GLRX8_YEAST
ID GLRX8_YEAST Reviewed; 109 AA.
AC Q05926; D6VZ03;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutaredoxin-8;
DE AltName: Full=Glutathione-dependent oxidoreductase 8;
GN Name=GRX8; OrderedLocusNames=YLR364W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 INDUCTION.
RX PubMed=15575969; DOI=10.1186/gb-2004-5-12-r95;
RA Haugen A.C., Kelley R., Collins J.B., Tucker C.J., Deng C., Afshari C.A.,
RA Brown J.M., Ideker T., Van Houten B.;
RT "Integrating phenotypic and expression profiles to map arsenic-response
RT networks.";
RL Genome Biol. 5:R95.1-R95.18(2004).
RN [7]
RP FUNCTION.
RX PubMed=18400945; DOI=10.1091/mbc.e07-09-0896;
RA Mesecke N., Spang A., Deponte M., Herrmann J.M.;
RT "A novel group of glutaredoxins in the cis-Golgi critical for oxidative
RT stress resistance.";
RL Mol. Biol. Cell 19:2673-2680(2008).
RN [8]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-25 AND CYS-28.
RX PubMed=19166312; DOI=10.1021/bi801859b;
RA Eckers E., Bien M., Stroobant V., Herrmann J.M., Deponte M.;
RT "Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces
RT cerevisiae: the catalytic redox mechanism redux.";
RL Biochemistry 48:1410-1423(2009).
CC -!- FUNCTION: Glutathione-dependent oxidoreductase with lower activity
CC compared to the other members of the glutaredoxin family. The disulfide
CC bond functions as an electron carrier in the glutathione-dependent
CC synthesis of deoxyribonucleotides by the enzyme ribonucleotide
CC reductase. {ECO:0000269|PubMed:18400945, ECO:0000269|PubMed:19166312}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19166312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Strongly induced by the exposure to arsenic which causes
CC glutathione depletion. {ECO:0000269|PubMed:15575969}.
CC -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; U19103; AAB67570.1; -; Genomic_DNA.
DR EMBL; AY558221; AAS56547.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09669.1; -; Genomic_DNA.
DR PIR; S51382; S51382.
DR RefSeq; NP_013468.3; NM_001182253.3.
DR PDB; 2M80; NMR; -; A=1-109.
DR PDBsum; 2M80; -.
DR AlphaFoldDB; Q05926; -.
DR BMRB; Q05926; -.
DR SMR; Q05926; -.
DR BioGRID; 31626; 66.
DR IntAct; Q05926; 1.
DR STRING; 4932.YLR364W; -.
DR MaxQB; Q05926; -.
DR PaxDb; Q05926; -.
DR PRIDE; Q05926; -.
DR EnsemblFungi; YLR364W_mRNA; YLR364W; YLR364W.
DR GeneID; 851079; -.
DR KEGG; sce:YLR364W; -.
DR SGD; S000004356; GRX8.
DR VEuPathDB; FungiDB:YLR364W; -.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; Q05926; -.
DR OMA; RKWVPTI; -.
DR BioCyc; YEAST:G3O-32435-MON; -.
DR ChiTaRS; GRX8; yeast.
DR PRO; PR:Q05926; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05926; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IDA:SGD.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..109
FT /note="Glutaredoxin-8"
FT /id="PRO_0000268192"
FT DOMAIN 5..109
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 25..28
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT MUTAGEN 25
FT /note="C->S: Impairs activity."
FT /evidence="ECO:0000269|PubMed:19166312"
FT MUTAGEN 28
FT /note="C->S: Impairs activity."
FT /evidence="ECO:0000269|PubMed:19166312"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2M80"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:2M80"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:2M80"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2M80"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2M80"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:2M80"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2M80"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2M80"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2M80"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:2M80"
SQ SEQUENCE 109 AA; 12519 MW; 3353EFB47A61574A CRC64;
MSAFVTKAEE MIKSHPYFQL SASWCPDCVY ANSIWNKLNV QDKVFVFDIG SLPRNEQEKW
RIAFQKVVGS RNLPTIVVNG KFWGTESQLH RFEAKGTLEE ELTKIGLLP
