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Protein

Ras-like protein 1

Gene

Ras85D

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

Functioni

Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells (PubMed:11290305). During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis (PubMed:19965758).By similarity2 Publications

Enzyme regulationi

Alternates 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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi116 – 1194GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: FlyBase
  • GTPase activity Source: FlyBase
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cell fate determination Source: FlyBase
  • cell fate specification Source: FlyBase
  • cell growth Source: FlyBase
  • cell proliferation Source: FlyBase
  • cellular response to starvation Source: FlyBase
  • chorion-containing eggshell pattern formation Source: FlyBase
  • compound eye development Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • dorsal closure Source: FlyBase
  • establishment or maintenance of apical/basal cell polarity Source: FlyBase
  • eye-antennal disc morphogenesis Source: FlyBase
  • G1/S transition of mitotic cell cycle Source: FlyBase
  • gastrulation Source: FlyBase
  • heart development Source: FlyBase
  • hemocyte migration Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • imaginal disc-derived wing vein morphogenesis Source: FlyBase
  • instar larval development Source: FlyBase
  • intestinal stem cell homeostasis Source: FlyBase
  • Malpighian tubule development Source: FlyBase
  • metamorphosis Source: FlyBase
  • negative regulation of apoptotic process Source: FlyBase
  • negative regulation of apoptotic signaling pathway Source: FlyBase
  • negative regulation of autophagy Source: FlyBase
  • negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • negative regulation of macroautophagy Source: FlyBase
  • oocyte axis specification Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • perineurial glial growth Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • photoreceptor cell morphogenesis Source: FlyBase
  • positive regulation of cell growth Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of cell size Source: FlyBase
  • positive regulation of MAPK cascade Source: FlyBase
  • positive regulation of photoreceptor cell differentiation Source: FlyBase
  • primary branching, open tracheal system Source: FlyBase
  • protein import into nucleus Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of cell growth Source: FlyBase
  • regulation of cell size Source: FlyBase
  • regulation of growth Source: FlyBase
  • regulation of hemocyte differentiation Source: FlyBase
  • regulation of multicellular organism growth Source: FlyBase
  • sevenless signaling pathway Source: FlyBase
  • small GTPase mediated signal transduction Source: InterPro
  • stem cell differentiation Source: FlyBase
  • stem cell fate commitment Source: FlyBase
  • stem cell proliferation Source: FlyBase
  • TORC1 signaling Source: FlyBase
  • torso signaling pathway Source: FlyBase
  • trachea development Source: FlyBase
  • tracheal outgrowth, open tracheal system Source: FlyBase
  • wing disc morphogenesis Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-1433557. Signaling by SCF-KIT.
R-DME-171007. p38MAPK events.
R-DME-179812. GRB2 events in EGFR signaling.
R-DME-180336. SHC1 events in EGFR signaling.
R-DME-210993. Tie2 Signaling.
R-DME-2179392. EGFR Transactivation by Gastrin.
R-DME-2424491. DAP12 signaling.
R-DME-2871796. FCERI mediated MAPK activation.
R-DME-375165. NCAM signaling for neurite out-growth.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-5218921. VEGFR2 mediated cell proliferation.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5654688. SHC-mediated cascade:FGFR1.
R-DME-5654693. FRS-mediated FGFR1 signaling.
R-DME-5654699. SHC-mediated cascade:FGFR2.
R-DME-5654700. FRS-mediated FGFR2 signaling.
R-DME-5654704. SHC-mediated cascade:FGFR3.
R-DME-5654706. FRS-mediated FGFR3 signaling.
R-DME-5654712. FRS-mediated FGFR4 signaling.
R-DME-5654719. SHC-mediated cascade:FGFR4.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5673000. RAF activation.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP08646.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-like protein 1
Short name:
Dras1
Alternative name(s):
Dmras85D
Gene namesi
Name:Ras85D
Synonyms:Ras1
ORF Names:CG9375
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003205. Ras85D.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
  • membrane Source: UniProtKB
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown in the prothoracic gland (PG) delays the onset of pupariation by prolonging the L3 larval stage.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121G → V: Rough eyes characterized by the presence of additional R7 photoreceptor cells. Normal survival of postmitotic ommatidial cells but differentiation into photoreceptor cells is limited to R8 cells. Less severe Rough eye phenotype; when associated with E-38. Normal eyes; when associated with C-40. 1 Publication
Mutagenesisi38 – 381D → E: Mild rough eye phenotype; when associated with V-12. 1 Publication
Mutagenesisi40 – 401Y → C: Impaired cell growth, survival of postmitotic ommatidial cells and differentiation into R8 photoreceptors. Normal eye morphology; when associated with V-12. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186Ras-like protein 1PRO_0000082665Add
BLAST
Propeptidei187 – 1893Removed in mature formCuratedPRO_0000281313

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Cysteine methyl esterCurated
Lipidationi186 – 1861S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP08646.

