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Database: UniProt/SWISS-PROT
Entry: SODC_SCHPO
LinkDB: SODC_SCHPO
Original site: 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   28-FEB-2018, entry version 144.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=sod1; ORFNames=SPAC821.10c;
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 [MRNA].
RA   O'Dee K.M., Snider M.D.;
RT   "Nucleotide sequence of Schizosacharomyces 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
RT   cell 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.,
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).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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   ProteinModelPortal; P28758; -.
DR   SMR; P28758; -.
DR   BioGrid; 278604; 15.
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   EuPathDB; FungiDB:SPAC821.10c; -.
DR   PomBase; SPAC821.10c; sod1.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; P28758; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG092C578I; -.
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:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:PomBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0008270; F:zinc ion binding; IBA:GO_Central.
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; IC:PomBase.
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; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164127.
FT   METAL        47     47       Copper. {ECO:0000250}.
FT   METAL        49     49       Copper. {ECO:0000250}.
FT   METAL        64     64       Copper. {ECO:0000250}.
FT   METAL        64     64       Zinc. {ECO:0000250}.
FT   METAL        72     72       Zinc. {ECO:0000250}.
FT   METAL        81     81       Zinc. {ECO:0000250}.
FT   METAL        84     84       Zinc. {ECO:0000250}.
FT   METAL       121    121       Copper. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
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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