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   27-MAR-2024, entry version 152.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
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; Schizosaccharomycetaceae;
OC   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., 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   [3]
RP   PROTEIN SEQUENCE OF 22-34, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   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 its
RT   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 BY
RP   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 systems.
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P0A0J3};
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. {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. {ECO:0000269|PubMed:11350071}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {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   AlphaFoldDB; Q9UQX0; -.
DR   SMR; Q9UQX0; -.
DR   BioGRID; 279331; 34.
DR   STRING; 284812.Q9UQX0; -.
DR   iPTMnet; Q9UQX0; -.
DR   MaxQB; Q9UQX0; -.
DR   PaxDb; 4896-SPAC1486-01-1; -.
DR   EnsemblFungi; SPAC1486.01.1; SPAC1486.01.1:pep; SPAC1486.01.
DR   GeneID; 2542886; -.
DR   KEGG; spo:SPAC1486.01; -.
DR   PomBase; SPAC1486.01; sod2.
DR   VEuPathDB; FungiDB:SPAC1486.01; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_031625_2_0_1; -.
DR   InParanoid; Q9UQX0; -.
DR   OMA; DSLINWD; -.
DR   PhylomeDB; Q9UQX0; -.
DR   Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q9UQX0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   ExpressionAtlas; Q9UQX0; differential.
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; IDA:PomBase.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:PomBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:PomBase.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
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   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Direct protein sequencing; Manganese; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:11350071"
FT   CHAIN           22..218
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032887"
FT   BINDING         50
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         96
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         181
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         185
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="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
//