RNY1_YEAST
ID RNY1_YEAST Reviewed; 434 AA.
AC Q02933; D6W3P4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1; OrderedLocusNames=YPL123C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11158587; DOI=10.1073/pnas.98.3.1018;
RA MacIntosh G.C., Bariola P.A., Newbigin E., Green P.J.;
RT "Characterization of Rny1, the Saccharomyces cerevisiae member of the T2
RT RNase family of RNases: unexpected functions for ancient enzymes?";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1018-1023(2001).
RN [5]
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 [6]
RP FUNCTION, MUTAGENESIS OF HIS-87 AND HIS-160, AND SUBCELLULAR LOCATION.
RX PubMed=19332891; DOI=10.1083/jcb.200811119;
RA Thompson D.M., Parker R.;
RT "The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative
RT stress in Saccharomyces cerevisiae.";
RL J. Cell Biol. 185:43-50(2009).
CC -!- FUNCTION: Rnase which modulates cell survival under stress conditions.
CC Released from the vacuole to the cytoplasm during stress to promote
CC tRNA and rRNA cleavage and to activate separately a downstream pathway
CC that promotes cell death. Involved in cell size, vacuolar morphology
CC and growth at high temperatures and high salt concentration.
CC {ECO:0000269|PubMed:11158587, ECO:0000269|PubMed:19332891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046};
CC -!- SUBCELLULAR LOCATION: Vacuole lumen. Cytoplasm. Note=Is released from
CC the vacuole to the cytoplasm during stress conditions like oxidative
CC stress or stationary phase stress.
CC -!- INDUCTION: Up-regulated by heat shock and osmotic stress.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11158587}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; U43503; AAB68239.1; -; Genomic_DNA.
DR EMBL; AY692990; AAT93009.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11310.1; -; Genomic_DNA.
DR PIR; S61999; S61999.
DR RefSeq; NP_015202.1; NM_001183937.1.
DR AlphaFoldDB; Q02933; -.
DR SMR; Q02933; -.
DR BioGRID; 36058; 125.
DR STRING; 4932.YPL123C; -.
DR MaxQB; Q02933; -.
DR PaxDb; Q02933; -.
DR PRIDE; Q02933; -.
DR EnsemblFungi; YPL123C_mRNA; YPL123C; YPL123C.
DR GeneID; 855980; -.
DR KEGG; sce:YPL123C; -.
DR SGD; S000006044; RNY1.
DR VEuPathDB; FungiDB:YPL123C; -.
DR eggNOG; KOG1642; Eukaryota.
DR GeneTree; ENSGT00640000091563; -.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q02933; -.
DR OMA; LWIHEFN; -.
DR BioCyc; YEAST:G3O-34022-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:Q02933; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02933; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:SGD.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IGI:SGD.
DR GO; GO:0000902; P:cell morphogenesis; IMP:SGD.
DR GO; GO:0006401; P:RNA catabolic process; IMP:SGD.
DR CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase;
KW Nuclease; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..434
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000042717"
FT ACT_SITE 87
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT ACT_SITE 160
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..46
FT /evidence="ECO:0000250"
FT DISULFID 35..94
FT /evidence="ECO:0000250"
FT DISULFID 45..171
FT /evidence="ECO:0000250"
FT DISULFID 102..163
FT /evidence="ECO:0000250"
FT DISULFID 241..277
FT /evidence="ECO:0000250"
FT MUTAGEN 87
FT /note="H->F: Impairs cytosolic tRNA-cleaving activity; when
FT associated with F-160."
FT /evidence="ECO:0000269|PubMed:19332891"
FT MUTAGEN 160
FT /note="H->F: Impairs cytosolic tRNA-cleaving activity; when
FT associated with F-87."
FT /evidence="ECO:0000269|PubMed:19332891"
SQ SEQUENCE 434 AA; 50171 MW; 0BBE8B3C5C7351E1 CRC64;
MLLKNLHSLL QLPIFSNGAD KGIEPNCPIN IPLSCSNKTD IDNSCCFEYP GGIFLQTQFW
NYFPSKNDLN ETELVKELGP LDSFTIHGLW PDNCHGGYQQ FCNRSLQIDD VYYLLHDKKF
NNNDTSLQIS GEKLLEYLDL YWKSNNGNHE SLWIHEFNKH GTCISTIRPE CYTEWGANSV
DRKRAVYDYF RITYNLFKKL DTFSTLEKNN IVPSVDNSYS LEQIEAALSK EFEGKKVFIG
CDRHNSLNEV WYYNHLKGSL LSEMFVPMDS LAIRTNCKKD GIKFFPKGYV PTFRRRPNKG
ARYRGVVRLS NINNGDQMQG FLIKNGHWMS QGTPANYELI KSPYGNYYLR TNQGFCDIIS
SSSNELVCKF RNIKDAGQFD FDPTKGGDGY IGYSGNYNWG GDTYPRRRNQ SPIFSVDDEQ
NSKKYKFKLK FIKN
