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Protein

Ras-related protein Rac1

Gene

Rac1

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

Functioni

Involved in axon outgrowth and myoblast fusion. Plays a role in regulating dorsal closure during embryogenesis. Involved in integrin alpha-PS3/beta-nu-mediated phagocytosis of Gram-positive S.aureus by hemocytes.3 Publications

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 bundle assembly Source: FlyBase
  • actin filament organization Source: FlyBase
  • activation of protein kinase activity Source: FlyBase
  • adherens junction maintenance Source: FlyBase
  • axonal fasciculation Source: FlyBase
  • axon extension Source: FlyBase
  • axon guidance Source: FlyBase
  • axon midline choice point recognition Source: FlyBase
  • axonogenesis Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cell-cell junction organization Source: FlyBase
  • cell competition in a multicellular organism Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cell proliferation Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • dendrite development Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • determination of digestive tract left/right asymmetry Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • dorsal closure Source: UniProtKB
  • dorsal closure, amnioserosa morphology change Source: FlyBase
  • dorsal closure, elongation of leading edge cells Source: FlyBase
  • dorsal closure, spreading of leading edge cells Source: FlyBase
  • embryonic anterior midgut (ectodermal) morphogenesis Source: FlyBase
  • encapsulation of foreign target Source: FlyBase
  • establishment of ommatidial planar polarity Source: FlyBase
  • establishment of tissue polarity Source: FlyBase
  • germ-band shortening Source: FlyBase
  • glial cell migration Source: FlyBase
  • head involution Source: FlyBase
  • hemocyte development Source: FlyBase
  • hemocyte migration Source: FlyBase
  • imaginal disc-derived wing hair site selection Source: FlyBase
  • immune response-regulating cell surface receptor signaling pathway involved in phagocytosis Source: FlyBase
  • intracellular protein transport Source: InterPro
  • JNK cascade Source: FlyBase
  • lamellipodium assembly Source: FlyBase
  • melanotic encapsulation of foreign target Source: FlyBase
  • mesodermal cell migration Source: FlyBase
  • microtubule-based process Source: FlyBase
  • morphogenesis of larval imaginal disc epithelium Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • muscle attachment Source: FlyBase
  • muscle fiber development Source: FlyBase
  • myoblast fusion Source: FlyBase
  • myoblast proliferation Source: FlyBase
  • negative regulation of lamellipodium assembly Source: FlyBase
  • nephrocyte filtration Source: FlyBase
  • neuron projection development Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • nucleocytoplasmic transport Source: InterPro
  • open tracheal system development Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of axon extension Source: FlyBase
  • positive regulation of axon guidance Source: FlyBase
  • positive regulation of cell-matrix adhesion Source: FlyBase
  • positive regulation of filopodium assembly Source: FlyBase
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of wound healing Source: FlyBase
  • regulation of axonogenesis Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of dendrite morphogenesis Source: FlyBase
  • regulation of hemocyte differentiation Source: FlyBase
  • regulation of locomotor rhythm Source: FlyBase
  • regulation of synapse assembly Source: FlyBase
  • regulation of synapse organization Source: FlyBase
  • rhabdomere development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • sensory perception of touch Source: FlyBase
  • small GTPase mediated signal transduction Source: InterPro
  • tracheal outgrowth, open tracheal system Source: FlyBase
  • ventral cord development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Phagocytosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-1433557. Signaling by SCF-KIT.
R-DME-193648. NRAGE signals death through JNK.
R-DME-194840. Rho GTPase cycle.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-376172. DSCAM interactions.
R-DME-389359. CD28 dependent Vav1 pathway.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-3928664. Ephrin signaling.
R-DME-3928665. EPH-ephrin mediated repulsion of cells.
R-DME-4086400. PCP/CE pathway.
R-DME-416482. G alpha (12/13) signalling events.
R-DME-418885. DCC mediated attractive signaling.
R-DME-428540. Activation of Rac.
R-DME-428543. Inactivation of Cdc42 and Rac.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-445144. Signal transduction by L1.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5627123. RHO GTPases activate PAKs.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DME-5687128. MAPK6/MAPK4 signaling.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP40792.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rac1
Gene namesi
Name:Rac1
Synonyms:RacA
ORF Names:CG2248
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0010333. Rac1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosol Source: Reactome
  • extrinsic component of plasma membrane Source: FlyBase
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
  • ruffle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related protein Rac1PRO_0000198893Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000281244

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP40792.

Expressioni

Gene expression databases

BgeeiP40792.
ExpressionAtlasiP40792. differential.
GenevisibleiP40792. DM.

