ID   SODC_DROVI              Reviewed;         153 AA.
AC   P10791; B4LC46;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P61851};
DE            EC=1.15.1.1;
DE   AltName: Full=Superoxide dismutase 1 {ECO:0000250|UniProtKB:P61851};
GN   Name=Sod1 {ECO:0000250|UniProtKB:P61851};
GN   Synonyms=Sod {ECO:0000250|UniProtKB:P61851}; ORFNames=GJ11304;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2928122; DOI=10.1093/nar/17.5.2133;
RA   Kwiatowski J., Ayala F.J.;
RT   "Drosophila virilis Cu-Zn superoxide dismutase gene sequence.";
RL   Nucleic Acids Res. 17:2133-2133(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(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; X13831; CAA32060.1; -; Genomic_DNA.
DR   EMBL; CH940647; EDW70874.1; -; Genomic_DNA.
DR   PIR; S03606; S03606.
DR   RefSeq; XP_002048532.1; XM_002048496.2.
DR   AlphaFoldDB; P10791; -.
DR   SMR; P10791; -.
DR   STRING; 7244.FBpp0225721; -.
DR   EnsemblMetazoa; FBtr0227229; FBpp0225721; FBgn0013096.
DR   GeneID; 6624514; -.
DR   KEGG; dvi:6624514; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; P10791; -.
DR   OMA; AQRGFHI; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; P10791; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001306; P:age-dependent response to oxidative stress; IEA:EnsemblMetazoa.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR   GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:EnsemblMetazoa.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IEA:EnsemblMetazoa.
DR   GO; GO:2000331; P:regulation of terminal button organization; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..153
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164098"
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   DISULFID        56..145
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  15770 MW;  26E121BBF6B7A25C CRC64;
     MVVKAVCVIN GDAKGTVFFE QEGEGCPVKV TGEVTGLAKG QHGFHVHEFG DNTNGCMSSG
     PHFNPYQKEH GAPTDENRHL GDLGNIIANG DGPTPVNICD CKITLLGANS IIGRTVVVHA
     DPDDLGKGGH ELSKTTGNAG ARIGCGVIGI AKI