ID SODM2_CAEEL Reviewed; 218 AA. AC P41977; Q27469; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 04-NOV-2026, entry version 168. DE RecName: Full=Superoxide dismutase [Mn] 2, mitochondrial; DE EC=1.15.1.1; DE Flags: Precursor; GN Name=sod-3; ORFNames=C08A9.1; 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 [GENOMIC DNA / MRNA]. RC STRAIN=Bristol N2; RX PubMed=8081211; RA Giglio M.P., Hunter T., Bannister J.V., Bannister W.H., Hunter G.J.; RT "The manganese superoxide dismutase gene of Caenorhabditis elegans."; RL Biochem. Mol. Biol. Int. 33:37-40(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 [3] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY HEAT. RX PubMed=17894411; DOI=10.1002/jcp.21269; RA Wolf M., Nunes F., Henkel A., Heinick A., Paul R.J.; RT "The MAP kinase JNK-1 of Caenorhabditis elegans: location, activation, and RT influences over temperature-dependent insulin-like signaling, stress RT responses, and fitness."; RL J. Cell. Physiol. 214:721-729(2008). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17894411}. CC -!- TISSUE SPECIFICITY: Expressed in pharynx and rectum. Upon thermal CC stress, expressed in vulva, body wall muscles and hypodermis. CC {ECO:0000269|PubMed:17894411}. CC -!- INDUCTION: By heat. {ECO:0000269|PubMed:17894411}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000305}. 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; X77021; CAA54319.1; -; Genomic_DNA. DR EMBL; X85790; CAA59790.1; -; mRNA. DR EMBL; FO080426; CCD63614.1; -; Genomic_DNA. DR PIR; S52721; S52721. DR RefSeq; NP_510764.1; NM_078363.9. DR PDB; 3DC5; X-ray; 1.70 A; A/C=25-218. DR PDB; 4X9Q; X-ray; 1.77 A; A/C=25-218. DR PDB; 5AG2; X-ray; 1.77 A; A/C=25-218. DR PDB; 6ELK; X-ray; 1.65 A; A/C=25-218. DR PDB; 6QZM; X-ray; 1.60 A; A/C=25-218. DR PDB; 6QZN; X-ray; 1.64 A; A/C=25-218. DR PDB; 6S0D; X-ray; 1.52 A; A/C=25-218. DR AlphaFoldDB; P41977; -. DR SMR; P41977; -. DR FunCoup; P41977; 957. DR STRING; 6239.C08A9.1.1; -. DR iPTMnet; P41977; -. DR PaxDb; 6239-C08A9.1.1; -. DR PeptideAtlas; P41977; -. DR EnsemblMetazoa; C08A9.1.1; C08A9.1.1; WBGene00004932. DR GeneID; 181748; -. DR KEGG; cel:CELE_C08A9.1; -. DR UCSC; C08A9.1.1; c. elegans. DR AGR; WB:WBGene00004932; -. DR CTD; 181748; -. DR WormBase; C08A9.1; CE08002; WBGene00004932; sod-3. DR eggNOG; KOG0876; Eukaryota. DR HOGENOM; CLU_031625_2_1_1; -. DR InParanoid; P41977; -. DR OMA; AACSQHC; -. DR OrthoDB; 239262at2759; -. DR PhylomeDB; P41977; -. DR EvolutionaryTrace; P41977; -. DR PRO; PR:P41977; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00004932; Expressed in adult organism and 2 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; IDA:WormBase. DR GO; GO:0098803; C:respiratory chain complex; IDA:WormBase. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0004784; F:superoxide dismutase activity; IDA:WormBase. DR GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase. DR FunFam; 1.10.287.990:FF:000001; Superoxide dismutase; 1. DR FunFam; 3.55.40.20:FF:000003; Superoxide dismutase [Mn], mitochondrial; 1. DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1. DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1. DR InterPro; IPR050265; Fe/Mn_Superoxide_Dismutase. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR InterPro; IPR036324; Mn/Fe_SOD_N_sf. DR InterPro; IPR036314; SOD_C_sf. DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1. DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 1: Evidence at protein level; KW 3D-structure; Manganese; Metal-binding; Mitochondrion; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1..24 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 25..218 FT /note="Superoxide dismutase [Mn] 2, mitochondrial" FT /id="PRO_0000032877" FT BINDING 50 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 98 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 179 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 183 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:6S0D" FT TURN 35..41 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 44..49 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 50..55 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 56..75 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 78..83 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 85..103 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 114..124 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 127..139 FT /evidence="ECO:0007829|PDB:6S0D" FT STRAND 143..152 FT /evidence="ECO:0007829|PDB:6S0D" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:6S0D" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:6S0D" FT STRAND 171..179 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 186..189 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:6S0D" FT HELIX 206..217 FT /evidence="ECO:0007829|PDB:6S0D" SQ SEQUENCE 218 AA; 24661 MW; F35375C9E63BCDC7 CRC64; MLQSTARTAS KLVQPVAGVL AVRSKHTLPD LPFDYADLEP VISHEIMQLH HQKHHATYVN NLNQIEEKLH EAVSKGNLKE AIALQPALKF NGGGHINHSI FWTNLAKDGG EPSKELMDTI KRDFGSLDNL QKRLSDITIA VQGSGWGWLG YCKKDKILKI ATCANQDPLE GMVPLFGIDV WEHAYYLQYK NVRPDYVHAI WKIANWKNIS ERFANARQ //