RAC2_DROME
ID RAC2_DROME Reviewed; 192 AA.
AC P48554; Q540X5; Q9VS69;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ras-related protein Rac2;
DE Flags: Precursor;
GN Name=Rac2; Synonyms=RacB; ORFNames=CG8556;
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].
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 [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 [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=Ovary;
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 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 [7]
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).
CC -!- FUNCTION: Involved in integrin alpha-PS3/beta-nu-mediated phagocytosis
CC of Gram-positive S.aureus by hemocytes. {ECO:0000269|PubMed:22547074}.
CC -!- SUBUNIT: Interacts with Pkn (via N-terminus).
CC {ECO:0000269|PubMed:10323867}.
CC -!- INTERACTION:
CC P48554; Q9VI13: Pak; NbExp=3; IntAct=EBI-74869, EBI-74826;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
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DR EMBL; L38310; AAA67041.1; -; mRNA.
DR EMBL; Z35643; CAA84710.1; -; mRNA.
DR EMBL; AE014296; AAF50559.1; -; Genomic_DNA.
DR EMBL; AY118845; AAM50705.1; -; mRNA.
DR PIR; S54296; S54296.
DR RefSeq; NP_001261517.1; NM_001274588.2.
DR RefSeq; NP_648121.1; NM_139864.3.
DR AlphaFoldDB; P48554; -.
DR SMR; P48554; -.
DR BioGRID; 64269; 24.
DR DIP; DIP-18225N; -.
DR IntAct; P48554; 7.
DR STRING; 7227.FBpp0305023; -.
DR PaxDb; P48554; -.
DR PRIDE; P48554; -.
DR EnsemblMetazoa; FBtr0076867; FBpp0076577; FBgn0014011.
DR EnsemblMetazoa; FBtr0332800; FBpp0305023; FBgn0014011.
DR GeneID; 38831; -.
DR KEGG; dme:Dmel_CG8556; -.
DR CTD; 5880; -.
DR FlyBase; FBgn0014011; Rac2.
DR VEuPathDB; VectorBase:FBgn0014011; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155205; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P48554; -.
DR OMA; EINAVKF; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P48554; -.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9706019; RHOBTB3 ATPase cycle.
DR SignaLink; P48554; -.
DR BioGRID-ORCS; 38831; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38831; -.
DR PRO; PR:P48554; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0014011; Expressed in embryonic/larval hemocyte (Drosophila) and 55 other tissues.
DR ExpressionAtlas; P48554; baseline and differential.
DR Genevisible; P48554; DM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IGI:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IGI:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0002118; P:aggressive behavior; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; 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:0007631; P:feeding behavior; IMP:FlyBase.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; 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:0007617; P:mating behavior; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0008078; P:mesodermal cell migration; IGI:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0016203; P:muscle attachment; IGI:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; TAS:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
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; IGI: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:0010883; P:regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0007266; P:Rho protein signal transduction; IGI:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IGI:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IGI: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 Rac2"
FT /id="PRO_0000198894"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281245"
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"
SQ SEQUENCE 192 AA; 21359 MW; 06AE11CC18019982 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWFPE VRHHCPSVPI ILVGTKLDLR
DDKQTIEKLK DKKLTPITYP QGLAMAKEIA AVKYLECSAL TQKGLKTVFD EAIRSVLCPV
VRGPKRHKCA LL
