GLRX3_SCHPO
ID GLRX3_SCHPO Reviewed; 166 AA.
AC Q9Y7N3; Q76PC6; Q9UU55;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Monothiol glutaredoxin-3;
GN Name=grx3; ORFNames=SPCC1450.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moon J.-S., Kim H.-G., Lim H.-W., Lim C.-J.;
RT "Characterization of Glutaredoxin 3 (Thioltransferase 3) from
RT Schizosaccharomyces pombe.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-136, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; AY350733; AAQ56717.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB40173.1; -; Genomic_DNA.
DR EMBL; AB027803; BAA87107.1; -; Genomic_DNA.
DR PIR; T40988; T40988.
DR RefSeq; NP_588305.1; NM_001023295.2.
DR AlphaFoldDB; Q9Y7N3; -.
DR SMR; Q9Y7N3; -.
DR BioGRID; 275574; 32.
DR STRING; 4896.SPCC1450.06c.1; -.
DR SwissPalm; Q9Y7N3; -.
DR MaxQB; Q9Y7N3; -.
DR PaxDb; Q9Y7N3; -.
DR EnsemblFungi; SPCC1450.06c.1; SPCC1450.06c.1:pep; SPCC1450.06c.
DR GeneID; 2539000; -.
DR KEGG; spo:SPCC1450.06c; -.
DR PomBase; SPCC1450.06c; grx3.
DR VEuPathDB; FungiDB:SPCC1450.06c; -.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_136365_0_0_1; -.
DR InParanoid; Q9Y7N3; -.
DR OMA; GELDRWT; -.
DR PhylomeDB; Q9Y7N3; -.
DR PRO; PR:Q9Y7N3; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005796; C:Golgi lumen; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IMP:PomBase.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; ISO:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; ISO:PomBase.
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 3: Inferred from homology;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Nucleus; Redox-active center;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Monothiol glutaredoxin-3"
FT /id="PRO_0000102251"
FT DOMAIN 56..159
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 18314 MW; 6A2BAFD8FB8D72B6 CRC64;
MANRKIFLIT SLIISLLLIH IFIFSPLNEP EKNAKAGPLG LSDVSVPSAP KLPAKDSTDF
EVFLENPVII FSRPGCPYSA AAKKLLTETL RLDPPAVVVE VTDYEHTQEL RDWLSSISDI
STMPNIFVGG HSIGGSDSVR ALYQEEKLQS TLDEWTHNKV LILPTD
