GLRX4_SCHPO
ID GLRX4_SCHPO Reviewed; 244 AA.
AC O74790;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Monothiol glutaredoxin-4;
GN Name=grx4; ORFNames=SPBC26H8.06;
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 Kim H.-G., Lim C.-J.;
RT "Stress response of monothiol glutaredoxin genes from Schizosaccharomyces
RT pombe.";
RL Submitted (OCT-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 SUBCELLULAR LOCATION.
RX PubMed=15796926; DOI=10.1016/j.bbrc.2005.02.183;
RA Chung W.H., Kim K.D., Roe J.H.;
RT "Localization and function of three monothiol glutaredoxins in
RT Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 330:604-610(2005).
RN [4]
RP INDUCTION.
RX PubMed=16175211; DOI=10.1139/w05-034;
RA Kim H.G., Kim B.C., Park E.H., Lim C.J.;
RT "Stress-dependent regulation of a monothiol glutaredoxin gene from
RT Schizosaccharomyces pombe.";
RL Can. J. Microbiol. 51:613-620(2005).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP INTERACTION WITH PHP4.
RX PubMed=19502236; DOI=10.1074/jbc.m109.009563;
RA Mercier A., Labbe S.;
RT "Both Php4 function and subcellular localization are regulated by iron via
RT a multistep mechanism involving the glutaredoxin Grx4 and the exportin
RT Crm1.";
RL J. Biol. Chem. 284:20249-20262(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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with php4. {ECO:0000250,
CC ECO:0000269|PubMed:19502236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000305}.
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DR EMBL; AY435094; AAR08197.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21098.1; -; Genomic_DNA.
DR PIR; T40018; T40018.
DR RefSeq; NP_596647.1; NM_001022569.2.
DR AlphaFoldDB; O74790; -.
DR SMR; O74790; -.
DR BioGRID; 277104; 13.
DR IntAct; O74790; 1.
DR STRING; 4896.SPBC26H8.06.1; -.
DR MaxQB; O74790; -.
DR PaxDb; O74790; -.
DR EnsemblFungi; SPBC26H8.06.1; SPBC26H8.06.1:pep; SPBC26H8.06.
DR GeneID; 2540578; -.
DR KEGG; spo:SPBC26H8.06; -.
DR PomBase; SPBC26H8.06; grx4.
DR VEuPathDB; FungiDB:SPBC26H8.06; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; O74790; -.
DR OMA; MNEVVLE; -.
DR PhylomeDB; O74790; -.
DR PRO; PR:O74790; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
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:0140311; F:protein sequestering activity; EXP:PomBase.
DR GO; GO:0044572; P:[4Fe-4S] cluster assembly; ISO:PomBase.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:PomBase.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IMP:PomBase.
DR GO; GO:0051604; P:protein maturation; ISO:PomBase.
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 TIGRFAMs; TIGR00365; TIGR00365; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW Redox-active center; Reference proteome.
FT CHAIN 1..244
FT /note="Monothiol glutaredoxin-4"
FT /id="PRO_0000102253"
FT DOMAIN 2..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 147..244
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 164
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 172
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 201..205
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 226..227
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 27099 MW; 63D9022435EB6385 CRC64;
MSVEITFVEQ FQEILQNGKE QIILLNFYAP WAAPCKQMNQ VFDQFAKDTK NAVFLKIEAE
KFSDIAESFD VNAVPLFVLI HGAKVLARIS GANPQKLKAA IDEYIQPLIS QISSTNASVE
TQVNSVQTTN TTSNTSKAPN GLDSELNERL STLTNAHNVM LFLKGTPSEP ACGFSRKLVG
LLREQNVQYG FFNILADDSV RQGLKVFSDW PTFPQLYIKG EFVGGLDIVS EMIENGELQE
MLPN
