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 03-AUG-2022, entry version 147.
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 Danionidae; Danioninae; 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 from
RT 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:
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 {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; Y12236; CAA72925.1; -; mRNA.
DR EMBL; BC055516; AAH55516.1; -; mRNA.
DR RefSeq; NP_571369.1; NM_131294.1.
DR AlphaFoldDB; 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 GeneTree; ENSGT00940000155551; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; O73872; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
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; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000043848; Expressed in testis and 25 other tissues.
DR ExpressionAtlas; O73872; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:ZFIN.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:ZFIN.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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; Copper; Cytoplasm; Disulfide bond; Lipoprotein; Metal-binding;
KW Nucleus; Oxidoreductase; Palmitate; Reference proteome; Zinc.
FT CHAIN 1..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164071"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 58..147
FT /evidence="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
