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Database: UniProt/SWISS-PROT
Entry: SODC_DROPS
LinkDB: SODC_DROPS
Original site: SODC_DROPS 
ID   SODC_DROPS              Reviewed;         152 AA.
AC   Q95086; Q2LZ29;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 116.
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};
GN   ORFNames=GA11202 {ECO:0000312|FlyBase:FBgn0016313};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-121.
RC   STRAIN=NDSSC 14011-0121.43;
RX   PubMed=9007023; DOI=10.1006/mpev.1996.0375;
RA   Barrio E., Ayala F.J.;
RT   "Evolution of the Drosophila obscura species group inferred from the
RT   Gpdh and Sod genes.";
RL   Mol. Phylogenet. Evol. 7:79-93(1997).
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; 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; CH379069; EAL29680.2; -; Genomic_DNA.
DR   EMBL; U47871; AAB50303.1; -; Genomic_DNA.
DR   RefSeq; XP_001353944.2; XM_001353908.3.
DR   ProteinModelPortal; Q95086; -.
DR   SMR; Q95086; -.
DR   STRING; 7237.FBpp0275438; -.
DR   EnsemblMetazoa; FBtr0277000; FBpp0275438; FBgn0016313.
DR   GeneID; 4813641; -.
DR   KEGG; dpo:Dpse_GA11202; -.
DR   FlyBase; FBgn0016313; Dpse\Sod.
DR   InParanoid; Q95086; -.
DR   KO; K04565; -.
DR   OMA; MAMKAVC; -.
DR   Proteomes; UP000001819; Partially assembled WGS sequence.
DR   Bgee; FBgn0016313; Expressed in 5 organ(s), highest expression level in female reproductive system.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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; Complete proteome; Copper; Cytoplasm; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164092.
FT   METAL        44     44       Copper; catalytic. {ECO:0000250}.
FT   METAL        46     46       Copper; catalytic. {ECO:0000250}.
FT   METAL        61     61       Copper; catalytic. {ECO:0000250}.
FT   METAL        61     61       Zinc; structural. {ECO:0000250}.
FT   METAL        69     69       Zinc; structural. {ECO:0000250}.
FT   METAL        78     78       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL       118    118       Copper; catalytic. {ECO:0000250}.
FT   CONFLICT     33     33       V -> G (in Ref. 2; AAB50303).
FT                                {ECO:0000305}.
SQ   SEQUENCE   152 AA;  15628 MW;  5D3D57E5E56E19C1 CRC64;
     MVKAVCVING DAKGTVFFEQ ETSEAPVKVT GEVLGLAKGL HGFHVHEFGD NTNGCMSSGP
     HFNPRNKEHG APTDENRHLG DLGNIQAAGD SPTAVSITDS KITLFGADSI IGRTVVVHAD
     ADDLGKGGHE LSKTTGNAGA RIGCGVIGIA KI
//
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