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Database: UniProt/SWISS-PROT
Entry: SODC_DANRE
LinkDB: SODC_DANRE
Original site: SODC_DANRE 
ID   SODC_DANRE              Reviewed;         154 AA.
AC   O73872;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-MAY-2018, entry version 131.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=sod1; Synonyms=cuzn;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ken C.F., Lin C.T.;
RT   "Cloning and characterization of a cDNA for Cu/Zn-superoxide dismutase
RT   from zebrafish.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; Y12236; CAA72925.1; -; mRNA.
DR   EMBL; BC055516; AAH55516.1; -; mRNA.
DR   RefSeq; NP_571369.1; NM_131294.1.
DR   UniGene; Dr.75822; -.
DR   ProteinModelPortal; O73872; -.
DR   SMR; O73872; -.
DR   STRING; 7955.ENSDARP00000064375; -.
DR   PaxDb; O73872; -.
DR   PRIDE; O73872; -.
DR   Ensembl; ENSDART00000064376; ENSDARP00000064375; ENSDARG00000043848.
DR   GeneID; 30553; -.
DR   KEGG; dre:30553; -.
DR   CTD; 6647; -.
DR   ZFIN; ZDB-GENE-990415-258; sod1.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; O73872; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; O73872; -.
DR   TreeFam; TF105131; -.
DR   Reactome; R-DRE-114608; Platelet degranulation.
DR   Reactome; R-DRE-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:O73872; -.
DR   Proteomes; UP000000437; Chromosome 10.
DR   Bgee; ENSDARG00000043848; -.
DR   ExpressionAtlas; O73872; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:ZFIN.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IMP:ZFIN.
DR   GO; GO:0010038; P:response to metal ion; IDA:ZFIN.
DR   GO; GO:0051597; P:response to methylmercury; IDA:ZFIN.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:ZFIN.
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   Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate;
KW   Reference proteome; Zinc.
FT   CHAIN         1    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164071.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; structural. {ECO:0000250}.
FT   METAL        72     72       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL        84     84       Zinc; structural. {ECO:0000250}.
FT   METAL       121    121       Copper; catalytic. {ECO:0000250}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
SQ   SEQUENCE   154 AA;  15953 MW;  62F44CA146C5057C CRC64;
     MVNKAVCVLK GTGEVTGTVY FNQEGEKKPV KVTGEITGLT PGKHGFHVHA FGDNTNGCIS
     AGPHFNPHDK THGGPTDSVR HVGDLGNVTA DASGVAKIEI EDAMLTLSGQ HSIIGRTMVI
     HEKEDDLGKG GNEESLKTGN AGGRLACGVI GITQ
//
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