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SODC_SCHPO
ID   SODC_SCHPO              Reviewed;         154 AA.
AC   P28758;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P85978};
GN   Name=sod1; ORFNames=SPAC821.10c;
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 [MRNA].
RA   O'Dee K.M., Snider M.D.;
RT   "Nucleotide sequence of Schizosaccharomyces pombe superoxide dismutase
RT   cDNA.";
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kawamukai M.;
RT   "S.pombe superoxide dismutase.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=12359231; DOI=10.1016/s0006-291x(02)02290-8;
RA   Lee J., Kwon E.-S., Kim D.-W., Cha J., Roe J.-H.;
RT   "Regulation and the role of Cu,Zn-containing superoxide dismutase in cell
RT   cycle progression of Schizosaccharomyces pombe.";
RL   Biochem. Biophys. Res. Commun. 297:854-862(2002).
RN   [4]
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).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000250|UniProtKB:P00442}.
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:P85978};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00445};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00445};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P85978}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X66722; CAA47254.1; -; mRNA.
DR   EMBL; AB016217; BAA31741.1; -; mRNA.
DR   EMBL; CU329670; CAB57444.1; -; Genomic_DNA.
DR   EMBL; AF069075; AAC99342.1; -; Genomic_DNA.
DR   PIR; S24971; S24971.
DR   RefSeq; NP_593163.1; NM_001018561.2.
DR   AlphaFoldDB; P28758; -.
DR   SMR; P28758; -.
DR   BioGRID; 278604; 16.
DR   IntAct; P28758; 2.
DR   MINT; P28758; -.
DR   STRING; 4896.SPAC821.10c.1; -.
DR   iPTMnet; P28758; -.
DR   MaxQB; P28758; -.
DR   PaxDb; P28758; -.
DR   PRIDE; P28758; -.
DR   EnsemblFungi; SPAC821.10c.1; SPAC821.10c.1:pep; SPAC821.10c.
DR   GeneID; 2542128; -.
DR   KEGG; spo:SPAC821.10c; -.
DR   PomBase; SPAC821.10c; sod1.
DR   VEuPathDB; FungiDB:SPAC821.10c; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; P28758; -.
DR   OMA; AQRGFHI; -.
DR   PhylomeDB; P28758; -.
DR   Reactome; R-SPO-114608; Platelet degranulation.
DR   Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P28758; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; ISS:PomBase.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IMP:PomBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:PomBase.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; ISS:PomBase.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:PomBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   CHAIN           2..154
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164127"
FT   BINDING         47
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         49
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         64
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         121
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
FT   DISULFID        58..147
FT                   /evidence="ECO:0000250|UniProtKB:P00445"
SQ   SEQUENCE   154 AA;  15913 MW;  BB14EFDD4108938F CRC64;
     MVRAVAVLRG DSKVSGVVTF EQVDQNSQVS VIVDLVGNDA NAKRGFHIHQ FGDNTNGCTS
     AGPHFNPEGK THGDRTAAVR HVGDLGNLES DAQGNIKTTF SDSVISLFGA NSIIGRTIVI
     HAGEDDLGKG TSEESLKTGN AGARNACGVI GIAV
 
 
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