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Database: UniProt/SWISS-PROT
Entry: SODC_DROME
LinkDB: SODC_DROME
Original site: SODC_DROME 
ID   SODC_DROME              Reviewed;         153 AA.
AC   P61851; P00444; Q27770; Q9VTF6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 134.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000303|PubMed:3110743};
DE            EC=1.15.1.1;
DE   AltName: Full=Superoxide dismutase 1 {ECO:0000312|FlyBase:FBgn0003462};
GN   Name=Sod1 {ECO:0000312|FlyBase:FBgn0003462};
GN   Synonyms=Sod {ECO:0000303|PubMed:3110743};
GN   ORFNames=CG11793 {ECO:0000312|FlyBase:FBgn0003462};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3110743; DOI=10.1093/nar/15.13.5483;
RA   Seto N.O.L., Hayashi S., Tener G.M.;
RT   "Drosophila Cu-Zn superoxide dismutase cDNA sequence.";
RL   Nucleic Acids Res. 15:5483-5483(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3122185; DOI=10.1093/nar/15.24.10601;
RA   Seto N.O.L., Hayashi S., Tener G.M.;
RT   "The sequence of the Cu-Zn superoxide dismutase gene of Drosophila.";
RL   Nucleic Acids Res. 15:10601-10601(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2470654; DOI=10.1016/0378-1119(89)90385-5;
RA   Seto N.O., Hayashi S., Tener G.M.;
RT   "Cloning, sequence analysis and chromosomal localization of the Cu-Zn
RT   superoxide dismutase gene of Drosophila melanogaster.";
RL   Gene 75:85-92(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   PubMed=2493630; DOI=10.1093/nar/17.3.1264;
RA   Kwiatowski J., Patel M., Ayala F.J.;
RT   "Drosophila melanogaster Cu,Zn superoxide dismutase gene sequence.";
RL   Nucleic Acids Res. 17:1264-1264(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Canton-S;
RA   Phillips J.P.;
RL   Submitted (DEC-1989) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [7]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-153.
RX   PubMed=3919383; DOI=10.1073/pnas.82.3.824;
RA   Lee Y.M., Friedman D.J., Ayala F.J.;
RT   "Superoxide dismutase: an evolutionary puzzle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:824-828(1985).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-153.
RX   PubMed=3929689; DOI=10.1016/0003-9861(85)90583-1;
RA   Lee Y.M., Friedman D.J., Ayala F.J.;
RT   "Complete amino acid sequence of copper-zinc superoxide dismutase from
RT   Drosophila melanogaster.";
RL   Arch. Biochem. Biophys. 241:577-589(1985).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-153.
RX   PubMed=8013910;
RA   Hudson R.R., Bailey K., Skarecky D., Kwiatowski J., Ayala F.J.;
RT   "Evidence for positive selection in the superoxide dismutase (Sod)
RT   region of Drosophila melanogaster.";
RL   Genetics 136:1329-1340(1994).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-122.
RC   STRAIN=Canton-S;
RX   PubMed=3128462; DOI=10.1016/0378-1119(87)90203-4;
RA   Kirkland K.C., Phillips J.P.;
RT   "Isolation and chromosomal localization of genomic DNA sequences
RT   coding for cytoplasmic superoxide dismutase from Drosophila
RT   melanogaster.";
RL   Gene 61:415-419(1987).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53 AND SER-59, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
RA   Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy
RT   for (quantitative) phosphoproteomics: application to Drosophila
RT   melanogaster Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; Y00367; CAA68443.1; -; mRNA.
DR   EMBL; Z19591; CAA79639.1; -; Genomic_DNA.
DR   EMBL; M24421; AAA28906.1; -; Genomic_DNA.
DR   EMBL; X13780; CAA32028.1; -; Genomic_DNA.
DR   EMBL; X17332; CAA35210.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF50095.1; -; Genomic_DNA.
DR   EMBL; AY071435; AAL49057.1; -; mRNA.
DR   EMBL; S72589; AAD14963.2; -; Genomic_DNA.
DR   EMBL; M18823; AAA28905.1; -; Genomic_DNA.
DR   PIR; S02725; DSFFCZ.
DR   RefSeq; NP_476735.1; NM_057387.5.
DR   UniGene; Dm.926; -.
DR   ProteinModelPortal; P61851; -.
DR   SMR; P61851; -.
DR   BioGrid; 64623; 62.
DR   IntAct; P61851; 3.
DR   iPTMnet; P61851; -.
DR   PRIDE; P61851; -.
DR   EnsemblMetazoa; FBtr0076229; FBpp0075958; FBgn0003462.
DR   GeneID; 39251; -.
DR   KEGG; dme:Dmel_CG11793; -.
DR   CTD; 6647; -.
DR   FlyBase; FBgn0003462; Sod1.
DR   GeneTree; ENSGT00940000155551; -.
DR   InParanoid; P61851; -.
DR   KO; K04565; -.
DR   OMA; MAMKAVC; -.
DR   PhylomeDB; P61851; -.
DR   Reactome; R-DME-114608; Platelet degranulation.
DR   Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR   GenomeRNAi; 39251; -.
DR   PRO; PR:P61851; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0003462; Expressed in 38 organ(s), highest expression level in antenna.
DR   ExpressionAtlas; P61851; baseline and differential.
DR   Genevisible; P61851; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:FlyBase.
DR   GO; GO:0016209; F:antioxidant activity; NAS:FlyBase.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR   GO; GO:0004784; F:superoxide dismutase activity; IMP:FlyBase.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:FlyBase.
DR   GO; GO:0007568; P:aging; TAS:FlyBase.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR   GO; GO:1903146; P:regulation of autophagy of mitochondrion; IGI:FlyBase.
DR   GO; GO:2000331; P:regulation of terminal button organization; IMP:FlyBase.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3919383,
FT                                ECO:0000269|PubMed:3929689}.
FT   CHAIN         2    153       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164085.
FT   METAL        45     45       Copper; catalytic.
FT   METAL        47     47       Copper; catalytic.
FT   METAL        62     62       Copper; catalytic.
FT   METAL        62     62       Zinc; structural.
FT   METAL        70     70       Zinc; structural.
FT   METAL        79     79       Zinc; structural.
FT   METAL        82     82       Zinc; structural.
FT   METAL       119    119       Copper; catalytic.
FT   MOD_RES      53     53       Phosphothreonine.
FT                                {ECO:0000269|PubMed:17372656}.
FT   MOD_RES      59     59       Phosphoserine.
FT                                {ECO:0000269|PubMed:17372656}.
FT   DISULFID     56    145
FT   CONFLICT     97     97       N -> K (in Ref. 4; CAA35210, 11; AAD14963
FT                                and 12; AAA28905). {ECO:0000305}.
SQ   SEQUENCE   153 AA;  15699 MW;  4A6AAAA1EB545E70 CRC64;
     MVVKAVCVIN GDAKGTVFFE QESSGTPVKV SGEVCGLAKG LHGFHVHEFG DNTNGCMSSG
     PHFNPYGKEH GAPVDENRHL GDLGNIEATG DCPTKVNITD SKITLFGADS IIGRTVVVHA
     DADDLGQGGH ELSKSTGNAG ARIGCGVIGI AKV
//
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