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Protein

Cdc42 homolog

Gene

Cdc42

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates mbt kinase activity and is also required to recruit mbt to adherens junctions. Together with mbt, regulates photoreceptor cell morphogenesis.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

  • GTPase activating protein binding Source: FlyBase
  • GTPase activity Source: FlyBase
  • GTP binding Source: UniProtKB-KW
  • protein kinase binding Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • actin cytoskeleton reorganization Source: FlyBase
  • actin filament organization Source: FlyBase
  • actin filament polymerization Source: FlyBase
  • axon extension Source: FlyBase
  • axon guidance Source: FlyBase
  • axonogenesis Source: FlyBase
  • branching involved in open tracheal system development Source: FlyBase
  • cell projection assembly Source: FlyBase
  • cellularization Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • cytoskeleton organization Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • dorsal closure Source: FlyBase
  • encapsulation of foreign target Source: FlyBase
  • epithelium development Source: FlyBase
  • establishment of neuroblast polarity Source: FlyBase
  • exocyst localization Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • hemocyte migration Source: FlyBase
  • imaginal disc-derived wing hair outgrowth Source: FlyBase
  • JNK cascade Source: FlyBase
  • maintenance of cell polarity Source: FlyBase
  • maintenance of protein location Source: UniProtKB
  • melanotic encapsulation of foreign target Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • nephrocyte filtration Source: FlyBase
  • neuromuscular synaptic transmission Source: FlyBase
  • neuron projection development Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • oogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of filopodium assembly Source: FlyBase
  • positive regulation of lamellipodium assembly Source: FlyBase
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of wound healing Source: FlyBase
  • protein localization to plasma membrane Source: FlyBase
  • regulation of actin filament polymerization Source: FlyBase
  • regulation of axonogenesis Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • Rho protein signal transduction Source: FlyBase
  • sensory perception of touch Source: FlyBase
  • spermatid development Source: FlyBase
  • suture of dorsal opening Source: FlyBase
  • transforming growth factor beta receptor signaling pathway Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
  • wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-182971. EGFR downregulation.
R-DME-194840. Rho GTPase cycle.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-375170. CDO in myogenesis.
R-DME-389359. CD28 dependent Vav1 pathway.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-418885. DCC mediated attractive signaling.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5627123. RHO GTPases activate PAKs.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DME-5663220. RHO GTPases Activate Formins.
R-DME-5687128. MAPK6/MAPK4 signaling.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP40793.

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42 homolog
Gene namesi
Name:Cdc42
ORF Names:CG12530
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0010341. Cdc42.

Subcellular locationi

  • Cell junctionadherens junction 1 Publication
  • Cell membrane 1 Publication; Lipid-anchor 1 Publication

  • Note: Adherens junctions of developing photoreceptor cells.

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical part of cell Source: FlyBase
  • axon Source: FlyBase
  • cell cortex Source: FlyBase
  • cytoplasm Source: FlyBase
  • growth cone Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: UniProtKB-SubCell
  • rhabdomere Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121G → V: Enhances interaction with mbt. Coexpression with mbt slightly reduced the substrate phosphorylation ability of mbt. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Cdc42 homologPRO_0000198958Add
BLAST
Propeptidei189 – 1913Removed in mature formBy similarityPRO_0000281288

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Cysteine methyl esterBy similarity
Lipidationi188 – 1881S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP40793.
PRIDEiP40793.

Expressioni

Gene expression databases

BgeeiP40793.
ExpressionAtlasiP40793. differential.
GenevisibleiP40793. DM.

Interactioni

Subunit structurei

The GTP-bound but not the GDP-bound form interacts with mbt and gek.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mbtQ9VXE52EBI-114324,EBI-75994

GO - Molecular functioni

  • GTPase activating protein binding Source: FlyBase
  • protein kinase binding Source: FlyBase

Protein-protein interaction databases

BioGridi59277. 10 interactions.
DIPiDIP-31003N.
IntActiP40793. 1 interaction.
MINTiMINT-1206579.
STRINGi7227.FBpp0301153.

