RAS2_DROME
ID RAS2_DROME Reviewed; 192 AA.
AC P04388; Q9VZH7;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Ras-like protein 2;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=Ras64B; Synonyms=ras2; ORFNames=CG1167;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3921827; DOI=10.1128/mcb.5.4.885-889.1985;
RA Mozer B., Marlor R., Parkhusrt S., Corces V.G.;
RT "Characterization and developmental expression of a Drosophila ras
RT oncogene.";
RL Mol. Cell. Biol. 5:885-889(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3110012; DOI=10.1016/0378-1119(87)90301-5;
RA Brock H.W.;
RT "Sequence and genomic structure of ras homologues Dmras85D and Dmras64B of
RT Drosophila melanogaster.";
RL Gene 51:129-137(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Iso-1 / Kennison;
RX PubMed=7789770; DOI=10.1093/genetics/139.4.1701;
RA Harrison S.D., Solomon N., Rubin G.M.;
RT "A genetic analysis of the 63E-64A genomic region of Drosophila
RT melanogaster: identification of mutations in a replication factor C
RT subunit.";
RL Genetics 139:1701-1709(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-192.
RX PubMed=6430564; DOI=10.1016/0092-8674(84)90437-9;
RA Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.;
RT "The Drosophila ras oncogenes: structure and nucleotide sequence.";
RL Cell 37:1027-1033(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-192.
RC STRAIN=A1;
RX PubMed=10552039; DOI=10.1007/pl00006579;
RA Gasperini R., Gibson G.;
RT "Absence of protein polymorphism in the Ras genes of Drosophila
RT melanogaster.";
RL J. Mol. Evol. 49:583-590(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18 AND 44-64, SPLICE SITES, AND
RP MUTAGENESIS OF GLY-14.
RX PubMed=2838380; DOI=10.1101/gad.2.5.567;
RA Bishop J.G. III, Corces V.G.;
RT "Expression of an activated ras gene causes developmental abnormalities in
RT transgenic Drosophila melanogaster.";
RL Genes Dev. 2:567-577(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=3412773;
RA Cohen N., Salzberg A., Lev Z.;
RT "A bidirectional promoter is regulating the Drosophila ras2 gene.";
RL Oncogene 3:137-142(1988).
RN [11]
RP CHARACTERIZATION.
RX PubMed=8404533; DOI=10.1242/dev.117.4.1309;
RA Salzberg A., Cohen N., Halachmi N., Kimchie Z., Lev Z.;
RT "The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast Ras-
RT like gene and a suppressor of its loss-of-function phenotype.";
RL Development 117:1309-1319(1993).
RN [12]
RP INTERACTION WITH HZG.
RX PubMed=31491385; DOI=10.1016/j.cell.2019.08.019;
RA Nil Z., Hervas R., Gerbich T., Leal P., Yu Z., Saraf A., Sardiu M.,
RA Lange J.J., Yi K., Unruh J., Slaughter B., Si K.;
RT "Amyloid-like Assembly Activates a Phosphatase in the Developing Drosophila
RT Embryo.";
RL Cell 178:1403-1420.E21(2019).
RN [13]
RP PALMITOYLATION AT CYS-46; CYS-120 AND CYS-147, AND MUTAGENESIS OF CYS-46;
RP CYS-120 AND CYS-147.
RX PubMed=30735487; DOI=10.1371/journal.pone.0198149;
RA Strassburger K., Kang E., Teleman A.A.;
RT "Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth
RT and viability.";
RL PLoS ONE 14:e0198149-e0198149(2019).
CC -!- FUNCTION: May be involved in endocytic processes and/or other transport
CC pathways mediated by vesicle trafficking. May interact functionally
CC with ROP protein. Ras proteins bind GDP/GTP and possess intrinsic
CC GTPase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Interacts with hzg. {ECO:0000269|PubMed:31491385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: A uniform expression is seen in unfertilized eggs,
CC embryos, larvae, pupae and adult flies. Expression during embryogenesis
CC is restricted to the CNS and the Garland cells, a small group of
CC nephrocytes that takes up waste materials from the hemolymph by
CC endocytosis. In post-embryonic stages, expression is seen in the larval
CC salivary glands and the CNS, and in the adult CNS and reproductive
CC systems.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M10804; AAA99202.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M10759; AAA99202.1; JOINED; Genomic_DNA.
