GenomeNet

Database: UniProt
Entry: P41977
LinkDB: P41977
Original site: P41977 
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   16-JAN-2019, entry version 137.
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
RT   investigating 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,
RT   and influences over temperature-dependent insulin-like signaling,
RT   stress 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
CC       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
CC       family. {ECO:0000305}.
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   UniGene; Cel.17915; -.
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   PDBsum; 3DC5; -.
DR   PDBsum; 4X9Q; -.
DR   PDBsum; 5AG2; -.
DR   PDBsum; 6ELK; -.
DR   ProteinModelPortal; P41977; -.
DR   SMR; P41977; -.
DR   STRING; 6239.C08A9.1; -.
DR   iPTMnet; P41977; -.
DR   EPD; P41977; -.
DR   PaxDb; P41977; -.
DR   PeptideAtlas; P41977; -.
DR   PRIDE; P41977; -.
DR   EnsemblMetazoa; C08A9.1; C08A9.1; 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   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P41977; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1353361at2759; -.
DR   PhylomeDB; P41977; -.
DR   Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR   EvolutionaryTrace; P41977; -.
DR   PRO; PR:P41977; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00004932; Expressed in 3 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005746; C:mitochondrial respirasome; IDA:WormBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0046872; F:metal 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:0007568; P:aging; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    218       Superoxide dismutase [Mn] 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000032877.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       179    179       Manganese. {ECO:0000250}.
FT   METAL       183    183       Manganese. {ECO:0000250}.
FT   TURN         35     41       {ECO:0000244|PDB:6ELK}.
FT   HELIX        44     52       {ECO:0000244|PDB:6ELK}.
FT   HELIX        54     75       {ECO:0000244|PDB:6ELK}.
FT   HELIX        78    103       {ECO:0000244|PDB:6ELK}.
FT   HELIX       114    124       {ECO:0000244|PDB:6ELK}.
FT   HELIX       127    139       {ECO:0000244|PDB:6ELK}.
FT   STRAND      142    152       {ECO:0000244|PDB:6ELK}.
FT   TURN        153    156       {ECO:0000244|PDB:6ELK}.
FT   STRAND      157    164       {ECO:0000244|PDB:6ELK}.
FT   STRAND      171    179       {ECO:0000244|PDB:6ELK}.
FT   HELIX       182    184       {ECO:0000244|PDB:6ELK}.
FT   HELIX       186    189       {ECO:0000244|PDB:6ELK}.
FT   HELIX       193    200       {ECO:0000244|PDB:6ELK}.
FT   HELIX       201    203       {ECO:0000244|PDB:6ELK}.
FT   HELIX       206    216       {ECO:0000244|PDB:6ELK}.
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
//
DBGET integrated database retrieval system