RAS1_YEAST
ID RAS1_YEAST Reviewed; 309 AA.
AC P01119; D6W2G2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ras-like protein 1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=RAS1; OrderedLocusNames=YOR101W; ORFNames=YOR3205W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6365329; DOI=10.1016/0092-8674(84)90340-4;
RA Powers S., Kataoka T., Fasano O., Goldfarb M., Strathern J., Broach J.,
RA Wigler M.;
RT "Genes in S. cerevisiae encoding proteins with domains homologous to the
RT mammalian ras proteins.";
RL Cell 36:607-612(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6328429; DOI=10.1093/nar/12.8.3611;
RA Dhar R., Nieto A., Koller R., DeFeo-Jones D., Scolnick E.M.;
RT "Nucleotide sequence of two rasH related-genes isolated from the yeast
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 12:3611-3618(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 245-309.
RX PubMed=7593165; DOI=10.1083/jcb.131.2.371;
RA Silberstein S., Collins P.G., Kelleher D.J., Gilmore R.;
RT "The essential OST2 gene encodes the 16-kD subunit of the yeast
RT oligosaccharyltransferase, a highly conserved protein expressed in diverse
RT eukaryotic organisms.";
RL J. Cell Biol. 131:371-383(1995).
RN [7]
RP PALMITOYLATION AT CYS-305.
RX PubMed=3513173; DOI=10.1073/pnas.83.5.1266;
RA Fujiyama A., Tamanoi F.;
RT "Processing and fatty acid acylation of RAS1 and RAS2 proteins in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1266-1270(1986).
RN [8]
RP METHYLATION AT CYS-306 BY STE14.
RX PubMed=2050108; DOI=10.1002/j.1460-2075.1991.tb07694.x;
RA Hrycyna C.A., Sapperstein S.K., Clarke S., Michaelis S.;
RT "The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that
RT mediates C-terminal methylation of a-factor and RAS proteins.";
RL EMBO J. 10:1699-1709(1991).
RN [9]
RP ISOPRENYLATION AT CYS-306 BY RAM1-RAM2.
RX PubMed=1763050; DOI=10.1073/pnas.88.24.11373;
RA He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.;
RT "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide
RT components of the farnesyltransferase that prenylates a-factor and Ras
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991).
RN [10]
RP PROTEOLYTIC PROCESSING BY RCE1.
RX PubMed=9065405; DOI=10.1126/science.275.5307.1796;
RA Boyartchuk V.L., Ashby M.N., Rine J.;
RT "Modulation of Ras and a-factor function by carboxyl-terminal
RT proteolysis.";
RL Science 275:1796-1800(1997).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The S.cerevisiae Ras proteins modulate the activity of the
CC adenylate cyclase catalytic subunit and therefore affect the
CC biosynthesis of cyclic-AMP.
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 guanine nucleotide-
CC exchange factor (GEF) CDC25 and inactivated by GTPase-activating
CC proteins (GAPs) IRA1 and IRA2.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC -!- PTM: Farnesylated by RAM1-RAM2, which is required for targeting RAS1 to
CC the cytoplasmic site of the endoplasmic reticulum, where proteolytic
CC processing of the C-terminus by RCE1 and methylation of the resulting
CC carboxyl group by STE14 occurs. {ECO:0000269|PubMed:2050108,
CC ECO:0000269|PubMed:9065405}.
CC -!- PTM: Palmitoylated by the ERF2-SHR5 complex, which is required for
CC proper plasma membrane localization of RAS1. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; K01970; AAA34958.1; -; Genomic_DNA.
DR EMBL; X00527; CAA25206.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64023.1; -; Genomic_DNA.
DR EMBL; Z75009; CAA99298.1; -; Genomic_DNA.
DR EMBL; U32307; AAC49087.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10878.1; -; Genomic_DNA.
DR PIR; S61661; TVBYR1.
DR RefSeq; NP_014744.1; NM_001183520.1.
DR AlphaFoldDB; P01119; -.
DR SMR; P01119; -.
DR BioGRID; 34499; 88.
DR DIP; DIP-1041N; -.
DR IntAct; P01119; 8.
DR MINT; P01119; -.
DR STRING; 4932.YOR101W; -.
DR TCDB; 8.A.92.1.15; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; P01119; -.
DR SwissPalm; P01119; -.
DR MaxQB; P01119; -.
DR PaxDb; P01119; -.
DR PRIDE; P01119; -.
DR ABCD; P01119; 1 sequenced antibody.
DR EnsemblFungi; YOR101W_mRNA; YOR101W; YOR101W.
DR GeneID; 854268; -.
DR KEGG; sce:YOR101W; -.
DR SGD; S000005627; RAS1.
DR VEuPathDB; FungiDB:YOR101W; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000176617; -.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; P01119; -.
DR OMA; ECIKVIV; -.
DR BioCyc; YEAST:G3O-33634-MON; -.
DR PRO; PR:P01119; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P01119; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:SGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IGI:SGD.
DR GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
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..306
FT /note="Ras-like protein 1"
FT /id="PRO_0000030193"
FT PROPEP 307..309
FT /note="Removed in mature form"
FT /id="PRO_0000030194"
FT REGION 177..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="Effector region"
FT COMPBIAS 180..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 36..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 66..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 153..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 306
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:2050108"
FT LIPID 305
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:3513173"
FT LIPID 306
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1763050"
FT CONFLICT 204
FT /note="R -> I (in Ref. 1; AAA34958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34347 MW; A70D720EB67E2F91 CRC64;
MQGNKSTIRE YKIVVVGGGG VGKSALTIQF IQSYFVDEYD PTIEDSYRKQ VVIDDKVSIL
DILDTAGQEE YSAMREQYMR TGEGFLLVYS VTSRNSFDEL LSYYQQIQRV KDSDYIPVVV
VGNKLDLENE RQVSYEDGLR LAKQLNAPFL ETSAKQAINV DEAFYSLIRL VRDDGGKYNS
MNRQLDNTNE IRDSELTSSA TADREKKNNG SYVLDNSLTN AGTGSSSKSA VNHNGETTKR
TDEKNYVNQN NNNEGNTKYS SNGNGNRSDI SRGNQNNALN SRSKQSAEPQ KNSSANARKE
SSGGCCIIC
