SODC_CANLF
ID SODC_CANLF Reviewed; 153 AA.
AC Q8WNN6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12140271; DOI=10.1093/jhered/93.2.119;
RA Green S.L., Tolwani R.J., Varma S., Quignon P., Galibert F., Cork L.C.;
RT "Structure, chromosomal location, and analysis of the canine Cu/Zn
RT superoxide dismutase (SOD1) gene.";
RL J. Hered. 93:119-124(2002).
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic
CC activity. {ECO:0000250}.
CC -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC {ECO:0000250|UniProtKB:P00441}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF346417; AAL61608.1; -; mRNA.
DR RefSeq; NP_001003035.1; NM_001003035.1.
DR STRING; 9615.ENSCAFP00000013012; -.
DR PRIDE; Q8WNN6; -.
DR GeneID; 403559; -.
DR KEGG; cfa:403559; -.
DR CTD; 6647; -.
DR InParanoid; Q8WNN6; -.
DR OrthoDB; 1574423at2759; -.
DR Proteomes; UP000002254; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
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; PS00332; SOD_CU_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antioxidant; Copper; Cytoplasm; Disulfide bond; Lipoprotein;
KW Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164051"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 91
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 57..146
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 15913 MW; 0D7900E59C57E6B0 CRC64;
MEMKAVCVLK GQGPVEGTIH FVQKGSGPVV VSGTITGLTE GEHGFHVHQF EDXTQGCTSA
GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE DSLIALSGDY SIIGRTMVVH
EKRDDLGKGD NEESTQTGNA GSRLACGVIG IAQ
