RSR1_YEAST
ID RSR1_YEAST Reviewed; 272 AA.
AC P13856; D6VUT2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ras-related protein RSR1 {ECO:0000303|PubMed:2690082};
DE EC=3.6.5.2 {ECO:0000269|PubMed:1910037};
DE Flags: Precursor;
GN Name=RSR1 {ECO:0000303|PubMed:2690082}; Synonyms=BUD1;
GN OrderedLocusNames=YGR152C {ECO:0000312|SGD:S000003384}; ORFNames=G6658;
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], AND FUNCTION.
RX PubMed=2690082; DOI=10.1073/pnas.86.24.9976;
RA Bender A., Pringle J.R.;
RT "Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and
RT three newly identified genes including the ras-related gene RSR1.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9976-9980(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP GLY-12.
RX PubMed=1910037; DOI=10.1016/s0021-9258(19)47330-4;
RA Holden J.L., Nur-E-Kamal M.S., Fabri L., Nice E., Hammacher A., Maruta H.;
RT "Rsr1 and Rap1 GTPases are activated by the same GTPase-activating protein
RT and require threonine 65 for their activation.";
RL J. Biol. Chem. 266:16992-16995(1991).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
CC -!- FUNCTION: Ras-related protein which binds GDP/GTP and possesses
CC intrinsic GTPase activity (PubMed:1910037). Involved in development of
CC cell polarity during the cell division cycle, and essential for bud
CC emergence (PubMed:2690082). {ECO:0000269|PubMed:1910037,
CC ECO:0000269|PubMed:2690082}.
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:0000269|PubMed:1910037};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP (PubMed:1910037). Activated by a
CC guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC activating protein (GAP) (PubMed:1910037).
CC {ECO:0000269|PubMed:1910037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; M26928; AAA35013.1; -; Genomic_DNA.
DR EMBL; X85807; CAA59809.1; -; Genomic_DNA.
DR EMBL; Z72936; CAA97166.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08243.1; -; Genomic_DNA.
DR PIR; A34511; A34511.
DR RefSeq; NP_011668.3; NM_001181281.3.
DR AlphaFoldDB; P13856; -.
DR SMR; P13856; -.
DR BioGRID; 33400; 64.
DR DIP; DIP-2230N; -.
DR IntAct; P13856; 25.
DR MINT; P13856; -.
DR STRING; 4932.YGR152C; -.
DR iPTMnet; P13856; -.
DR MaxQB; P13856; -.
DR PaxDb; P13856; -.
DR PRIDE; P13856; -.
DR EnsemblFungi; YGR152C_mRNA; YGR152C; YGR152C.
DR GeneID; 853056; -.
DR KEGG; sce:YGR152C; -.
DR SGD; S000003384; RSR1.
DR VEuPathDB; FungiDB:YGR152C; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000173447; -.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; P13856; -.
DR OMA; NVPMVIV; -.
DR BioCyc; YEAST:G3O-30854-MON; -.
DR Reactome; R-SCE-354192; Integrin signaling.
DR Reactome; R-SCE-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-SCE-392517; Rap1 signalling.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P13856; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P13856; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005774; C:vacuolar 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:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0000755; P:cytogamy; IMP:SGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:SGD.
DR GO; GO:0032507; P:maintenance of protein location in cell; IGI:SGD.
DR GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IMP:SGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:SGD.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:SGD.
DR CDD; cd04177; RSR1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041841; Rsr1.
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 cycle; Cell division; Cell membrane; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..269
FT /note="Ras-related protein RSR1"
FT /id="PRO_0000082691"
FT PROPEP 270..272
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281342"
FT REGION 177..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 177..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 269
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 269
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 12
FT /note="G->V: Loss of GAP-induced GTPase activity."
FT /evidence="ECO:0000269|PubMed:1910037"
SQ SEQUENCE 272 AA; 30391 MW; 6FF0B6C9E114A6DC CRC64;
MRDYKLVVLG AGGVGKSCLT VQFVQGVYLD TYDPTIEDSY RKTIEIDNKV FDLEILDTAG
IAQFTAMREL YIKSGMGFLL VYSVTDRQSL EELMELREQV LRIKDSDRVP MVLIGNKADL
INERVISVEE GIEVSSKWGR VPFYETSALL RSNVDEVFVD LVRQIIRNEM ESVAVKDARN
QSQQFSKIES PSTRLPSSAK QDTKQSNNKQ SSKGLYNKSS QGQAKVKQST PVNEKHKPSH
AVPKSGSSNR TGISATSQQK KKKKNASTCT IL
