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Reviewed, UniProtKB/Swiss-Prot P40792 (RAC1_DROME)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ras-related protein Rac1
Gene names
Name: Rac1
Synonyms: RacA
ORF Names: CG2248
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in axon outgrowth and myoblast fusion. Ref.1

Subunit structure

Interacts with Sra-1. Ref.7

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processJNK cascade

Inferred from mutant phenotype. Source: FlyBase

actin cytoskeleton organization

Inferred from mutant phenotype. Source: FlyBase

adherens junction maintenance

Inferred from mutant phenotype. Source: FlyBase

axon extension

Inferred from mutant phenotype. Source: FlyBase

axon guidance Ref.7

Inferred from mutant phenotype. Source: FlyBase

axonal fasciculation

Inferred from mutant phenotype. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype. Source: FlyBase

cell competition in a multicellular organism

Inferred from mutant phenotype. Source: FlyBase

dendrite morphogenesis

Traceable author statement. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype. Source: FlyBase

dorsal closure, amnioserosa morphology change

Inferred from mutant phenotype. Source: FlyBase

dorsal closure, elongation of leading edge cells

Inferred from mutant phenotype. Source: FlyBase

establishment of ommatidial polarity

Non-traceable author statement. Source: FlyBase

germ-band shortening

Inferred from mutant phenotype. Source: FlyBase

glial cell migration

Inferred from mutant phenotype. Source: FlyBase

head involution

Inferred from mutant phenotype. Source: FlyBase

hemocyte development

Inferred from mutant phenotype. Source: FlyBase

hemocyte migration

Inferred from mutant phenotype. Source: FlyBase

imaginal disc-derived wing hair site selection

Inferred from mutant phenotype. Source: FlyBase

lamellipodium assembly

Inferred from mutant phenotype. Source: FlyBase

microtubule-based process

Non-traceable author statement. Source: FlyBase

morphogenesis of larval imaginal disc epithelium

Traceable author statement. Source: FlyBase

myoblast fusion

Inferred from mutant phenotype. Source: FlyBase

myoblast proliferation

Inferred from mutant phenotype. Source: FlyBase

peripheral nervous system development

Inferred from mutant phenotype. Source: FlyBase

phagocytosis triggered by activation of immune response cell surface activating receptor

Inferred from direct assay. Source: FlyBase

phagocytosis, engulfment

Inferred from mutant phenotype. Source: FlyBase

regulation of axonogenesis

Inferred from genetic interaction. Source: FlyBase

regulation of dendrite morphogenesis

Inferred from genetic interaction. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype. Source: FlyBase

regulation of synapse organization Ref.7

Inferred from genetic interaction. Source: FlyBase

rhabdomere development

Inferred from genetic interaction. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype. Source: FlyBase

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

tracheal outgrowth, open tracheal system

Inferred from genetic interaction. Source: FlyBase

ventral cord development

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

rhabdomere

Inferred from direct assay. Source: FlyBase

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement. Source: FlyBase

protein binding Ref.7

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PakQ242132EBI-74845,EBI-74826
Rac2P485541EBI-74845,EBI-74869

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Ras-related protein Rac1
PRO_0000198893
Propeptide190 – 1923Removed in mature form By similarity
PRO_0000281244

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue1891Cysteine methyl ester By similarity
Lipidation1891S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict1351A → V in AAA62870. Ref.1
Sequence conflict143 – 1464LAMA → SGHG in AAA67040. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40792-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: F910B54BDBD8AFA3

FASTA19221,354
        10         20         30         40         50         60 
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP INLGLWDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWYPE VRHHCPSTPI ILVGTKLDLR 

       130        140        150        160        170        180 
DDKNTIEKLR DKKLAPITYP QGLAMAKEIG AVKYLECSAL TQKGLKTVFD EAIRSVLCPV 

       190 
LQPKSKRKCA LL 

« Hide

References

« Hide '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], FUNCTION.
Strain: Oregon-R.
[2]"Characterization of rho GTPase family homologues in Drosophila melanogaster: overexpressing Rho1 in retinal cells causes a late developmental defect."
Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., Settleman J.
EMBO J. 14:292-302(1995) [PubMed: 7835340] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"A dominant inhibitory version of the small GTP-binding protein Rac disrupts cytoskeletal structures and inhibits developmental cell shape changes in Drosophila."
Harden N., Loh H., Chia W., Lim L.
Development 121:903-914(1995) [PubMed: 7720592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Canton-S.
[4]"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. expand/collapse author list , 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.
[5]"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. expand/collapse author list , 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.
[6]"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: Embryo.
[7]"CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the Rac1 GTPase pathway to the fragile X protein."
Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L., Giangrande A.
Neuron 38:887-898(2003) [PubMed: 12818175] [Abstract]
Cited for: INTERACTION WITH SRA-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

U11823 mRNA. Translation: AAA62870.1.
L38309 mRNA. Translation: AAA67040.1.
Z35642 mRNA. Translation: CAA84709.1.
AE014296 Genomic DNA. Translation: AAF47469.1.
AY060408 mRNA. Translation: AAL25447.1.
PIRI45715.
S51718.
S54295.
RefSeqNP_476950.1.
UniGeneDm.4299

3D structure databases

HSSPHSSP built from PDB template 1G4U based on UniProtKB P15154.
SMRP40792. Positions 1-177.
ModBaseSearch...

Protein-protein interaction databases

IntActP40792. 34 interactions.

Genome annotation databases

EnsemblFBgn0010333. Drosophila melanogaster. [Contig view]
GeneID38146.
KEGGdme:Dmel_CG2248.
NMPDRfig|7227.3.peg.7516.

Organism-specific databases

FlyBaseFBgn0010333. Rac1.

Phylogenomic databases

HOGENOMP40792.
OMAP40792. TQVGVKE.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-014604-MON.

Gene expression databases

ArrayExpressP40792.
GermOnlineCG2248. Drosophila melanogaster.

Family and domain databases

InterProIPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio807185.

Entry information

Entry nameRAC1_DROME
AccessionPrimary (citable) accession number: P40792
Secondary accession number(s): Q9W0H7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents