GLRX4_YEAST
ID GLRX4_YEAST Reviewed; 244 AA.
AC P32642; D3DM82;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Monothiol glutaredoxin-4;
GN Name=GRX4; OrderedLocusNames=YER174C; ORFNames=SYGP-ORF64;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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, AND INTERACTION
RP WITH FRA2.
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).
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 P32642; P22149: AFT1; NbExp=2; IntAct=EBI-22211, EBI-2332;
CC P32642; P53323: BUD32; NbExp=11; IntAct=EBI-22211, EBI-3809;
CC -!- MISCELLANEOUS: Present with 7800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {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; U18922; AAB64701.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07836.1; -; Genomic_DNA.
DR PIR; S30860; S30860.
DR RefSeq; NP_011101.3; NM_001179064.3.
DR AlphaFoldDB; P32642; -.
DR SMR; P32642; -.
DR BioGRID; 36927; 115.
DR ComplexPortal; CPX-6865; BOL2-GRX4 iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-6921; GRX4 iron-sulfur cluster assembly homodimer complex.
DR DIP; DIP-6635N; -.
DR IntAct; P32642; 14.
DR MINT; P32642; -.
DR STRING; 4932.YER174C; -.
DR iPTMnet; P32642; -.
DR MaxQB; P32642; -.
DR PaxDb; P32642; -.
DR PRIDE; P32642; -.
DR EnsemblFungi; YER174C_mRNA; YER174C; YER174C.
DR GeneID; 856921; -.
DR KEGG; sce:YER174C; -.
DR SGD; S000000976; GRX4.
DR VEuPathDB; FungiDB:YER174C; -.
DR eggNOG; KOG0911; Eukaryota.
DR GeneTree; ENSGT00550000075030; -.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; P32642; -.
DR OMA; MNEVVLE; -.
DR BioCyc; YEAST:G3O-30334-MON; -.
DR PRO; PR:P32642; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32642; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004364; F:glutathione transferase activity; 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:cellular iron ion homeostasis; IGI: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 GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IMP:SGD.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:SGD.
DR CDD; cd03028; GRX_PICOT_like; 1.
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; PTHR10293; 2.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Redox-active center;
KW Reference proteome.
FT CHAIN 1..244
FT /note="Monothiol glutaredoxin-4"
FT /id="PRO_0000102250"
FT DOMAIN 3..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 146..244
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 225..226
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 27493 MW; 86B4C4993545B5B2 CRC64;
MTVVEIKSQD QFTQLTTTNA ANKLIVLYFK AQWADPCKTM SQVLEAVSEK VRQEDVRFLS
IDADEHPEIS DLFEIAAVPY FVFIQNGTIV KEISAADPKE FVKSLEILSN ASASLANNAK
GPKSTSDEES SGSSDDEEDE TEEEINARLV KLVQAAPVML FMKGSPSEPK CGFSRQLVGI
LREHQIRFGF FDILRDENVR QSLKKFSDWP TFPQLYINGE FQGGLDIIKE SIEEDPEYFQ
HALQ