DR EMBL; M10803; AAA99202.1; JOINED; Genomic_DNA.
DR EMBL; M16431; AAA28849.1; -; Genomic_DNA.
DR EMBL; M16124; AAA28849.1; JOINED; Genomic_DNA.
DR EMBL; M16430; AAA28849.1; JOINED; Genomic_DNA.
DR EMBL; U15967; AAB60243.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47845.2; -; Genomic_DNA.
DR EMBL; AY119135; AAM50995.1; -; mRNA.
DR EMBL; K01962; AAA28848.1; ALT_SEQ; Genomic_DNA.
DR EMBL; K01961; AAA28848.1; JOINED; Genomic_DNA.
DR EMBL; AF186651; AAF15517.1; -; Genomic_DNA.
DR EMBL; X12559; CAA31072.1; -; Genomic_DNA.
DR EMBL; X12558; CAA31071.1; ALT_INIT; Genomic_DNA.
DR EMBL; X07255; CAA30242.1; -; Genomic_DNA.
DR PIR; A01370; TVFFR.
DR PIR; S55022; S55022.
DR RefSeq; NP_523917.2; NM_079193.4.
DR AlphaFoldDB; P04388; -.
DR SMR; P04388; -.
DR BioGRID; 63974; 22.
DR STRING; 7227.FBpp0073068; -.
DR SwissPalm; P04388; -.
DR PaxDb; P04388; -.
DR PRIDE; P04388; -.
DR EnsemblMetazoa; FBtr0073212; FBpp0073068; FBgn0003206.
DR GeneID; 38494; -.
DR KEGG; dme:Dmel_CG1167; -.
DR CTD; 38494; -.
DR FlyBase; FBgn0003206; Ras64B.
DR VEuPathDB; VectorBase:FBgn0003206; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160972; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P04388; -.
DR OMA; QCVIDDI; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P04388; -.
DR BioGRID-ORCS; 38494; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38494; -.
DR PRO; PR:P04388; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003206; Expressed in crop (Drosophila) and 28 other tissues.
DR Genevisible; P04388; DM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Ras-like protein 2"
FT /id="PRO_0000082668"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281316"
FT MOTIF 34..42
FT /note="Effector region"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:30735487"
FT LIPID 120
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:30735487"
FT LIPID 147
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:30735487"
FT LIPID 189
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 14
FT /note="G->V: Causes developmental abnormalities."
FT /evidence="ECO:0000269|PubMed:2838380"
FT MUTAGEN 46
FT /note="C->A: Reduces protein stability and palmitoylation.
FT Loss of palmitoylation; when associated with A-120 and A-
FT 147."
FT /evidence="ECO:0000269|PubMed:30735487"
FT MUTAGEN 120
FT /note="C->A: Reduces palmitoylation. Loss of
FT palmitoylation; when associated with A-120 and A-147."
FT /evidence="ECO:0000269|PubMed:30735487"
FT MUTAGEN 147
FT /note="C->A: Reduces palmitoylation. Loss of
FT palmitoylation; when associated with A-120 and A-147."
FT /evidence="ECO:0000269|PubMed:30735487"
FT CONFLICT 28..29
FT /note="SY -> VS (in Ref. 10; CAA30242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 22236 MW; 3F58A3A33E8FDEBC CRC64;
MQMQTYKLVV VGGGGVGKSA ITIQFIQSYF VTDYDPTIED SYTKQCNIDD VPAKLDILDT
AGQEEFSAMR EQYMRSGEGF LLVFALNDHS SFDEIPKFQR QILRVKDRDE FPMLMVGNKC
DLKHQQQVSL EEAQNTSRNL MIPYIECSAK LRVNVDQAFH ELVRIVRKFQ IAERPFIEQD
YKKKGKRKCC LM
