ID   GPX1_SCHPO              Reviewed;         158 AA.
AC   O59858;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Glutathione peroxidase;
DE            EC=1.11.1.9;
GN   Name=gpx1; ORFNames=SPBC32F12.03c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=JY741;
RX   MEDLINE=99387094; PubMed=10455235;
RX   DOI=10.1002/(SICI)1097-0061(199908)15:11<1125::AID-YEA442>3.0.CO;2-Z;
RA   Yamada K., Nakagawa C.W., Mutoh N.;
RT   "Schizosaccharomyces pombe homologue of glutathione peroxidase, which
RT   does not contain selenocysteine, is induced by several stresses and
RT   works as an antioxidant.";
RL   Yeast 15:1125-1132(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Constitutes a glutathionine peroxidase-like protective
CC       system against oxidative stresses. Acts as a scavenger of
CC       H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- INDUCTION: By oxidative, osmo- and heat stress.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AB012395; BAA25326.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA19364.1; -; Genomic_DNA.
DR   PIR; T43376; T43376.
DR   RefSeq; NP_596146.1; -.
DR   HSSP; P00435; 1GP1.
DR   PeroxiBase; 3744; SpomGPx01.
DR   GeneID; 2540222; -.
DR   KEGG; spo:SPBC32F12.03c; -.
DR   NMPDR; fig|4896.1.peg.2012; -.
DR   GeneDB_Spombe; SPBC32F12.03c; -.
DR   OMA; O59858; NTASECA.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004182-MON; -.
DR   BRENDA; 1.11.1.9; 653.
DR   ArrayExpress; O59858; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0004602; F:glutathione peroxidase activity; TAS:GeneDB_SPombe.
DR   GO; GO:0034605; P:cellular response to heat; IEP:GeneDB_SPombe.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IGI:GeneDB_SPombe.
DR   GO; GO:0006970; P:response to osmotic stress; IEP:GeneDB_SPombe.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11592; Glut_peroxidase; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Oxidoreductase; Peroxidase; Stress response.
FT   CHAIN         1    158       Glutathione peroxidase.
FT                                /FTId=PRO_0000066644.
FT   ACT_SITE     36     36       By similarity.
SQ   SEQUENCE   158 AA;  18061 MW;  2D7009280B676876 CRC64;
     MSHFYDLAPK DKDGNPFPFS NLKGKVVLVV NTASKCGFTP QYKGLEALYQ KYKDRGFIIL
     GFPCNQFGNQ EPGSDEEIAQ FCQKNYGVTF PVLAKINVNG DNVDPVYQFL KSQKKQLGLE
     RIKWNFEKFL VNRQGQVIER YSSISKPEHL ENDIESVL
//