CDC42_DROME
ID CDC42_DROME Reviewed; 191 AA.
AC P40793; Q540W4; Q9U9S3; Q9U9S4; Q9U9S5; Q9U9S6; Q9V465;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Cdc42 homolog;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953};
DE Flags: Precursor;
GN Name=Cdc42; ORFNames=CG12530;
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].
RC STRAIN=Oregon-R; TISSUE=Embryo;
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 [GENOMIC DNA].
RX PubMed=10772800; DOI=10.1006/dbio.2000.9671;
RA Genova J.L., Jong S., Camp J.T., Fehon R.G.;
RT "Functional analysis of Cdc42 in actin filament assembly, epithelial
RT morphogenesis, and cell signaling during Drosophila development.";
RL Dev. Biol. 221:181-194(2000).
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 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 [7]
RP INTERACTION WITH GEK.
RX PubMed=9371783; DOI=10.1073/pnas.94.24.12963;
RA Luo L., Lee T., Tsai L., Tang G., Jan L.Y., Jan Y.N.;
RT "Genghis Khan (Gek) as a putative effector for Drosophila Cdc42 and
RT regulator of actin polymerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12963-12968(1997).
RN [8]
RP FUNCTION, INTERACTION WITH MBT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-12.
RX PubMed=12490550; DOI=10.1242/dev.00248;
RA Schneeberger D., Raabe T.;
RT "Mbt, a Drosophila PAK protein, combines with Cdc42 to regulate
RT photoreceptor cell morphogenesis.";
RL Development 130:427-437(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH FRL.
RX PubMed=26801180; DOI=10.1534/genetics.115.181438;
RA Dollar G., Gombos R., Barnett A.A., Sanchez Hernandez D., Maung S.M.,
RA Mihaly J., Jenny A.;
RT "Unique and Overlapping Functions of Formins Frl and DAAM During Ommatidial
RT Rotation and Neuronal Development in Drosophila.";
RL Genetics 202:1135-1151(2016).
CC -!- FUNCTION: Regulates mbt kinase activity and is also required to recruit
CC mbt to adherens junctions (PubMed:12490550). Together with mbt and Frl,
CC regulates photoreceptor cell morphogenesis (PubMed:12490550,
CC PubMed:26801180). Together with Frl, has a role in the neuronal
CC development of mushroom bodies (PubMed:26801180).
CC {ECO:0000269|PubMed:12490550, ECO:0000269|PubMed:26801180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P60766,
CC ECO:0000250|UniProtKB:P60953};
CC -!- SUBUNIT: Interacts with Frl (via GBD/FH3 domain); the interaction is
CC stronger with the GTP bound form of Cdc42 (PubMed:26801180). The GTP-
CC bound but not the GDP-bound form interacts with mbt and gek
CC (PubMed:9371783, PubMed:12490550). When GTP-bound, interacts with Pak
CC (PubMed:8628256). {ECO:0000269|PubMed:12490550,
CC ECO:0000269|PubMed:26801180, ECO:0000269|PubMed:8628256,
CC ECO:0000269|PubMed:9371783}.
CC -!- INTERACTION:
CC P40793; Q9VXE5: mbt; NbExp=2; IntAct=EBI-114324, EBI-75994;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:12490550}. Cell membrane
CC {ECO:0000269|PubMed:12490550}; Lipid-anchor
CC {ECO:0000269|PubMed:12490550}. Note=Adherens junctions of developing
CC photoreceptor cells.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42
CC subfamily. {ECO:0000305}.
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DR EMBL; U11824; AAA62871.1; -; mRNA.
DR EMBL; AF153423; AAD43787.1; -; Genomic_DNA.
DR EMBL; AF153424; AAD43788.1; -; Genomic_DNA.
DR EMBL; AF153425; AAD43789.1; -; Genomic_DNA.
DR EMBL; AF153426; AAD43790.1; -; Genomic_DNA.
