SODC_CAEEL
ID SODC_CAEEL Reviewed; 180 AA.
AC P34697; Q5W7E8; Q9N5Y1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE Short=SOD-1 {ECO:0000303|PubMed:16234242};
DE EC=1.15.1.1 {ECO:0000269|PubMed:16234242};
DE Flags: Precursor;
GN Name=sod-1; ORFNames=C15F1.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=8415630; DOI=10.1073/pnas.90.19.8905;
RA Larsen P.L.;
RT "Aging and resistance to oxidative damage in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8905-8909(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
RC STRAIN=Bristol N2;
RX PubMed=8081212;
RA Giglio M.P., Hunter T., Bannister J.V., Bannister W.H., Hunter G.J.;
RT "The copper/zinc superoxide dismutase gene of Caenorhabditis elegans.";
RL Biochem. Mol. Biol. Int. 33:41-44(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=14657502; DOI=10.1126/science.1087167;
RA Shibata Y., Branicky R., Landaverde I.O., Hekimi S.;
RT "Redox regulation of germline and vulval development in Caenorhabditis
RT elegans.";
RL Science 302:1779-1782(2003).
RN [5]
RP ACTIVITY REGULATION, SUBUNIT, MUTAGENESIS OF ALA-167 AND ALA-169, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=16234242; DOI=10.1074/jbc.m509142200;
RA Jensen L.T., Culotta V.C.;
RT "Activation of CuZn superoxide dismutases from Caenorhabditis elegans does
RT not require the copper chaperone CCS.";
RL J. Biol. Chem. 280:41373-41379(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18073424; DOI=10.1534/genetics.107.080788;
RA Yang W., Li J., Hekimi S.;
RT "A measurable increase in oxidative damage due to reduction in superoxide
RT detoxification fails to shorten the life span of long-lived mitochondrial
RT mutants of Caenorhabditis elegans.";
RL Genetics 177:2063-2074(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20380830; DOI=10.1016/j.ydbio.2010.03.026;
RA Yang Y., Han S.M., Miller M.A.;
RT "MSP hormonal control of the oocyte MAP kinase cascade and reactive oxygen
RT species signaling.";
RL Dev. Biol. 342:96-107(2010).
CC -!- FUNCTION: Protects cells against oxidative stress by converting
CC superoxide radicals to hydrogen peroxide (PubMed:16234242). Required
CC for normal brood size (PubMed:18073424). May be involved in regulating
CC mpk-1 phosphorylation downstream of phosphatase ptp-2 during oocyte
CC maturation (PubMed:20380830). {ECO:0000250|UniProtKB:P00441,
CC ECO:0000269|PubMed:16234242, ECO:0000269|PubMed:18073424,
CC ECO:0000269|PubMed:20380830}.
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:0000269|PubMed:16234242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000269|PubMed:16234242};
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 -!- ACTIVITY REGULATION: The insertion of copper which activates the
CC protein requires glutathione. This is independent of copper chaperone
CC for SOD1 (CCS), which activates orthologs.
CC {ECO:0000269|PubMed:16234242}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16234242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34697-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34697-2; Sequence=VSP_033146;
CC -!- DISRUPTION PHENOTYPE: Worms exhibit increased oxidative stress and
CC reduced brood size (PubMed:18073424). RNAi-mediated knockdown
CC suppresses the slow germline development and the delayed egg-production
CC of clk-1 mutants (PubMed:14657502). RNAi-mediated knockdown causes an
CC increase in the number of oocytes with mpk-1 phosphorylation
CC (PubMed:20380830). {ECO:0000269|PubMed:14657502,
CC ECO:0000269|PubMed:18073424, ECO:0000269|PubMed:20380830}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; L20135; AAA28147.1; -; mRNA.
DR EMBL; X77020; CAA54318.1; -; Genomic_DNA.
DR EMBL; FO080553; CCD64617.1; -; Genomic_DNA.
DR EMBL; FO080553; CCD64618.1; -; Genomic_DNA.
DR PIR; S41319; A48256.
DR RefSeq; NP_001021956.1; NM_001026785.2. [P34697-1]
DR RefSeq; NP_001021957.1; NM_001026786.3. [P34697-2]
DR PDB; 3KBE; X-ray; 1.10 A; A=24-180.
DR PDB; 3KBF; X-ray; 1.30 A; A=24-180.
DR PDBsum; 3KBE; -.
DR PDBsum; 3KBF; -.
DR AlphaFoldDB; P34697; -.
DR SMR; P34697; -.
DR BioGRID; 39479; 46.
DR IntAct; P34697; 1.
DR STRING; 6239.C15F1.7a; -.
DR EPD; P34697; -.
DR PaxDb; P34697; -.
DR PeptideAtlas; P34697; -.
DR EnsemblMetazoa; C15F1.7a.1; C15F1.7a.1; WBGene00004930. [P34697-1]
DR EnsemblMetazoa; C15F1.7b.1; C15F1.7b.1; WBGene00004930. [P34697-2]
DR GeneID; 174141; -.
DR KEGG; cel:CELE_C15F1.7; -.
DR UCSC; C15F1.7a; c. elegans. [P34697-1]
DR CTD; 174141; -.
DR WormBase; C15F1.7a; CE23550; WBGene00004930; sod-1. [P34697-1]
DR WormBase; C15F1.7b; CE20508; WBGene00004930; sod-1. [P34697-2]
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000168521; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P34697; -.
DR OMA; KWVAFHV; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P34697; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR EvolutionaryTrace; P34697; -.
DR PRO; PR:P34697; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004930; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005507; F:copper ion binding; IDA:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IDA:WormBase.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase.
DR GO; GO:0006801; P:superoxide metabolic process; IDA: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; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antioxidant; Copper; Cytoplasm;
KW Disulfide bond; Metal-binding; Oxidoreductase; Reference proteome; Signal;
KW Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..180
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164102"
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"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:8415630"
FT /id="VSP_033146"
FT MUTAGEN 167
FT /note="A->P: Abolishes enzyme activation but has no effect
FT on disulfide bond formation or dimer formation; when
FT associated with A-169."
FT /evidence="ECO:0000269|PubMed:16234242"
FT MUTAGEN 169
FT /note="A->P: Abolishes enzyme activation but has no effect
FT on disulfide bond formation or dimer formation; when
FT associated with A-167."
FT /evidence="ECO:0000269|PubMed:16234242"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3KBE"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:3KBE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3KBE"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3KBE"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3KBF"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:3KBF"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:3KBE"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:3KBE"
SQ SEQUENCE 180 AA; 18700 MW; 5F013D99A650AA97 CRC64;
MFMNLLTQVS NAIFPQVEAA QKMSNRAVAV LRGETVTGTI WITQKSENDQ AVIEGEIKGL
TPGLHGFHVH QYGDSTNGCI SAGPHFNPFG KTHGGPKSEI RHVGDLGNVE AGADGVAKIK
LTDTLVTLYG PNTVVGRSMV VHAGQDDLGE GVGDKAEESK KTGNAGARAA CGVIALAAPQ
