SODC_XENTR
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 03-AUG-2022, entry version 95.
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}.
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DR EMBL; BC121540; AAI21541.1; -; mRNA.
DR RefSeq; NP_001016252.1; NM_001016252.2.
DR AlphaFoldDB; Q0IIW3; -.
DR SMR; Q0IIW3; -.
DR PaxDb; Q0IIW3; -.
DR DNASU; 549006; -.
DR Ensembl; ENSXETT00000015994; ENSXETP00000015994; ENSXETG00000007350.
DR GeneID; 549006; -.
DR KEGG; xtr:549006; -.
DR CTD; 6647; -.
DR Xenbase; XB-GENE-1006488; sod1.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; Q0IIW3; -.
DR OrthoDB; 1574423at2759; -.
DR Reactome; R-XTR-114608; Platelet degranulation.
DR Reactome; R-XTR-3299685; Detoxification of Reactive Oxygen Species.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007350; Expressed in mesonephros and 16 other tissues.
DR ExpressionAtlas; Q0IIW3; 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; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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 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