Expressioni

Tissue specificityi

Expressed in the posterior termini of the embryo, restricted mainly to the embryonic central nervous system, and in the eye imaginal disk.1 Publication

Gene expression databases

BgeeiP08646.
GenevisibleiP08646. DM.

Interactioni

Protein-protein interaction databases

BioGridi66301. 123 interactions.
DIPiDIP-23541N.
MINTiMINT-293375.
STRINGi7227.FBpp0081600.

Structurei

3D structure databases

ProteinModelPortaliP08646.
SMRiP08646. Positions 1-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
InParanoidiP08646.
KOiK07827.
OMAiVDMNQAR.
OrthoDBiEOG7QVM41.
PhylomeDBiP08646.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET
60 70 80 90 100
CLLDILDTAG QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI
110 120 130 140 150
KRVKDAEEVP MVLVGNKCDL ASWNVNNEQA REVAKQYGIP YIETSAKTRM
160 170 180
GVDDAFYTLV REIRKDKDNK GRRGRKMNKP NRRFKCKML
Length:189
Mass (Da):21,594
Last modified:July 1, 1989 - v2
Checksum:i14236DCD65EACCD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → P in AAA28846 (PubMed:6430564).Curated
Sequence conflicti44 – 452VV → RF in AAA28846 (PubMed:6430564).Curated
Sequence conflicti84 – 841V → I in AAA28846 (PubMed:6430564).Curated
Sequence conflicti102 – 1021R → H in AAA28846 (PubMed:6430564).Curated
Sequence conflicti114 – 1141V → A in AAA28846 (PubMed:6430564).Curated
Sequence conflicti182 – 1821R → C in AAA28846 (PubMed:6430564).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA29048. TVFF85.
S35097.
RefSeqiNP_476699.1. NM_057351.5.
UniGeneiDm.4812.

Genome annotation databases

EnsemblMetazoaiFBtr0082122; FBpp0081600; FBgn0003205.
GeneIDi41140.
KEGGidme:Dmel_CG9375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA29048. TVFF85.
S35097.
RefSeqiNP_476699.1. NM_057351.5.
UniGeneiDm.4812.

3D structure databases

ProteinModelPortaliP08646.
SMRiP08646. Positions 1-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66301. 123 interactions.
DIPiDIP-23541N.
MINTiMINT-293375.
STRINGi7227.FBpp0081600.

Proteomic databases

PaxDbiP08646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082122; FBpp0081600; FBgn0003205.
GeneIDi41140.
KEGGidme:Dmel_CG9375.

Organism-specific databases

CTDi41140.
FlyBaseiFBgn0003205. Ras85D.

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
InParanoidiP08646.
KOiK07827.
OMAiVDMNQAR.
OrthoDBiEOG7QVM41.
PhylomeDBiP08646.

Enzyme and pathway databases

ReactomeiR-DME-1433557. Signaling by SCF-KIT.
R-DME-171007. p38MAPK events.
R-DME-179812. GRB2 events in EGFR signaling.
R-DME-180336. SHC1 events in EGFR signaling.
R-DME-210993. Tie2 Signaling.
R-DME-2179392. EGFR Transactivation by Gastrin.
R-DME-2424491. DAP12 signaling.
R-DME-2871796. FCERI mediated MAPK activation.
R-DME-375165. NCAM signaling for neurite out-growth.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-5218921. VEGFR2 mediated cell proliferation.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5654688. SHC-mediated cascade:FGFR1.
R-DME-5654693. FRS-mediated FGFR1 signaling.
R-DME-5654699. SHC-mediated cascade:FGFR2.
R-DME-5654700. FRS-mediated FGFR2 signaling.
R-DME-5654704. SHC-mediated cascade:FGFR3.
R-DME-5654706. FRS-mediated FGFR3 signaling.
R-DME-5654712. FRS-mediated FGFR4 signaling.
R-DME-5654719. SHC-mediated cascade:FGFR4.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5673000. RAF activation.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP08646.

Miscellaneous databases

ChiTaRSiRas85D. fly.
GenomeRNAii41140.
PROiP08646.

Gene expression databases

BgeeiP08646.
GenevisibleiP08646. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and genomic structure of ras homologues Dmras85D and Dmras64B of Drosophila melanogaster."
    Brock H.W.
    Gene 51:129-137(1987) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
    , 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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, TISSUE SPECIFICITY.
    Strain: Canton-S.
  8. "Ras controls growth, survival and differentiation in the Drosophila eye by different thresholds of MAP kinase activity."
    Halfar K., Rommel C., Stocker H., Hafen E.
    Development 128:1687-1696(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-12; ASP-38 AND TYR-40.
  9. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION.
  10. "The insect neuropeptide PTTH activates receptor tyrosine kinase torso to initiate metamorphosis."
    Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.
    Science 326:1403-1405(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRAS1_DROME
AccessioniPrimary (citable) accession number: P08646
Secondary accession number(s): Q9V448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 168 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.