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Database: UniProt/SWISS-PROT
Entry: SODM1_CAEEL
LinkDB: SODM1_CAEEL
Original site: SODM1_CAEEL 
ID   SODM1_CAEEL             Reviewed;         221 AA.
AC   P31161;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   07-JUN-2017, entry version 126.
DE   RecName: Full=Superoxide dismutase [Mn] 1, mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sod-2; Synonyms=sdm-1; ORFNames=F10D11.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Suzuki N., Ishii N., Suzuki K.;
RT   "Cloning and characterization of manganese superoxide dismutase gene
RT   in C.elegans.";
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8905235; DOI=10.1093/dnares/3.3.171;
RA   Suzuki N., Inokuma K., Yasuda K., Ishii N.;
RT   "Cloning, sequencing and mapping of a manganese superoxide dismutase
RT   gene of the nematode Caenorhabditis elegans.";
RL   DNA Res. 3:171-174(1996).
RN   [3]
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).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; D12984; BAA02363.1; -; mRNA.
DR   EMBL; D85499; BAA12821.1; -; Genomic_DNA.
DR   EMBL; Z81057; CAB02913.1; -; Genomic_DNA.
DR   PIR; JC5122; JC5122.
DR   RefSeq; NP_492290.1; NM_059889.4.
DR   UniGene; Cel.112; -.
DR   PDB; 3DC6; X-ray; 1.80 A; A/C=25-221.
DR   PDBsum; 3DC6; -.
DR   ProteinModelPortal; P31161; -.
DR   SMR; P31161; -.
DR   STRING; 6239.F10D11.1.2; -.
DR   iPTMnet; P31161; -.
DR   EPD; P31161; -.
DR   PaxDb; P31161; -.
DR   PeptideAtlas; P31161; -.
DR   PRIDE; P31161; -.
DR   EnsemblMetazoa; F10D11.1.1; F10D11.1.1; WBGene00004931.
DR   EnsemblMetazoa; F10D11.1.2; F10D11.1.2; WBGene00004931.
DR   GeneID; 172632; -.
DR   KEGG; cel:CELE_F10D11.1; -.
DR   UCSC; F10D11.1.1; c. elegans.
DR   CTD; 172632; -.
DR   WormBase; F10D11.1; CE09323; WBGene00004931; sod-2.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P31161; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; EOG091G0MVL; -.
DR   PhylomeDB; P31161; -.
DR   Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR   EvolutionaryTrace; P31161; -.
DR   PRO; PR:P31161; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00004931; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0097249; C:mitochondrial respiratory chain supercomplex; IDA:WormBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   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    221       Superoxide dismutase [Mn] 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000032876.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       182    182       Manganese. {ECO:0000250}.
FT   METAL       186    186       Manganese. {ECO:0000250}.
FT   TURN         35     41       {ECO:0000244|PDB:3DC6}.
FT   HELIX        44     52       {ECO:0000244|PDB:3DC6}.
FT   HELIX        54     74       {ECO:0000244|PDB:3DC6}.
FT   HELIX        78     83       {ECO:0000244|PDB:3DC6}.
FT   HELIX        85    103       {ECO:0000244|PDB:3DC6}.
FT   HELIX       114    124       {ECO:0000244|PDB:3DC6}.
FT   HELIX       127    139       {ECO:0000244|PDB:3DC6}.
FT   STRAND      143    152       {ECO:0000244|PDB:3DC6}.
FT   TURN        153    156       {ECO:0000244|PDB:3DC6}.
FT   STRAND      157    164       {ECO:0000244|PDB:3DC6}.
FT   HELIX       169    173       {ECO:0000244|PDB:3DC6}.
FT   STRAND      176    182       {ECO:0000244|PDB:3DC6}.
FT   HELIX       185    187       {ECO:0000244|PDB:3DC6}.
FT   HELIX       189    192       {ECO:0000244|PDB:3DC6}.
FT   HELIX       196    202       {ECO:0000244|PDB:3DC6}.
FT   HELIX       203    206       {ECO:0000244|PDB:3DC6}.
FT   HELIX       209    219       {ECO:0000244|PDB:3DC6}.
SQ   SEQUENCE   221 AA;  24537 MW;  EEA518B2800379F7 CRC64;
     MLQNTVRCVS KLVQPITGVA AVRSKHSLPD LPYDYADLEP VISHEIMQLH HQKHHATYVN
     NLNQIEEKLH EAVSKGNVKE AIALQPALKF NGGGHINHSI FWTNLAKDGG EPSAELLTAI
     KSDFGSLDNL QKQLSASTVA VQGSGWGWLG YCPKGKILKV ATCANQDPLE ATTGLVPLFG
     IDVWEHAYYL QYKNVRPDYV NAIWKIANWK NVSERFAKAQ Q
//
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