ID   SODC_PAROL              Reviewed;          26 AA.
AC   P83129;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1 {ECO:0000305|PubMed:11290457};
DE   Flags: Fragment;
GN   Name=sod1;
OS   Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC   Paralichthys.
OX   NCBI_TaxID=8255 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-26, CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Hepatopancreas;
RX   PubMed=11290457; DOI=10.1016/s1096-4959(01)00299-8;
RA   Osatomi K., Masuda Y., Hara K., Ishihara T.;
RT   "Purification, N-terminal amino acid sequence, and some properties of
RT   Cu,Zn-superoxide dismutase from Japanese flounder (Paralichthys olivaceus)
RT   hepato-pancreas.";
RL   Comp. Biochem. Physiol. 128B:751-760(2001).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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:0000305|PubMed:11290457};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC         Evidence={ECO:0000305|PubMed:11290457};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11290457}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83129; -.
DR   SMR; P83129; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; TAS:UniProtKB.
PE   1: Evidence at protein level;
KW   Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Lipoprotein;
KW   Metal-binding; Nucleus; Oxidoreductase; Palmitate; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11290457"
FT   CHAIN           2..>26
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164073"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  2735 MW;  768DE680740857C5 CRC64;
     MALKAVCVLK GAGETSGTVH FEQEDN