GLRX6_YEAST
ID GLRX6_YEAST Reviewed; 231 AA.
AC Q12438; D6VRX8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Monothiol glutaredoxin-6;
DE Flags: Precursor;
GN Name=GRX6; OrderedLocusNames=YDL010W; ORFNames=D2890;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PROTEIN SEQUENCE OF 70-82; 85-102; 144-175; 181-193 AND 208-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
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 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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1643 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48432; CAA88349.1; -; Genomic_DNA.
DR EMBL; Z74059; CAA98567.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11838.1; -; Genomic_DNA.
DR PIR; S52509; S52509.
DR RefSeq; NP_010274.1; NM_001180069.1.
DR PDB; 3L4N; X-ray; 1.50 A; A=113-231.
DR PDB; 5J3R; X-ray; 2.46 A; A=37-231.
DR PDBsum; 3L4N; -.
DR PDBsum; 5J3R; -.
DR AlphaFoldDB; Q12438; -.
DR SMR; Q12438; -.
DR BioGRID; 32043; 50.
DR ComplexPortal; CPX-2841; GRX6 iron-sulfur cluster assembly homodimer complex.
DR STRING; 4932.YDL010W; -.
DR iPTMnet; Q12438; -.
DR MaxQB; Q12438; -.
DR PaxDb; Q12438; -.
DR PRIDE; Q12438; -.
DR EnsemblFungi; YDL010W_mRNA; YDL010W; YDL010W.
DR GeneID; 851551; -.
DR KEGG; sce:YDL010W; -.
DR SGD; S000002168; GRX6.
DR VEuPathDB; FungiDB:YDL010W; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000176461; -.
DR HOGENOM; CLU_026126_0_1_1; -.
DR InParanoid; Q12438; -.
DR OMA; VAQNANF; -.
DR BioCyc; YEAST:G3O-29441-MON; -.
DR EvolutionaryTrace; Q12438; -.
DR PRO; PR:Q12438; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12438; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005796; C:Golgi lumen; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:SGD.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IDA:SGD.
DR GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..231
FT /note="Monothiol glutaredoxin-6"
FT /id="PRO_0000042988"
FT DOMAIN 116..219
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:3L4N"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3L4N"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:3L4N"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3L4N"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3L4N"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3L4N"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:3L4N"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3L4N"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:3L4N"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3L4N"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:3L4N"
SQ SEQUENCE 231 AA; 25783 MW; C76DD4E2A6E16744 CRC64;
MIPSNKRNAR ILSITTLLLL LVFFVAQNAN FLTVEIKEET SKAFSTNMDN MAGGSSREYA
AMPTSTTNKG SSEVDEEINE IKQKVGLQQP IASVDDSLSA IKNDKGSRIT KAFNVQKEYS
LILDLSPIII FSKSTCSYSK GMKELLENEY QFIPNYYIIE LDKHGHGEEL QEYIKLVTGR
GTVPNLLVNG VSRGGNEEIK KLHTQGKLLE SLQVWSDGKF SVEQREKPSN N
