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Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)

 SODM_SCHPO              Reviewed;         218 AA.
Q9UQX0;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 129.
RecName: Full=Superoxide dismutase [Mn], mitochondrial;
EC=1.15.1.1;
Flags: Precursor;
Name=sod2; ORFNames=SPAC1486.01;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=972 / ATCC 24843;
Jeong J.-H., Kwon E.-S., Roe J.-H.;
"Isolation and characterization of the sod2+ gene encoding a putative
mitochondrial manganese superoxide dismutase in Schizosaccharomyces
pombe.";
J. Microbiol. 39:37-41(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PROTEIN SEQUENCE OF 22-34, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION,
AND INDUCTION.
STRAIN=JH201;
PubMed=11350071; DOI=10.1006/bbrc.2001.4853;
Jeong J.-H., Kwon E.-S., Roe J.-H.;
"Characterization of the manganese-containing superoxide dismutase and
its gene regulation in stress response of Schizosaccharomyces pombe.";
Biochem. Biophys. Res. Commun. 283:908-914(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11350071};
Note=Binds 1 Mn(2+) ion per subunit.
{ECO:0000269|PubMed:11350071};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11350071}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11350071}.
-!- INDUCTION: By high osmolarity and heat.
{ECO:0000269|PubMed:11350071}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF069292; AAF19051.1; -; Genomic_DNA.
EMBL; CU329670; CAB62411.1; -; Genomic_DNA.
PIR; T50070; T50070.
RefSeq; NP_594089.1; NM_001019513.2.
ProteinModelPortal; Q9UQX0; -.
SMR; Q9UQX0; -.
BioGrid; 279331; 32.
STRING; 4896.SPAC1486.01.1; -.
iPTMnet; Q9UQX0; -.
MaxQB; Q9UQX0; -.
PaxDb; Q9UQX0; -.
PRIDE; Q9UQX0; -.
EnsemblFungi; SPAC1486.01.1; SPAC1486.01.1:pep; SPAC1486.01.
GeneID; 2542886; -.
KEGG; spo:SPAC1486.01; -.
EuPathDB; FungiDB:SPAC1486.01; -.
PomBase; SPAC1486.01; sod2.
HOGENOM; HOG000013583; -.
KO; K04564; -.
OMA; KWGSFDK; -.
OrthoDB; EOG092C4NQ6; -.
PhylomeDB; Q9UQX0; -.
Reactome; R-SPO-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:Q9UQX0; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
GO; GO:0005739; C:mitochondrion; IDA:PomBase.
GO; GO:0030145; F:manganese ion binding; IDA:PomBase.
GO; GO:0004784; F:superoxide dismutase activity; IDA:PomBase.
GO; GO:0001324; P:age-dependent response to oxidative stress involved in chronological cell aging; IMP:PomBase.
GO; GO:0019430; P:removal of superoxide radicals; IMP:PomBase.
Gene3D; 1.10.287.990; -; 1.
Gene3D; 2.40.500.20; -; 1.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
InterPro; IPR036324; Mn/Fe_SOD_N_sf.
InterPro; IPR036314; SOD_C_sf.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Manganese;
Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1 21 Mitochondrion.
{ECO:0000269|PubMed:11350071}.
CHAIN 22 218 Superoxide dismutase [Mn], mitochondrial.
/FTId=PRO_0000032887.
METAL 50 50 Manganese. {ECO:0000250}.
METAL 96 96 Manganese. {ECO:0000250}.
METAL 181 181 Manganese. {ECO:0000250}.
METAL 185 185 Manganese. {ECO:0000250}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
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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