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Database: UniProt/SWISS-PROT
Entry: SODC_XENTR
LinkDB: SODC_XENTR
Original site: 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   30-AUG-2017, entry version 77.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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.
CC       {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}.
CC       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000255}.
DR   EMBL; BC121540; AAI21541.1; -; mRNA.
DR   RefSeq; NP_001016252.1; NM_001016252.2.
DR   UniGene; Str.1999; -.
DR   ProteinModelPortal; Q0IIW3; -.
DR   SMR; Q0IIW3; -.
DR   STRING; 8364.ENSXETP00000015994; -.
DR   PaxDb; Q0IIW3; -.
DR   GeneID; 549006; -.
DR   KEGG; xtr:549006; -.
DR   CTD; 6647; -.
DR   Xenbase; XB-GENE-1006488; sod1.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; Q0IIW3; -.
DR   KO; K04565; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P15107}.
FT   CHAIN         2    151       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000250|UniProtKB:P15107}.
FT                                /FTId=PRO_0000392433.
FT   METAL        45     45       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        47     47       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        62     62       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        62     62       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        70     70       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        79     79       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL        82     82       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   METAL       118    118       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P15107}.
FT   LIPID         6      6       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     56    144       {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
//
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