OXR1_YEAST
ID OXR1_YEAST Reviewed; 273 AA.
AC Q08952; D6W3H2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Oxidation resistance protein 1;
GN Name=OXR1; OrderedLocusNames=YPL196W;
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 FUNCTION.
RX PubMed=11114193; DOI=10.1073/pnas.260495897;
RA Volkert M.R., Elliott N.A., Housman D.E.;
RT "Functional genomics reveals a family of eukaryotic oxidation protection
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14530-14535(2000).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15060142; DOI=10.1128/mcb.24.8.3180-3187.2004;
RA Elliott N.A., Volkert M.R.;
RT "Stress induction and mitochondrial localization of Oxr1 proteins in yeast
RT and humans.";
RL Mol. Cell. Biol. 24:3180-3187(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: Involved in protection from oxidative damage.
CC {ECO:0000269|PubMed:11114193, ECO:0000269|PubMed:15060142}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15060142}.
CC -!- INDUCTION: Up-regulated by heat and oxidative stress.
CC {ECO:0000269|PubMed:15060142}.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
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DR EMBL; Z73552; CAA97909.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11238.1; -; Genomic_DNA.
DR PIR; S65215; S65215.
DR RefSeq; NP_015128.1; NM_001184010.1.
DR PDB; 7FDE; EM; 3.80 A; P=1-273.
DR PDBsum; 7FDE; -.
DR AlphaFoldDB; Q08952; -.
DR SMR; Q08952; -.
DR BioGRID; 35987; 81.
DR DIP; DIP-3976N; -.
DR IntAct; Q08952; 3.
DR STRING; 4932.YPL196W; -.
DR iPTMnet; Q08952; -.
DR MaxQB; Q08952; -.
DR PaxDb; Q08952; -.
DR PRIDE; Q08952; -.
DR TopDownProteomics; Q08952; -.
DR EnsemblFungi; YPL196W_mRNA; YPL196W; YPL196W.
DR GeneID; 855905; -.
DR KEGG; sce:YPL196W; -.
DR SGD; S000006117; OXR1.
DR VEuPathDB; FungiDB:YPL196W; -.
DR eggNOG; KOG2372; Eukaryota.
DR GeneTree; ENSGT00940000167904; -.
DR HOGENOM; CLU_029204_0_0_1; -.
DR InParanoid; Q08952; -.
DR OMA; YRGGSHP; -.
DR BioCyc; YEAST:G3O-34089-MON; -.
DR PRO; PR:Q08952; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08952; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00584; TLDc; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..273
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000058123"
FT DOMAIN 74..273
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 18..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 273 AA; 30779 MW; 17697B583D1296CA CRC64;
MFGVKDAIFK IKRSIAGTDS SDSTAYTTAS ESSPQLKDSH NPFRNKTTSE RTIVEEGSLP
PVRLNGYLPS TKNKLLTPEM CDEIRTLMPT RIQLYTEWNL LYSLEQHGSS LHSLYSNVAP
DSKEFRRVGY VLVIKDRKNG IFGAYSNEAF HPNEHRQYTG NGECFLWKLD KVPDVNISEK
EESEQEGKEG KEEGDKEERW RFSGYPYTGV NEFAIYCTSE FLSMGAGDGH YGLLCDDGLL
HGVSNPCQTY GNEVLSKEGK KFSIVALEVW RVG