DR EMBL; AF153427; AAD43791.1; -; Genomic_DNA.
DR EMBL; AF153428; AAD43792.1; -; Genomic_DNA.
DR EMBL; AF153429; AAD43793.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF49007.1; -; Genomic_DNA.
DR EMBL; AY119570; AAM50224.1; -; mRNA.
DR PIR; I45716; I45716.
DR RefSeq; NP_001245762.1; NM_001258833.3.
DR RefSeq; NP_001245763.1; NM_001258834.3.
DR RefSeq; NP_523414.1; NM_078690.4.
DR AlphaFoldDB; P40793; -.
DR SMR; P40793; -.
DR BioGRID; 59277; 61.
DR DIP; DIP-31003N; -.
DR IntAct; P40793; 2.
DR MINT; P40793; -.
DR STRING; 7227.FBpp0301153; -.
DR PaxDb; P40793; -.
DR PRIDE; P40793; -.
DR EnsemblMetazoa; FBtr0074751; FBpp0074520; FBgn0010341.
DR EnsemblMetazoa; FBtr0309214; FBpp0301153; FBgn0010341.
DR EnsemblMetazoa; FBtr0309215; FBpp0301154; FBgn0010341.
DR GeneID; 32981; -.
DR KEGG; dme:Dmel_CG12530; -.
DR CTD; 998; -.
DR FlyBase; FBgn0010341; Cdc42.
DR VEuPathDB; VectorBase:FBgn0010341; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153675; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P40793; -.
DR OMA; ITHHQQK; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P40793; -.
DR Reactome; R-DME-114604; GPVI-mediated activation cascade.
DR Reactome; R-DME-182971; EGFR downregulation.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-DME-418885; DCC mediated attractive signaling.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR Reactome; R-DME-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DME-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DME-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P40793; -.
DR BioGRID-ORCS; 32981; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Cdc42; fly.
DR GenomeRNAi; 32981; -.
DR PRO; PR:P40793; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010341; Expressed in seminal fluid secreting gland and 42 other tissues.
DR ExpressionAtlas; P40793; baseline and differential.
DR Genevisible; P40793; DM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IMP:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; IMP:FlyBase.
DR GO; GO:0048675; P:axon extension; IGI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; TAS:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; TAS:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045200; P:establishment of neuroblast polarity; IMP:FlyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0051601; P:exocyst localization; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0035318; P:imaginal disc-derived wing hair outgrowth; IMP:FlyBase.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0045185; P:maintenance of protein location; IMP:UniProtKB.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0097206; P:nephrocyte filtration; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IGI:FlyBase.
DR GO; GO:0031175; P:neuron projection development; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IGI:UniProtKB.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0006909; P:phagocytosis; 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:0010592; P:positive regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IDA:FlyBase.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0007266; P:Rho protein signal transduction; IGI:FlyBase.
DR GO; GO:0050975; P:sensory perception of touch; IMP:FlyBase.
DR GO; GO:0007286; P:spermatid development; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR CDD; cd01874; Cdc42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037874; Cdc42.
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 junction; Cell membrane; Developmental protein; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Cdc42 homolog"
FT /id="PRO_0000198958"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281288"
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 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 12
FT /note="G->V: Enhances interaction with mbt. Coexpression
FT with mbt slightly reduced the substrate phosphorylation
FT ability of mbt."
FT /evidence="ECO:0000269|PubMed:12490550"
FT CONFLICT 10
FT /note="G -> D (in Ref. 2; AAD43788)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> N (in Ref. 2; AAD43792)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> L (in Ref. 2; AAD43793)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> D (in Ref. 2; AAD43790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21403 MW; 0AB96574ADC8E0E3 CRC64;
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCQKTPF LLVGTQIDLR
DENSTLEKLA KNKQKPITME QGEKLAKELK AVKYVECSAL TQKGLKNVFD EAILAALEPP
EPTKKRKCKF L
