ID GLRX3_YEAST Reviewed; 250 AA.
AC Q03835; D6VS83;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=Monothiol glutaredoxin-3;
GN Name=GRX3; OrderedLocusNames=YDR098C; ORFNames=YD8557.05C;
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 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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FRA2.
RX PubMed=18281282; DOI=10.1074/jbc.m801160200;
RA Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H.,
RA Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J.;
RT "Identification of FRA1 and FRA2 as genes involved in regulating the yeast
RT iron regulon in response to decreased mitochondrial iron-sulfur cluster
RT synthesis.";
RL J. Biol. Chem. 283:10276-10286(2008).
RN [5]
RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH
RP FRA2, AND IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=19715344; DOI=10.1021/bi901182w;
RA Li H., Mapolelo D.T., Dingra N.N., Naik S.G., Lees N.S., Hoffman B.M.,
RA Riggs-Gelasco P.J., Huynh B.H., Johnson M.K., Outten C.E.;
RT "The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric
RT complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl
RT ligation.";
RL Biochemistry 48:9569-9581(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-113.
RX PubMed=18703840; DOI=10.1107/s0907444908021641;
RA Gibson L.M., Dingra N.N., Outten C.E., Lebioda L.;
RT "Structure of the thioredoxin-like domain of yeast glutaredoxin 3.";
RL Acta Crystallogr. D 64:927-932(2008).
CC -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-
CC sulfur clusters (By similarity). Binds one iron-sulfur cluster per
CC dimer. The iron-sulfur cluster is bound between subunits, and is
CC complexed by a bound glutathione and a cysteine residue from each
CC subunit (Probable). {ECO:0000250, ECO:0000269|PubMed:19715344,
CC ECO:0000305}.
CC -!- SUBUNIT: Homodimer. Heterodimer with FRA2.
CC {ECO:0000269|PubMed:19715344}.
CC -!- INTERACTION:
CC Q03835; P22149: AFT1; NbExp=4; IntAct=EBI-22178, EBI-2332;
CC Q03835; P53082: BOL2; NbExp=2; IntAct=EBI-22178, EBI-24159;
CC Q03835; P53323: BUD32; NbExp=3; IntAct=EBI-22178, EBI-3809;
CC -!- MISCELLANEOUS: Present with 11000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA87672.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z47746; CAA87672.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA11943.2; -; Genomic_DNA.
DR PIR; S51247; S51247.
DR RefSeq; NP_010383.4; NM_001180406.4.
DR PDB; 3D6I; X-ray; 1.50 A; A/B=2-113.
DR PDB; 5Y4U; X-ray; 1.70 A; A=144-250.
DR PDBsum; 3D6I; -.
DR PDBsum; 5Y4U; -.
DR AlphaFoldDB; Q03835; -.
DR SMR; Q03835; -.
DR BioGRID; 32153; 114.
DR ComplexPortal; CPX-6864; BOL2-GRX3 iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-6924; GRX3 iron-sulfur cluster assembly homodimer complex.
DR DIP; DIP-1350N; -.
DR IntAct; Q03835; 9.
DR MINT; Q03835; -.
DR STRING; 4932.YDR098C; -.
DR PaxDb; 4932-YDR098C; -.
DR PeptideAtlas; Q03835; -.
DR EnsemblFungi; YDR098C_mRNA; YDR098C; YDR098C.
DR GeneID; 851672; -.
DR KEGG; sce:YDR098C; -.
DR AGR; SGD:S000002505; -.
DR SGD; S000002505; GRX3.
DR VEuPathDB; FungiDB:YDR098C; -.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075030; -.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; Q03835; -.
DR OrthoDB; 1038at2759; -.
DR BioCyc; YEAST:MONOMER3O-100; -.
DR BioGRID-ORCS; 851672; 4 hits in 10 CRISPR screens.
DR EvolutionaryTrace; Q03835; -.
DR PRO; PR:Q03835; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03835; Protein.
DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IMP:SGD.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IGI:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:ComplexPortal.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IMP:SGD.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR CDD; cd02984; TRX_PICOT; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding;
KW Redox-active center; Reference proteome.
FT CHAIN 1..250
FT /note="Monothiol glutaredoxin-3"
FT /id="PRO_0000102249"
FT DOMAIN 1..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 151..250
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 113..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3D6I"
FT TURN 17..22
FT /evidence="ECO:0007829|PDB:3D6I"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3D6I"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3D6I"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:3D6I"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:3D6I"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:3D6I"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5Y4U"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5Y4U"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5Y4U"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5Y4U"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:5Y4U"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:5Y4U"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5Y4U"
SQ SEQUENCE 250 AA; 28261 MW; 8CC1A04EC1E7DAB3 CRC64;
MPVIEINDQE QFTYLTTTAA GDKLIVLYFH TSWAEPCKAL KQVFEAISNE PSNSNVSFLS
IDADENSEIS ELFEISAVPY FIIIHKGTIL KELSGADPKE YVSLLEDCKN SVNSGSSQTH
TMENANVNEG SHNDEDDDDE EEEEETEEQI NARLTKLVNA APVMLFMKGS PSEPKCGFSR
QLVGILREHQ VRFGFFDILR DESVRQNLKK FSEWPTFPQL YINGEFQGGL DIIKESLEED
PDFLQHALQS
//
