SRX1_SCHPO
ID SRX1_SCHPO Reviewed; 124 AA.
AC Q9URV9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sulfiredoxin;
DE EC=1.8.98.2 {ECO:0000305|PubMed:15824112};
GN Name=srx1; ORFNames=SPBC106.02c;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TPX1.
RX PubMed=15824112; DOI=10.1074/jbc.m502757200;
RA Bozonet S.M., Findlay V.J., Day A.M., Cameron J., Veal E.A., Morgan B.A.;
RT "Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch
RT controlling the transcriptional response to increasing levels of hydrogen
RT peroxide.";
RL J. Biol. Chem. 280:23319-23327(2005).
RN [3]
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).
CC -!- FUNCTION: Contributes to oxidative stress resistance by reducing
CC cysteine-sulfinic acid formed under exposure to oxidants in a
CC peroxiredoxin. May catalyze the reduction in a multi-step process by
CC acting both as a specific phosphotransferase and a thioltransferase.
CC {ECO:0000269|PubMed:15824112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-
CC [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-
CC L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA-
CC COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-
CC COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974,
CC ChEBI:CHEBI:456216; EC=1.8.98.2;
CC Evidence={ECO:0000305|PubMed:15824112};
CC -!- SUBUNIT: Interacts with tpx1 in response to oxidative stress.
CC {ECO:0000269|PubMed:15824112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the sulfiredoxin family. {ECO:0000305}.
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DR EMBL; CU329671; CAB53718.1; -; Genomic_DNA.
DR PIR; T39259; T39259.
DR RefSeq; NP_595151.1; NM_001021060.2.
DR AlphaFoldDB; Q9URV9; -.
DR SMR; Q9URV9; -.
DR BioGRID; 276607; 4.
DR STRING; 4896.SPBC106.02c.1; -.
DR iPTMnet; Q9URV9; -.
DR MaxQB; Q9URV9; -.
DR PaxDb; Q9URV9; -.
DR EnsemblFungi; SPBC106.02c.1; SPBC106.02c.1:pep; SPBC106.02c.
DR GeneID; 2540069; -.
DR KEGG; spo:SPBC106.02c; -.
DR PomBase; SPBC106.02c; srx1.
DR VEuPathDB; FungiDB:SPBC106.02c; -.
DR eggNOG; KOG3388; Eukaryota.
DR HOGENOM; CLU_124532_1_1_1; -.
DR InParanoid; Q9URV9; -.
DR OMA; CHRFAAY; -.
DR PhylomeDB; Q9URV9; -.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:Q9URV9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0032542; F:sulfiredoxin activity; IDA:PomBase.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:PomBase.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR016692; Sulfiredoxin.
DR PANTHER; PTHR21348; PTHR21348; 1.
DR Pfam; PF02195; ParBc; 1.
DR PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
PE 1: Evidence at protein level;
KW Antioxidant; ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..124
FT /note="Sulfiredoxin"
FT /id="PRO_0000211434"
FT DISULFID 83
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 124 AA; 13603 MW; FE34FE87ADF3EA64 CRC64;
MTSIHTGSNN NIVELDMSEL IRPIPPVLDM NKVNSMMETM TGKTPPASCG LTSEDLEAGE
LPPVDVLTFK KSGKPYYFAF GGCHRLRAHD EAGRKKVRCK LVNCSPNTLR LYLGASANKF
LDSD
