SODM_SCHPO
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 03-AUG-2022, entry version 145.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4896.SPAC1486.01.1; -.
DR iPTMnet; Q9UQX0; -.
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; sod2.
DR VEuPathDB; FungiDB:SPAC1486.01; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_2_0_1; -.
DR OMA; KWGSFDK; -.
DR PhylomeDB; Q9UQX0; -.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q9UQX0; -.
DR Proteomes; UP000002485; Chromosome I.
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; -; 1.
DR Gene3D; 3.55.40.20; -; 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 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 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
