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 03-AUG-2022, entry version 150.
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA 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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT 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., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA 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; DOI=10.1093/genetics/136.4.1329;
RA Hudson R.R., Bailey K., Skarecky D., Kwiatowski J., Ayala F.J.;
RT "Evidence for positive selection in the superoxide dismutase (Sod) region
RT 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 coding for
RT cytoplasmic superoxide dismutase from Drosophila 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., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT 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}.
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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 AlphaFoldDB; P61851; -.
DR SMR; P61851; -.
DR BioGRID; 64623; 64.
DR IntAct; P61851; 3.
DR STRING; 7227.FBpp0305736; -.
DR iPTMnet; P61851; -.
DR PRIDE; P61851; -.
DR DNASU; 39251; -.
DR EnsemblMetazoa; FBtr0076229; FBpp0075958; FBgn0003462.
DR GeneID; 39251; -.
DR KEGG; dme:Dmel_CG11793; -.
DR CTD; 6647; -.
DR FlyBase; FBgn0003462; Sod1.
DR VEuPathDB; VectorBase:FBgn0003462; -.
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000155551; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P61851; -.
DR OMA; AQRGFHI; -.
DR PhylomeDB; P61851; -.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; P61851; -.
DR BioGRID-ORCS; 39251; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39251; -.
DR PRO; PR:P61851; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003462; Expressed in mouthpart and 31 other tissues.
DR ExpressionAtlas; P61851; baseline and differential.
DR Genevisible; P61851; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005777; C:peroxisome; IDA: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:0001306; P:age-dependent response to oxidative stress; IMP: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:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
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; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3919383,
FT ECO:0000269|PubMed:3929689"
FT CHAIN 2..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164085"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT DISULFID 56..145
FT CONFLICT 97
FT /note="N -> K (in Ref. 4; CAA35210, 11; AAD14963 and 12;
FT AAA28905)"
FT /evidence="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
