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Database: UniProt
Entry: Q27538_CAEEL
LinkDB: Q27538_CAEEL
Original site: Q27538_CAEEL 
ID   Q27538_CAEEL            Unreviewed;       178 AA.
AC   Q27538;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   10-APR-2019, entry version 147.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sod-5 {ECO:0000313|EMBL:CCD61672.1,
GN   ECO:0000313|WormBase:ZK430.3};
GN   ORFNames=CELE_ZK430.3 {ECO:0000313|EMBL:CCD61672.1}, ZK430.3
GN   {ECO:0000313|WormBase:ZK430.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD61672.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CCD61672.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD61672.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; BX284602; CCD61672.1; -; Genomic_DNA.
DR   PIR; JE0098; JE0098.
DR   PIR; T27860; T27860.
DR   RefSeq; NP_494779.1; NM_062378.3.
DR   UniGene; Cel.13783; -.
DR   ProteinModelPortal; Q27538; -.
DR   SMR; Q27538; -.
DR   STRING; 6239.ZK430.3; -.
DR   PaxDb; Q27538; -.
DR   PeptideAtlas; Q27538; -.
DR   EnsemblMetazoa; ZK430.3; ZK430.3; WBGene00007036.
DR   GeneID; 173776; -.
DR   KEGG; cel:CELE_ZK430.3; -.
DR   UCSC; ZK430.3; c. elegans.
DR   CTD; 173776; -.
DR   WormBase; ZK430.3; CE05080; WBGene00007036; sod-5.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000168521; -.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; Q27538; -.
DR   KO; K04565; -.
DR   OMA; MAKAVCT; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; Q27538; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00007036; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; 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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; 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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001940};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q27538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       32    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   178 AA;  18507 MW;  7A7D93D8E8DB5329 CRC64;
     MDILSDIANA VLPQDVVSKV ESKRAVAVLR GTAVFGTVWL TQKAEGEETE FEGEIKGLSP
     GLHGFHIHQY GDSTDGCTSA GPHFNPCKMN HGGRDSVVRH VGDLGNVEAG ADGVAKIKFS
     DKVVSLFGAN TVIGRSMVVH VDRDDLGQGI DDKAEESLKT GNAGARAACG VIALAAPA
//
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