SODM2_CAEEL
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 03-AUG-2022, entry version 150.
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 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 -!- 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}.
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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_078363.6.
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 PDBsum; 3DC5; -.
DR PDBsum; 4X9Q; -.
DR PDBsum; 5AG2; -.
DR PDBsum; 6ELK; -.
DR PDBsum; 6QZM; -.
DR PDBsum; 6QZN; -.
DR PDBsum; 6S0D; -.
DR AlphaFoldDB; P41977; -.
DR SMR; P41977; -.
DR STRING; 6239.C08A9.1; -.
DR iPTMnet; P41977; -.
DR EPD; P41977; -.
DR PaxDb; P41977; -.
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 CTD; 181748; -.
DR WormBase; C08A9.1; CE08002; WBGene00004932; sod-3.
DR eggNOG; KOG0876; Eukaryota.
DR GeneTree; ENSGT00390000011877; -.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; P41977; -.
DR OMA; YEGWKGE; -.
DR OrthoDB; 1353361at2759; -.
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 tissues.
DR GO; GO:0005746; C:mitochondrial respirasome; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:WormBase.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:WormBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 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 TURN 35..41
FT /evidence="ECO:0007829|PDB:6S0D"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6S0D"
FT HELIX 54..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
