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Monothiol glutaredoxin-6

 GLRX6_YEAST             Reviewed;         231 AA.
Q12438; D6VRX8;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 128.
RecName: Full=Monothiol glutaredoxin-6;
Flags: Precursor;
Name=GRX6; OrderedLocusNames=YDL010W; ORFNames=D2890;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 70-82; 85-102; 144-175; 181-193 AND 208-219, AND
IDENTIFICATION BY MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 1643 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
subfamily. {ECO:0000305}.
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EMBL; Z48432; CAA88349.1; -; Genomic_DNA.
EMBL; Z74059; CAA98567.1; -; Genomic_DNA.
EMBL; BK006938; DAA11838.1; -; Genomic_DNA.
PIR; S52509; S52509.
RefSeq; NP_010274.1; NM_001180069.1.
PDB; 3L4N; X-ray; 1.50 A; A=113-231.
PDB; 5J3R; X-ray; 2.46 A; A=37-231.
PDBsum; 3L4N; -.
PDBsum; 5J3R; -.
ProteinModelPortal; Q12438; -.
SMR; Q12438; -.
BioGrid; 32043; 39.
MINT; MINT-4478768; -.
STRING; 4932.YDL010W; -.
iPTMnet; Q12438; -.
MaxQB; Q12438; -.
PRIDE; Q12438; -.
EnsemblFungi; YDL010W; YDL010W; YDL010W.
GeneID; 851551; -.
KEGG; sce:YDL010W; -.
EuPathDB; FungiDB:YDL010W; -.
SGD; S000002168; GRX6.
GeneTree; ENSGT00550000075735; -.
HOGENOM; HOG000208731; -.
InParanoid; Q12438; -.
OMA; PMTIFSK; -.
OrthoDB; EOG092C3ZJC; -.
BioCyc; YEAST:G3O-29441-MONOMER; -.
EvolutionaryTrace; Q12438; -.
PRO; PR:Q12438; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0005796; C:Golgi lumen; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IDA:SGD.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:SGD.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0004362; F:glutathione-disulfide reductase activity; IDA:SGD.
GO; GO:0005506; F:iron ion binding; IDA:SGD.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:SGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR014025; Glutaredoxin_subgr.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00462; Glutaredoxin; 1.
PRINTS; PR00160; GLUTAREDOXIN.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Direct protein sequencing;
Iron; Iron-sulfur; Metal-binding; Reference proteome; Signal; Vacuole.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 231 Monothiol glutaredoxin-6.
/FTId=PRO_0000042988.
DOMAIN 116 219 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 136 136 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000255}.
HELIX 115 123 {ECO:0000244|PDB:3L4N}.
STRAND 127 132 {ECO:0000244|PDB:3L4N}.
HELIX 137 149 {ECO:0000244|PDB:3L4N}.
STRAND 150 154 {ECO:0000244|PDB:3L4N}.
STRAND 157 160 {ECO:0000244|PDB:3L4N}.
HELIX 161 163 {ECO:0000244|PDB:3L4N}.
HELIX 167 178 {ECO:0000244|PDB:3L4N}.
STRAND 185 188 {ECO:0000244|PDB:3L4N}.
HELIX 196 204 {ECO:0000244|PDB:3L4N}.
HELIX 208 214 {ECO:0000244|PDB:3L4N}.
STRAND 221 224 {ECO:0000244|PDB:3L4N}.
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


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