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Database: UniProt
Entry: Q9UQX0
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Original site: Q9UQX0 
ID   SODM_SCHPO              Reviewed;         218 AA.
AC   Q9UQX0;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   26-NOV-2014, entry version 104.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sod2; ORFNames=SPAC1486.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RA   Jeong J.-H., Kwon E.-S., Roe J.-H.;
RT   "Isolation and characterization of the sod2+ gene encoding a putative
RT   mitochondrial manganese superoxide dismutase in Schizosaccharomyces
RT   pombe.";
RL   J. Microbiol. 39:37-41(2001).
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.,
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-34, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND INDUCTION.
RC   STRAIN=JH201;
RX   PubMed=11350071; DOI=10.1006/bbrc.2001.4853;
RA   Jeong J.-H., Kwon E.-S., Roe J.-H.;
RT   "Characterization of the manganese-containing superoxide dismutase and
RT   its gene regulation in stress response of Schizosaccharomyces pombe.";
RL   Biochem. Biophys. Res. Commun. 283:908-914(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11350071};
CC       Note=Binds 1 Mn(2+) ion per subunit.
CC       {ECO:0000269|PubMed:11350071};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11350071}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:11350071}.
CC   -!- INDUCTION: By high osmolarity and heat.
CC       {ECO:0000269|PubMed:11350071}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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DR   EMBL; AF069292; AAF19051.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB62411.1; -; Genomic_DNA.
DR   PIR; T50070; T50070.
DR   RefSeq; NP_594089.1; NM_001019513.2.
DR   ProteinModelPortal; Q9UQX0; -.
DR   SMR; Q9UQX0; 25-217.
DR   BioGrid; 279331; 33.
DR   MINT; MINT-4706830; -.
DR   STRING; 4896.SPAC1486.01-1; -.
DR   MaxQB; Q9UQX0; -.
DR   PaxDb; Q9UQX0; -.
DR   EnsemblFungi; SPAC1486.01.1; SPAC1486.01.1:pep; SPAC1486.01.
DR   GeneID; 2542886; -.
DR   KEGG; spo:SPAC1486.01; -.
DR   PomBase; SPAC1486.01; -.
DR   eggNOG; COG0605; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; TERYTAC; -.
DR   PhylomeDB; Q9UQX0; -.
DR   Reactome; REACT_219607; Detoxification of Reactive Oxygen Species.
DR   NextBio; 20803926; -.
DR   PRO; PR:Q9UQX0; -.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0030145; F:manganese ion binding; ISS:PomBase.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:PomBase.
DR   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; ISO:PomBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:PomBase.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   PANTHER; PTHR11404; PTHR11404; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     21       Mitochondrion.
FT                                {ECO:0000269|PubMed:11350071}.
FT   CHAIN        22    218       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032887.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        96     96       Manganese. {ECO:0000250}.
FT   METAL       181    181       Manganese. {ECO:0000250}.
FT   METAL       185    185       Manganese. {ECO:0000250}.
FT   MOD_RES     129    129       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   218 AA;  24347 MW;  F701C8375830DDE7 CRC64;
     MLRFLSKNSV AAIRNVSIAR GVHTKATLPP LPYAYNALEP ALSETIMKLH HDKHHQTYVN
     NLNAAQEKLA DPNLDLEGEV ALQAAIKFNG GGHINHSLFW KILAPQKEGG GKPVTSGSLH
     KAITSKWGSL EDFQKEMNAA LASIQGSGWA WLIVDKDGSL RITTTANQDT IVKSKPIIGI
     DAWEHAYYPQ YENRKAEYFK AIWNVINWKE AESRYSNR
//
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