
CC (via N-terminus). When GTP-bound, interacts with Pak (PubMed:8628256).
CC {ECO:0000269|PubMed:10323867, ECO:0000269|PubMed:12818175,
CC ECO:0000269|PubMed:17507675, ECO:0000269|PubMed:8628256}.
CC -!- INTERACTION:
CC P40792; P25843: chic; NbExp=3; IntAct=EBI-74845, EBI-156199;
CC P40792; Q9VI13: Pak; NbExp=3; IntAct=EBI-74845, EBI-74826;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in oocyte border cells (BC), with
CC increased expression at the front of the BC cluster.
CC {ECO:0000269|PubMed:24855950}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U11823; AAA62870.1; -; mRNA.
DR EMBL; L38309; AAA67040.1; -; mRNA.
DR EMBL; Z35642; CAA84709.1; -; mRNA.
DR EMBL; AE014296; AAF47469.1; -; Genomic_DNA.
DR EMBL; AY060408; AAL25447.1; -; mRNA.
DR PIR; I45715; I45715.
DR PIR; S51718; S51718.
DR PIR; S54295; S54295.
DR RefSeq; NP_001261247.1; NM_001274318.1.
DR RefSeq; NP_476950.1; NM_057602.4.
DR AlphaFoldDB; P40792; -.
DR SMR; P40792; -.
DR BioGRID; 63689; 125.
DR IntAct; P40792; 4.
DR STRING; 7227.FBpp0304252; -.
DR PaxDb; P40792; -.
DR PRIDE; P40792; -.
DR EnsemblMetazoa; FBtr0072730; FBpp0072614; FBgn0010333.
DR EnsemblMetazoa; FBtr0331868; FBpp0304252; FBgn0010333.
DR GeneID; 38146; -.
DR KEGG; dme:Dmel_CG2248; -.
DR CTD; 5879; -.
DR FlyBase; FBgn0010333; Rac1.
DR VEuPathDB; VectorBase:FBgn0010333; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155205; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P40792; -.
DR OMA; DRRMQPI; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P40792; -.
DR Reactome; R-DME-114604; GPVI-mediated activation cascade.
DR Reactome; R-DME-1433557; Signaling by SCF-KIT.
DR Reactome; R-DME-193648; NRAGE signals death through JNK.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-2424491; DAP12 signaling.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-350376; Activation of RAC1:GTP by FZ:DSH complex.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-3928664; Ephrin signaling.
DR Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-4086400; PCP/CE pathway.
DR Reactome; R-DME-418885; DCC mediated attractive signaling.
DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DME-445144; Signal transduction by L1.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DME-5625900; RHO GTPases activate CIT.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-5687128; MAPK6/MAPK4 signaling.
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-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-DME-9748787; Azathioprine ADME.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P40792; -.
DR BioGRID-ORCS; 38146; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rac1; fly.
DR GenomeRNAi; 38146; -.
DR PRO; PR:P40792; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010333; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; P40792; baseline and differential.
DR Genevisible; P40792; DM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
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:0019897; C:extrinsic component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0001726; C:ruffle; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP: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:0032147; P:activation of protein kinase activity; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP: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:0016358; P:dendrite development; IMP:FlyBase.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
DR GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; IMP:FlyBase.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
DR GO; GO:0048615; P:embryonic anterior midgut (ectodermal) morphogenesis; IMP:FlyBase.
DR GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007516; P:hemocyte development; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0035320; P:imaginal disc-derived wing hair site selection; IMP:FlyBase.
DR GO; GO:0002433; P:immune response-regulating cell surface receptor signaling pathway involved in phagocytosis; IDA:FlyBase.
DR GO; GO:0007254; P:JNK cascade; IMP:FlyBase.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IGI:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0051450; P:myoblast proliferation; IMP:FlyBase.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0110125; P:negative regulation of myotube cell migration; IMP:FlyBase.
DR GO; GO:0097206; P:nephrocyte filtration; IMP:FlyBase.
DR GO; GO:0031175; P:neuron projection development; 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:0045773; P:positive regulation of axon extension; IGI:FlyBase.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI: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; IGI:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1903391; P:regulation of adherens junction organization; IMP:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IMP:FlyBase.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:FlyBase.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0050975; P:sensory perception of touch; IMP:FlyBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IGI:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; 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 Cell membrane; Developmental protein; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phagocytosis; Prenylation;
KW Reference proteome.
FT CHAIN 1..189
FT /note="Ras-related protein Rac1"
FT /id="PRO_0000198893"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281244"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
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 115..118
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 CONFLICT 135
FT /note="A -> V (in Ref. 1; AAA62870)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..146
FT /note="LAMA -> SGHG (in Ref. 2; AAA67040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21354 MW; F910B54BDBD8AFA3 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWYPE VRHHCPSTPI ILVGTKLDLR
DDKNTIEKLR DKKLAPITYP QGLAMAKEIG AVKYLECSAL TQKGLKTVFD EAIRSVLCPV
LQPKSKRKCA LL
