ID SODC_CAEBR Reviewed; 180 AA.
AC A8XCP3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sod-1 {ECO:0000250|UniProtKB:P34697}; ORFNames=CBG11197;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems. Required for normal
CC brood size. May be involved in regulating mpk-1 phosphorylation
CC downstream of phosphatase ptp-2 during oocyte maturation.
CC {ECO:0000250|UniProtKB:P00441, ECO:0000250|UniProtKB:P34697}.
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: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. {ECO:0000250|UniProtKB:P00441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000255}.
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DR EMBL; HE601002; CAP30392.3; -; Genomic_DNA.
DR RefSeq; XP_002630464.1; XM_002630418.1.
DR AlphaFoldDB; A8XCP3; -.
DR SMR; A8XCP3; -.
DR STRING; 6238.A8XCP3; -.
DR EnsemblMetazoa; CBG11197a.1; CBG11197a.1; WBGene00032360.
DR GeneID; 8571979; -.
DR KEGG; cbr:CBG_11197; -.
DR CTD; 8571979; -.
DR WormBase; CBG11197a; CBP02740; WBGene00032360; Cbr-sod-1.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; A8XCP3; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblMetazoa.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; ISS:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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:SF103; 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 3: Inferred from homology;
KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..180
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000255"
FT /id="PRO_0000331231"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 79..171
FT /evidence="ECO:0000250|UniProtKB:P00441"
SQ SEQUENCE 180 AA; 18524 MW; 24362A5FEDF4D8E0 CRC64;
MFMNLLSQVS NAIFPQVEAA QKMSNRAVAV LRGDVVSGTI WITQNSESDP AVIEGEIKGL
TPGLHGFHVH QYGDSTNGCL SAGPHFNPFG KTHGGPNSET RHVGDLGNVE AGADGVAKVH
ITDKLITLYG ANTVIGRSMV VHAGQDDLGQ GVGDKAEESA KTGNAGARAA CGVIALAAPQ
//
