GLRX2_SCHPO
ID GLRX2_SCHPO Reviewed; 110 AA.
AC Q9UTI2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Glutaredoxin-2;
GN Name=grx2; ORFNames=SPAC15E1.09;
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., Cho Y.-W., Lee Y.-Y., Lim C.-J.;
RT "Cloning and expression of glutaredoxin 2 (thioltransferase 2) from
RT Schizosaccharomyces pombe.";
RL Submitted (MAY-2001) 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).
CC -!- FUNCTION: The disulfide bond functions as an electron carrier in the
CC glutathione-dependent synthesis of deoxyribonucleotides by the enzyme
CC ribonucleotide reductase. In addition, it is also involved in reducing
CC some disulfides in a coupled system with glutathione reductase.
CC Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation
CC reactions. It transfers reducing equivalents to cytosolic protein and
CC nonprotein disulfides (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {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; AF380128; AAK55420.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB52428.1; -; Genomic_DNA.
DR PIR; T37724; T37724.
DR RefSeq; NP_594310.1; NM_001019733.2.
DR AlphaFoldDB; Q9UTI2; -.
DR SMR; Q9UTI2; -.
DR BioGRID; 279255; 2.
DR STRING; 4896.SPAC15E1.09.1; -.
DR MaxQB; Q9UTI2; -.
DR PaxDb; Q9UTI2; -.
DR EnsemblFungi; SPAC15E1.09.1; SPAC15E1.09.1:pep; SPAC15E1.09.
DR GeneID; 2542807; -.
DR KEGG; spo:SPAC15E1.09; -.
DR PomBase; SPAC15E1.09; grx2.
DR VEuPathDB; FungiDB:SPAC15E1.09; -.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; Q9UTI2; -.
DR OMA; DSTHAQF; -.
DR PhylomeDB; Q9UTI2; -.
DR PRO; PR:Q9UTI2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; 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:0004602; F:glutathione peroxidase activity; ISS:PomBase.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:PomBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:PomBase.
DR InterPro; IPR011767; GLR_AS.
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; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..110
FT /note="Glutaredoxin-2"
FT /id="PRO_0000141611"
FT DOMAIN 6..106
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 26..29
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 110 AA; 12235 MW; 93B4FEA9DBEA2287 CRC64;
MTSIAKAFVE KAISNNPVTV FSKSFCPFCK AAKNTLTKYS APYKAYELDK IENGSDIQAY
LHEKTKQSTV PSIFFRNQFI GGNSDLNKLR SSGTLTKMIA ELKENKSSIL