Structurei

3D structure databases

ProteinModelPortaliP40793.
SMRiP40793. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
InParanoidiP40793.
KOiK04393.
OMAiNMQTIKC.
OrthoDBiEOG764747.
PhylomeDBiP40793.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP
60 70 80 90 100
YTLGLFDTAG QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE
110 120 130 140 150
ITHHCQKTPF LLVGTQIDLR DENSTLEKLA KNKQKPITME QGEKLAKELK
160 170 180 190
AVKYVECSAL TQKGLKNVFD EAILAALEPP EPTKKRKCKF L
Length:191
Mass (Da):21,403
Last modified:February 1, 1995 - v1
Checksum:i0AB96574ADC8E0E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101G → D in AAD43788 (PubMed:10772800).Curated
Sequence conflicti65 – 651D → N in AAD43792 (PubMed:10772800).Curated
Sequence conflicti83 – 831S → L in AAD43793 (PubMed:10772800).Curated
Sequence conflicti114 – 1141G → D in AAD43790 (PubMed:10772800).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11824 mRNA. Translation: AAA62871.1.
AF153423 Genomic DNA. Translation: AAD43787.1.
AF153424 Genomic DNA. Translation: AAD43788.1.
AF153425 Genomic DNA. Translation: AAD43789.1.
AF153426 Genomic DNA. Translation: AAD43790.1.
AF153427 Genomic DNA. Translation: AAD43791.1.
AF153428 Genomic DNA. Translation: AAD43792.1.
AF153429 Genomic DNA. Translation: AAD43793.1.
AE014298 Genomic DNA. Translation: AAF49007.1.
AY119570 mRNA. Translation: AAM50224.1.
PIRiI45716.
RefSeqiNP_001245762.1. NM_001258833.3.
NP_001245763.1. NM_001258834.3.
NP_523414.1. NM_078690.4.
UniGeneiDm.2867.

Genome annotation databases

EnsemblMetazoaiFBtr0074751; FBpp0074520; FBgn0010341.
FBtr0309214; FBpp0301153; FBgn0010341.
FBtr0309215; FBpp0301154; FBgn0010341.
GeneIDi32981.
KEGGidme:Dmel_CG12530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11824 mRNA. Translation: AAA62871.1.
AF153423 Genomic DNA. Translation: AAD43787.1.
AF153424 Genomic DNA. Translation: AAD43788.1.
AF153425 Genomic DNA. Translation: AAD43789.1.
AF153426 Genomic DNA. Translation: AAD43790.1.
AF153427 Genomic DNA. Translation: AAD43791.1.
AF153428 Genomic DNA. Translation: AAD43792.1.
AF153429 Genomic DNA. Translation: AAD43793.1.
AE014298 Genomic DNA. Translation: AAF49007.1.
AY119570 mRNA. Translation: AAM50224.1.
PIRiI45716.
RefSeqiNP_001245762.1. NM_001258833.3.
NP_001245763.1. NM_001258834.3.
NP_523414.1. NM_078690.4.
UniGeneiDm.2867.

3D structure databases

ProteinModelPortaliP40793.
SMRiP40793. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59277. 10 interactions.
DIPiDIP-31003N.
IntActiP40793. 1 interaction.
MINTiMINT-1206579.
STRINGi7227.FBpp0301153.

Proteomic databases

PaxDbiP40793.
PRIDEiP40793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074751; FBpp0074520; FBgn0010341.
FBtr0309214; FBpp0301153; FBgn0010341.
FBtr0309215; FBpp0301154; FBgn0010341.
GeneIDi32981.
KEGGidme:Dmel_CG12530.

Organism-specific databases

CTDi998.
FlyBaseiFBgn0010341. Cdc42.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
InParanoidiP40793.
KOiK04393.
OMAiNMQTIKC.
OrthoDBiEOG764747.
PhylomeDBiP40793.

Enzyme and pathway databases

ReactomeiR-DME-182971. EGFR downregulation.
R-DME-194840. Rho GTPase cycle.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-375170. CDO in myogenesis.
R-DME-389359. CD28 dependent Vav1 pathway.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-418885. DCC mediated attractive signaling.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5627123. RHO GTPases activate PAKs.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DME-5663220. RHO GTPases Activate Formins.
R-DME-5687128. MAPK6/MAPK4 signaling.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP40793.

Miscellaneous databases

GenomeRNAii32981.
PROiP40793.

Gene expression databases

BgeeiP40793.
ExpressionAtlasiP40793. differential.
GenevisibleiP40793. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion."
    Luo L., Liao Y.J., Jan L.Y., Jan Y.
    Genes Dev. 8:1787-1802(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "Functional analysis of Cdc42 in actin filament assembly, epithelial morphogenesis, and cell signaling during Drosophila development."
    Genova J.L., Jong S., Camp J.T., Fehon R.G.
    Dev. Biol. 221:181-194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Genghis Khan (Gek) as a putative effector for Drosophila Cdc42 and regulator of actin polymerization."
    Luo L., Lee T., Tsai L., Tang G., Jan L.Y., Jan Y.N.
    Proc. Natl. Acad. Sci. U.S.A. 94:12963-12968(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GEK.
  7. "Mbt, a Drosophila PAK protein, combines with Cdc42 to regulate photoreceptor cell morphogenesis."
    Schneeberger D., Raabe T.
    Development 130:427-437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MBT, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-12.

Entry informationi

Entry nameiCDC42_DROME
AccessioniPrimary (citable) accession number: P40793
Secondary accession number(s): Q540W4
, Q9U9S3, Q9U9S4, Q9U9S5, Q9U9S6, Q9V465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.