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 04-NOV-2026, entry version 97. 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 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE601002; CAP30392.3; -; Genomic_DNA. DR AlphaFoldDB; A8XCP3; -. DR SMR; A8XCP3; -. DR FunCoup; A8XCP3; 1973. DR STRING; 6238.A8XCP3; -. DR EnsemblMetazoa; CBG11197a.1; CBG11197a.1; WBGene00032360. DR KEGG; cbr:CBG_11197; -. DR WormBase; CBG11197a; CBP02740; WBGene00032360; Cbr-sod-1. DR eggNOG; KOG0441; Eukaryota. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; A8XCP3; -. DR OMA; AACTQQK; -. DR OrthoDB; 2015551at2759; -. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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 FunFam; 2.60.40.200:FF:000011; 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 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 //