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 29-MAY-2013, entry version 93.
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 MASS
RP 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: Binds 1 manganese ion per subunit.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- INDUCTION: By high osmolarity and heat.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC family.
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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 MINT; MINT-4706830; -.
DR STRING; 4896.SPAC1486.01-1; -.
DR PaxDb; Q9UQX0; -.
DR PRIDE; 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; MAPPGKG; -.
DR OrthoDB; EOG42Z80G; -.
DR NextBio; 20803926; -.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0030145; F:manganese ion binding; ISS:PomBase.
DR GO; GO:0004784; F:superoxide dismutase activity; ISO:PomBase.
DR GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; ISO:PomBase.
DR GO; GO:0006801; P:superoxide metabolic process; IC: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; SODismutase; 1.
DR SUPFAM; SSF54719; SODismutase; 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 CHAIN 22 218 Superoxide dismutase [Mn], mitochondrial.
FT /FTId=PRO_0000032887.
FT METAL 50 50 Manganese (By similarity).
FT METAL 96 96 Manganese (By similarity).
FT METAL 181 181 Manganese (By similarity).
FT METAL 185 185 Manganese (By similarity).
FT MOD_RES 129 129 Phosphoserine.
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
//
