ID SODC_XENTR Reviewed; 151 AA. AC Q0IIW3; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P00441}; DE EC=1.15.1.1; GN Name=sod1; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] {ECO:0000312|EMBL:AAI21541.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=N6 {ECO:0000312|EMBL:AAI21541.1}; RC TISSUE=Oviduct {ECO:0000312|EMBL:AAI21541.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2006) 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 {ECO:0000250|UniProtKB:P15107}. 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 Evidence={ECO:0000250|UniProtKB:P15107}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P15107}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P15107}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P15107}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15107}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00441}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15107}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC121540; AAI21541.1; -; mRNA. DR RefSeq; NP_001016252.1; NM_001016252.2. DR AlphaFoldDB; Q0IIW3; -. DR SMR; Q0IIW3; -. DR STRING; 8364.ENSXETP00000002201; -. DR PaxDb; 8364-ENSXETP00000015994; -. DR DNASU; 549006; -. DR Ensembl; ENSXETT00000105673; ENSXETP00000111899; ENSXETG00000047863. DR GeneID; 549006; -. DR KEGG; xtr:549006; -. DR AGR; Xenbase:XB-GENE-1006488; -. DR Xenbase; XB-GENE-1006488; sod1. DR eggNOG; KOG0441; Eukaryota. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; Q0IIW3; -. DR OMA; AQRGFHI; -. DR OrthoDB; 3470597at2759; -. DR Reactome; R-XTR-114608; Platelet degranulation. DR Reactome; R-XTR-3299685; Detoxification of Reactive Oxygen Species. DR Proteomes; UP000008143; Chromosome 2. DR Bgee; ENSXETG00000007350; Expressed in mesonephros and 16 other cell types or tissues. DR ExpressionAtlas; Q0IIW3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. 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; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 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 INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P15107" FT CHAIN 2..151 FT /note="Superoxide dismutase [Cu-Zn]" FT /evidence="ECO:0000250|UniProtKB:P15107" FT /id="PRO_0000392433" FT BINDING 45 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 62 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P15107" FT BINDING 118 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P15107" FT LIPID 6 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 56..144 FT /evidence="ECO:0000250|UniProtKB:P15107" SQ SEQUENCE 151 AA; 15698 MW; 6E4E5F8260D4CD4B CRC64; MVRAVCVLAG SGDVKGVVHF QQQDEGPVTV EGKIYGLTDG KHGFHIHEFG DNTNGCISAG PHFNPESKTH GAPEDAVRHV GDLGNVTAKD GVAEFKLTDS LISLKGNHSI IGRCAVVHEK EDDLGKGGND ESLKTGNAGG RLACGVIGLC Q //