P08646 (RAS1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-like protein 1
Short name=Dras1

Alternative name(s):
Dmras85D

Gene names

Name:	Ras85D
Synonyms:	Ras1
ORF Names:	CG9375

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	189 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	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 component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Traceable author statement PubMed 11735386. Source: FlyBase Malpighian tubule development Inferred from mutant phenotype PubMed 20432470. Source: FlyBase anterior/posterior axis specification, embryo Traceable author statement PubMed 10494038. Source: FlyBase border follicle cell migration Inferred from mutant phenotype PubMed 11141565. Source: FlyBase cell fate specification Traceable author statement PubMed 11606538. Source: FlyBase cell growth Traceable author statement PubMed 11735386. Source: FlyBase chorion-containing eggshell pattern formation Inferred from mutant phenotype PubMed 11606538PubMed 11959829. Source: FlyBase dorsal closure Traceable author statement PubMed 12147138. Source: FlyBase establishment or maintenance of apical/basal cell polarity Inferred from mutant phenotype PubMed 16908845. Source: FlyBase eye-antennal disc morphogenesis Inferred from mutant phenotype PubMed 16963016. Source: FlyBase gastrulation Inferred from mutant phenotype PubMed 14602078. Source: FlyBase heart development Non-traceable author statement PubMed 12027431. Source: FlyBase hemocyte migration Inferred from mutant phenotype PubMed 11955438. Source: FlyBase imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 12930782PubMed 16648592. Source: FlyBase instar larval development Inferred from mutant phenotype PubMed 16182526. Source: FlyBase negative regulation of apoptotic process Inferred from mutant phenotype PubMed 17055987PubMed 19840402. Source: FlyBase negative regulation of compound eye retinal cell programmed cell death Inferred from mutant phenotype PubMed 15511643. Source: FlyBase oocyte axis specification Inferred from mutant phenotype PubMed 16908845. Source: FlyBase peripheral nervous system development Inferred from mutant phenotype PubMed 12967983. Source: FlyBase positive regulation of cell growth Traceable author statement PubMed 11377964PubMed 13678953. Source: FlyBase positive regulation of cell proliferation Inferred from mutant phenotype PubMed 19141677PubMed 21176204. Source: FlyBase positive regulation of photoreceptor cell differentiation Inferred from mutant phenotype PubMed 16763554. Source: FlyBase primary branching, open tracheal system Traceable author statement PubMed 14570584. Source: FlyBase protein import into nucleus Inferred from genetic interaction PubMed 16763554. Source: FlyBase regulation of cell size Inferred from mutant phenotype PubMed 19840402. Source: FlyBase regulation of hemocyte differentiation Inferred from mutant phenotype PubMed 15381778. Source: FlyBase regulation of multicellular organism growth Inferred from mutant phenotype PubMed 16182526. Source: FlyBase sevenless signaling pathway Traceable author statement PubMed 10929403. Source: FlyBase small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro stem cell fate commitment Inferred from mutant phenotype PubMed 20463031. Source: FlyBase stem cell proliferation Inferred from mutant phenotype PubMed 20432470. Source: FlyBase torso signaling pathway Traceable author statement PubMed 10494038. Source: FlyBase tracheal outgrowth, open tracheal system Inferred from mutant phenotype PubMed 16326394. Source: FlyBase
Cellular_component	plasma membrane Inferred from direct assay Ref.8PubMed 20462449. Source: FlyBase
Molecular_function	GTP binding Non-traceable author statement. Source: UniProtKB GTPase activity Inferred from sequence or structural similarity PubMed 14579253. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 186	186	Ras-like protein 1		PRO_0000082665
	Propeptide	187 – 189	3	Removed in mature form Probable		PRO_0000281313
Regions
	Nucleotide binding	10 – 17	8	GTP By similarity
	Nucleotide binding	57 – 61	5	GTP By similarity
	Nucleotide binding	116 – 119	4	GTP By similarity
	Motif	32 – 40	9	Effector region By similarity
Amino acid modifications
	Modified residue	186	1	Cysteine methyl ester Probable
	Lipidation	186	1	S-geranylgeranyl cysteine Probable
Experimental info
	Sequence conflict	11	1	A → P in AAA28846. Ref.2
	Sequence conflict	44 – 45	2	VV → RF in AAA28846. Ref.2
	Sequence conflict	84	1	V → I in AAA28846. Ref.2
	Sequence conflict	102	1	R → H in AAA28846. Ref.2
	Sequence conflict	114	1	V → A in AAA28846. Ref.2
	Sequence conflict	182	1	R → C in AAA28846. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P08646 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 14236DCD65EACCD2	FASTA	189	21,594
	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

References

	« Hide 'large scale' referencesShow '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] [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]	"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] [Europe PMC] [Abstract] 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]	"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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	TVFF85. A29048. S35097.
RefSeq	NP_476699.1. NM_057351.5.
UniGene	Dm.4812.
3D structure databases
ProteinModelPortal	P08646.
SMR	P08646. Positions 1-165.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-23541N.
MINT	MINT-293375.
STRING	7227.FBpp0081600.
Proteomic databases
PaxDb	P08646.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082122; FBpp0081600; FBgn0003205.
GeneID	41140.
KEGG	dme:Dmel_CG9375.
Organism-specific databases
CTD	41140.
FlyBase	FBgn0003205. Ras85D.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00690000101785.
InParanoid	P08646.
KO	K07827.
OMA	MSKEGKK.
OrthoDB	EOG425491.
PhylomeDB	P08646.
Enzyme and pathway databases
SignaLink	P08646.
Gene expression databases
Bgee	P08646.
GermOnline	CG9375. Drosophila melanogaster.
Family and domain databases
InterPro	IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Ras85D. drosophila.
GenomeRNAi	41140.
NextBio	822376.

Entry information

Entry name

RAS1_DROME

Accession

Primary (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:	May 29, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project