ID   A3KLR9_BOVIN            Unreviewed;       241 AA.
AC   A3KLR9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=ECSOD {ECO:0000313|EMBL:AAY28415.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAY28415.1};
RN   [1] {ECO:0000313|EMBL:AAY28415.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AAY28415.1};
RA   Kristensen T., Enghild J.J.;
RT   "Structural studies of bovine extracellular superoxide dismutase.";
RL   Submitted (MAR-2005) 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: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. {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. {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; AY957404; AAY28415.1; -; mRNA.
DR   RefSeq; NP_001076079.1; NM_001082610.1.
DR   RefSeq; XP_005207846.1; XM_005207789.3.
DR   RefSeq; XP_015327049.1; XM_015471563.1.
DR   AlphaFoldDB; A3KLR9; -.
DR   SMR; A3KLR9; -.
DR   GeneID; 532481; -.
DR   KEGG; bta:532481; -.
DR   CTD; 6649; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_3_1_1; -.
DR   TreeFam; TF105133; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:SF77; EXTRACELLULAR 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..241
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014083576"
FT   DOMAIN          79..211
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   241 AA;  26177 MW;  E5FA9F77770A4D49 CRC64;
     MLALLCASVV LVAYASADQI QQQMGSNTEE QIRDMHAKVT EIWQEMMQRQ AAAIDPDAAL
     HAVCRVLPSA TLEAEQPRVS GLVLFRQLRP GALLEAFFHL EGFPNEPNGT NRAIHVHQFG
     DLSQGCDSTG PHYNPMSVPH PQHPGDFGNF AVRDGQVWKY RSGLAASLTG PHSIAGRAVV
     VHAGEDDMGR GGNQASLENG NAGRRLACCV VGLCGPGPWA RQTQEHAERK KRRRESECKA
     V
//