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Reviewed, UniProtKB/Swiss-Prot P08646 (RAS1_DROME)

Last modified June 16, 2009. Version 101. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ras-like protein 1
      Short name=Dras1
Alternative name(s):
    Dmras85D
Gene names
Name: Ras85D
Synonyms: Ras1
ORF Names: CG9375
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May mediate a signal that determines the fate of photoreceptor cells in the developing compound eye. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.

Enzyme regulation

Alternate between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Loss of prenylation causes protein location to the cytoplasm. Ref.8

Tissue specificity

Expressed in the posterior termini of the embryo, restricted mainly to the embryonic central nervous system, and in the eye imaginal disk. Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processG1/S transition of mitotic cell cycle

Traceable author statement. Source: FlyBase

anti-apoptosis

Non-traceable author statement. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype. Source: FlyBase

cell fate specification

Traceable author statement. Source: FlyBase

cell growth

Traceable author statement. Source: FlyBase

cell proliferation

Inferred from mutant phenotype. Source: FlyBase

chorion-containing eggshell pattern formation

Inferred from mutant phenotype. Source: FlyBase

determination of anterior/posterior axis, embryo

Traceable author statement. Source: FlyBase

dorsal closure

Traceable author statement. Source: FlyBase

establishment or maintenance of apical/basal cell polarity

Inferred from mutant phenotype. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from mutant phenotype. Source: FlyBase

gastrulation

Inferred from mutant phenotype. Source: FlyBase

heart development

Non-traceable author statement. Source: FlyBase

hemocyte migration

Inferred from mutant phenotype. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype. Source: FlyBase

instar larval development

Inferred from mutant phenotype. Source: FlyBase

negative regulation of compound eye retinal cell programmed cell death

Inferred from mutant phenotype. Source: FlyBase

oocyte axis specification

Inferred from mutant phenotype. Source: FlyBase

peripheral nervous system development

Inferred from mutant phenotype. Source: FlyBase

positive regulation of cell growth

Traceable author statement. Source: FlyBase

positive regulation of photoreceptor cell differentiation

Inferred from mutant phenotype. Source: FlyBase

primary branching, open tracheal system

Traceable author statement. Source: FlyBase

protein import into nucleus

Inferred from genetic interaction. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype. Source: FlyBase

regulation of multicellular organism growth

Inferred from mutant phenotype. Source: FlyBase

sevenless signaling pathway

Traceable author statement. Source: FlyBase

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

torso signaling pathway

Traceable author statement. Source: FlyBase

tracheal outgrowth, open tracheal system

Inferred from mutant phenotype. Source: FlyBase

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

plasma membrane Ref.8

Inferred from direct assay. Source: FlyBase

   Molecular functionGTP binding

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 186186Ras-like protein 1
PRO_0000082665
Propeptide187 – 1893Removed in mature form Probable
PRO_0000281313

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding116 – 1194GTP By similarity
Motif32 – 409Effector region By similarity

Amino acid modifications

Modified residue1861Cysteine methyl ester Probable
Lipidation1861S-geranylgeranyl cysteine Probable

Experimental info

Sequence conflict111A → P in AAA28846. Ref.2
Sequence conflict44 – 452VV → RF in AAA28846. Ref.2
Sequence conflict841V → I in AAA28846. Ref.2
Sequence conflict1021R → H in AAA28846. Ref.2
Sequence conflict1141V → A in AAA28846. Ref.2
Sequence conflict1821R → C in AAA28846. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08646-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 14236DCD65EACCD2

FASTA18921,594
        10         20         30         40         50         60 
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG 

        70         80         90        100        110        120 
QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL 

       130        140        150        160        170        180 
ASWNVNNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRRGRKMNKP 


NRRFKCKML 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and genomic structure of ras homologues Dmras85D and Dmras64B of Drosophila melanogaster."
Brock H.W.
Gene 51:129-137(1987) [PubMed: 3110012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Drosophila ras oncogenes: structure and nucleotide sequence."
Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.
Cell 37:1027-1033(1984) [PubMed: 6430564] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Absence of protein polymorphism in the Ras genes of Drosophila melanogaster."
Gasperini R., Gibson G.
J. Mol. Evol. 49:583-590(1999) [PubMed: 10552039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: W13.
[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]"Differential expression during embryogenesis of three genes clustered in the Ras1 region of Drosophila melanogaster."
Ezer S.T., Sahar D., Salzberg A., Lev Z.
Dev. Dyn. 201:179-190(1994) [PubMed: 7873789] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, TISSUE SPECIFICITY.
Strain: Canton-S.
[8]"Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein."
Day J.P., Cleghon V., Houslay M.D., Davies S.-A.
Biochem. J. 414:363-374(2008) [PubMed: 18503409] [Abstract]
Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

M16429, M16123, M16428 Genomic DNA. Translation: AAA28847.1.
K01960 mRNA. Translation: AAA28846.1.
AF186648 Genomic DNA. Translation: AAF15514.1.
AE014297 Genomic DNA. Translation: AAF54388.1.
AY089541 mRNA. Translation: AAL90279.1.
AY094888 mRNA. Translation: AAM11241.1.
X73219 Genomic DNA. Translation: CAA51689.1.
PIRTVFF85. A29048.
S35097.
RefSeqNP_476699.1.
UniGeneDm.4812

3D structure databases

HSSPHSSP built from PDB template 1IOZ based on UniProtKB P01112.
SMRP08646. Positions 1-165.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:23541N.
IntActP08646. 14 interactions.

Genome annotation databases

EnsemblFBgn0003205. Drosophila melanogaster. [Contig view]
GeneID41140.
KEGGdme:Dmel_CG9375.
NMPDRfig|7227.3.peg.11891.

Organism-specific databases

FlyBaseFBgn0003205. Ras85D.

Phylogenomic databases

HOGENOMP08646.
OMAP08646. SFEDIGT.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-010737-MON.

Gene expression databases

ArrayExpressP08646.
GermOnlineCG9375. Drosophila melanogaster.

Family and domain databases

InterProIPR003577. GTPase_Ras.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR015592. Ras_Ras_related.
IPR005225. Small_GTP_bd.
[Graphical view]
PANTHERPTHR11708:SF125. Ras_Ras_related. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio822376.

Entry information

Entry nameRAS1_DROME
AccessionPrimary (citable) accession number: P08646
Secondary accession number(s): Q9V448
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 1, 1989
Last modified: June 16, 2009
This is version 101 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents