ID   SODC_CAVPO              Reviewed;         153 AA.
AC   P33431;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 163.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P00441};
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P00441};
DE            EC=1.8.-.- {ECO:0000250|UniProtKB:P00441};
DE   AltName: Full=Hydrogen sulfide oxidase {ECO:0000250|UniProtKB:P00441};
GN   Name=SOD1 {ECO:0000250|UniProtKB:P00441};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Lung;
RX   PubMed=8597602; DOI=10.1016/0167-4781(95)00214-6;
RA   Yuan H.T., Bingle C.D., Kelly F.J.;
RT   "Differential patterns of antioxidant enzyme mRNA expression in guinea pig
RT   lung and liver during development.";
RL   Biochim. Biophys. Acta 1305:163-171(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-153.
RC   TISSUE=Liver;
RX   PubMed=8240718; DOI=10.1515/bchm3.1993.374.7-12.641;
RA   Wolf B., Reinecke K., Aumann K.-D., Brigelius-Flohe R., Flohe L.;
RT   "Taxonomical classification of the guinea pig based on its Cu/Zn superoxide
RT   dismutase sequence.";
RL   Biol. Chem. Hoppe-Seyler 374:641-649(1993).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.Catalyzes the oxidation
CC       of hydrogen sulfide (H2S) to sulfate, playing an important role in
CC       detoxifying H2S and limiting the accumulation of reactive sulfur
CC       species (RSS) such as persulfides and polysulfides.
CC       {ECO:0000250|UniProtKB:P00441}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 superoxide + 2 H(+) = 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:0000250|UniProtKB:P00441};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + 2 O2 = sulfate + H(+);
CC         Xref=Rhea:RHEA:85007, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:29919;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:85008;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00441};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00441};
CC   -!- SUBUNIT: Homodimer; non-disulfide-linked (By similarity). Heterodimer
CC       with CCS. The heterodimer CCS:SOD1 interacts with SLC31A1; this
CC       heterotrimer is Cu(1+)-mediated and its maintenance is regulated
CC       through SOD1 activation (By similarity). {ECO:0000250|UniProtKB:P00441,
CC       ECO:0000250|UniProtKB:P08228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}. Nucleus
CC       {ECO:0000250|UniProtKB:P00441}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic
CC       activity. {ECO:0000250|UniProtKB:P00441}.
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; U39844; AAC52720.1; -; mRNA.
DR   PIR; S36108; S36108.
DR   RefSeq; XP_003467296.1; XM_003467248.5.
DR   AlphaFoldDB; P33431; -.
DR   SMR; P33431; -.
DR   FunCoup; P33431; 1819.
DR   STRING; 10141.ENSCPOP00000012815; -.
DR   Ensembl; ENSCPOT00000014365.3; ENSCPOP00000012815.3; ENSCPOG00000014223.4.
DR   GeneID; 100135622; -.
DR   KEGG; cpoc:100135622; -.
DR   CTD; 6647; -.
DR   VEuPathDB; HostDB:ENSCPOG00000014223; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   GeneTree; ENSGT00940000155551; -.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; P33431; -.
DR   OMA; ACGKTHM; -.
DR   OrthoDB; 2015551at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000014223; Expressed in adrenal gland and 13 other cell types or tissues.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:1902694; C:superoxide dismutase copper chaperone complex; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
DR   GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR   GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   FunFam; 2.60.40.200:FF:000001; Superoxide dismutase [Cu-Zn]; 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/SOD-chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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   1: Evidence at protein level;
KW   Acetylation; Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase;
KW   Palmitate; Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00442,
FT                   ECO:0000269|PubMed:8240718"
FT   CHAIN           2..153
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164053"
FT   BINDING         46
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         48
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         63
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         120
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00442"
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         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         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07632"
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   MOD_RES         136
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08228"
FT   MOD_RES         136
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08228"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   DISULFID        57..146
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   CONFLICT        103..104
FT                   /note="LI -> IL (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   153 AA;  15670 MW;  B82C13327FACF227 CRC64;
     MATKAVCVLK GDGPVQGIIH FEQKANGPVV VKGRITGLVE GKHGFHVHEF GDNTQGCTSA
     GPHFNPLSKK HGGPQDEERH VGDLGNVTAG ADGVANVSIE DSLISLSGAN SIIGRTMVVH
     EKPDDLGKGG NEESTKTGNA GSRLACGVIG IAQ
//