Interactioni

Subunit structurei

Interacts with Sra-1. Interacts (via REM 1 repeats) with Pkn (via N-terminus).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
chicP258433EBI-74845,EBI-156199
PakQ242133EBI-74845,EBI-74826

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi63689. 60 interactions.
IntActiP40792. 4 interactions.
STRINGi7227.FBpp0304252.

Structurei

3D structure databases

ProteinModelPortaliP40792.
SMRiP40792. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
InParanoidiP40792.
KOiK04392.
OMAiGKKCTMF.
OrthoDBiEOG764747.
PhylomeDBiP40792.

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.

P40792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDAKP
60 70 80 90 100
INLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVNPASF ENVRAKWYPE
110 120 130 140 150
VRHHCPSTPI ILVGTKLDLR DDKNTIEKLR DKKLAPITYP QGLAMAKEIG
160 170 180 190
AVKYLECSAL TQKGLKTVFD EAIRSVLCPV LQPKSKRKCA LL
Length:192
Mass (Da):21,354
Last modified:February 1, 1996 - v2
Checksum:iF910B54BDBD8AFA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351A → V in AAA62870 (PubMed:7958857).Curated
Sequence conflicti143 – 1464LAMA → SGHG in AAA67040 (PubMed:7835340).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI45715.
S51718.
S54295.
RefSeqiNP_001261247.1. NM_001274318.1.
NP_476950.1. NM_057602.4.
UniGeneiDm.4299.

Genome annotation databases

EnsemblMetazoaiFBtr0072730; FBpp0072614; FBgn0010333.
FBtr0331868; FBpp0304252; FBgn0010333.
GeneIDi38146.
KEGGidme:Dmel_CG2248.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI45715.
S51718.
S54295.
RefSeqiNP_001261247.1. NM_001274318.1.
NP_476950.1. NM_057602.4.
UniGeneiDm.4299.

3D structure databases

ProteinModelPortaliP40792.
SMRiP40792. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63689. 60 interactions.
IntActiP40792. 4 interactions.
STRINGi7227.FBpp0304252.

Proteomic databases

PaxDbiP40792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072730; FBpp0072614; FBgn0010333.
FBtr0331868; FBpp0304252; FBgn0010333.
GeneIDi38146.
KEGGidme:Dmel_CG2248.

Organism-specific databases

CTDi5879.
FlyBaseiFBgn0010333. Rac1.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
InParanoidiP40792.
KOiK04392.
OMAiGKKCTMF.
OrthoDBiEOG764747.
PhylomeDBiP40792.

Enzyme and pathway databases

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-1433557. Signaling by SCF-KIT.
R-DME-193648. NRAGE signals death through JNK.
R-DME-194840. Rho GTPase cycle.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-376172. DSCAM interactions.
R-DME-389359. CD28 dependent Vav1 pathway.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-3928664. Ephrin signaling.
R-DME-3928665. EPH-ephrin mediated repulsion of cells.
R-DME-4086400. PCP/CE pathway.
R-DME-416482. G alpha (12/13) signalling events.
R-DME-418885. DCC mediated attractive signaling.
R-DME-428540. Activation of Rac.
R-DME-428543. Inactivation of Cdc42 and Rac.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-445144. Signal transduction by L1.
R-DME-5218920. VEGFR2 mediated vascular permeability.
R-DME-5627123. RHO GTPases activate PAKs.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DME-5687128. MAPK6/MAPK4 signaling.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP40792.

Miscellaneous databases

ChiTaRSiRac1. fly.
GenomeRNAii38146.
PROiP40792.

Gene expression databases

BgeeiP40792.
ExpressionAtlasiP40792. differential.
GenevisibleiP40792. 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], 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] [Europe PMC] [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] [Europe PMC] [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.
    , 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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis."
    Lu Y., Settleman J.
    Genes Dev. 13:1168-1180(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN.
  8. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRA-1.
  9. "A rho-binding protein kinase C-like activity is required for the function of protein kinase N in Drosophila development."
    Betson M., Settleman J.
    Genetics 176:2201-2212(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKN.
  10. "Independent recognition of Staphylococcus aureus by two receptors for phagocytosis in Drosophila."
    Shiratsuchi A., Mori T., Sakurai K., Nagaosa K., Sekimizu K., Lee B.L., Nakanishi Y.
    J. Biol. Chem. 287:21663-21672(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRAC1_DROME
AccessioniPrimary (citable) accession number: P40792
Secondary accession number(s): Q9W0H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 163 of the entry and version 2 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.