Reviewed, UniProtKB/Swiss-Prot P40793 (CDC42_DROME)

Names and origin

Protein names

Recommended name:
    Cdc42 homolog

Gene names

Name:	Cdc42
ORF Names:	CG12530

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Regulates mbt kinase activity and is also required to recruit mbt to adheren junctions. Together with mbt, regulates photoreceptor cell morphogenesis. Ref.7
Subunit structure	The GTP-bound but not the GDP-bound form interacts with mbt and gek. Ref.7 Ref.6
Subcellular location	Cell junction › adherens junction. Cell membrane; Lipid-anchor. Note: Adherens junctions of developing photoreceptor cells. Ref.7
Sequence similarities	Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Developmental protein
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	JNK cascade Traceable author statement. Source: FlyBase actin filament polymerization Inferred from mutant phenotype. Source: FlyBase axon guidance Inferred from mutant phenotype. Source: FlyBase cell projection assembly Inferred from mutant phenotype. Source: FlyBase cellularization Traceable author statement. Source: FlyBase cortical actin cytoskeleton organization Inferred from mutant phenotype. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype. Source: FlyBase dorsal appendage formation Inferred from mutant phenotype. Source: FlyBase hemocyte migration Inferred from mutant phenotype. Source: FlyBase imaginal disc-derived wing hair outgrowth Inferred from mutant phenotype. Source: FlyBase maintenance of cell polarity Inferred from mutant phenotype. Source: FlyBase maintenance of protein location Ref.7 Inferred from mutant phenotype. Source: UniProtKB phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase positive regulation of protein kinase activity Ref.7 Inferred from mutant phenotype. Source: UniProtKB regulation of axonogenesis Inferred from genetic interaction. Source: FlyBase regulation of cell shape Inferred from mutant phenotype. Source: FlyBase small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro suture of dorsal opening Traceable author statement. Source: FlyBase transforming growth factor beta receptor signaling pathway Traceable author statement. Source: FlyBase wound healing Inferred from mutant phenotype. Source: FlyBase
Cellular component	adherens junction Ref.7 Inferred from direct assay. Source: UniProtKB intracellular Inferred from electronic annotation. Source: InterPro rhabdomere Inferred from mutant phenotype. Source: FlyBase
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: FlyBase protein binding Ref.6 Ref.7 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mbt	Q9VXE5	2	EBI-114324,EBI-75994

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 188	188	Cdc42 homolog		PRO_0000198958
	Propeptide	189 – 191	3	Removed in mature form By similarity		PRO_0000281288
Regions
	Nucleotide binding	10 – 17	8	GTP By similarity
	Nucleotide binding	57 – 61	5	GTP By similarity
	Nucleotide binding	115 – 118	4	GTP By similarity
	Motif	32 – 40	9	Effector region Potential
Amino acid modifications
	Modified residue	188	1	Cysteine methyl ester By similarity
	Lipidation	188	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Mutagenesis	12	1	G → V: Enhances interaction with mbt. Coexpression with mbt slightly reduced the substrate phosphorylation ability of mbt. Ref.7
	Sequence conflict	10	1	G → D in AAD43788. Ref.2
	Sequence conflict	65	1	D → N in AAD43792. Ref.2
	Sequence conflict	83	1	S → L in AAD43793. Ref.2
	Sequence conflict	114	1	G → D in AAD43790. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P40793-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 0AB96574ADC8E0E3	FASTA	191	21,403
	10 20 30 40 50 60 MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG 70 80 90 100 110 120 QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCQKTPF LLVGTQIDLR 130 140 150 160 170 180 DENSTLEKLA KNKQKPITME QGEKLAKELK AVKYVECSAL TQKGLKNVFD EAILAALEPP 190 EPTKKRKCKF L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7958857] [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: 10772800] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] 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: 9371783] [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: 12490550] [Abstract] Cited for: FUNCTION, INTERACTION WITH MBT, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. AE014298 Genomic DNA. Translation: AAN09512.1. AY119570 mRNA. Translation: AAM50224.1.
PIR	I45716.
RefSeq	NP_523414.1. NP_728290.1.
UniGene	Dm.2867
3D structure databases
HSSP	HSSP built from PDB template 1AM4 based on UniProtKB P21181.
SMR	P40793. Positions 1-191.
ModBase	Search...
Protein-protein interaction databases
IntAct	P40793. 4 interactions.
Proteomic databases
PRIDE	P40793.
Genome annotation databases
Ensembl	FBgn0010341. Drosophila melanogaster. [Contig view]
GeneID	32981.
KEGG	dme:Dmel_CG12530.
Organism-specific databases
FlyBase	FBgn0010341. Cdc42.
Phylogenomic databases
HOGENOM	P40793.
OMA	P40793. EITHHCQ.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-002664-MON. DMEL-XXX-02:DMEL-XXX-02-002665-MON.
Gene expression databases
ArrayExpress	P40793.
GermOnline	CG12530. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003578. GTPase_Rho. IPR013753. Ras. IPR001806. Ras_GTPase. IPR005225. Small_GTP_bd. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	781350.

Entry information

Entry name

CDC42_DROME

Accession

Primary (citable) accession number: P40793
Secondary accession number(s): Q540W4 , Q9U9S3, Q9U9S4, Q9U9S5, Q9U9S6, Q9V465

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project