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Database: UniProt
Entry: P41981
LinkDB: P41981
Original site: P41981 
ID   SODM_ONCVO              Reviewed;         223 AA.
AC   P41981;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-DEC-2018, entry version 92.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sod-2;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=7772025; DOI=10.1042/bj3080441;
RA   Henkle-Duehrsen K., Tawe W., Warnecke C., Walter R.D.;
RT   "Characterization of the manganese superoxide dismutase cDNA and gene
RT   from the human parasite Onchocerca volvulus.";
RL   Biochem. J. 308:441-446(1995).
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 matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; X82172; CAA57658.1; -; Genomic_DNA.
DR   EMBL; X82171; CAA57657.1; -; mRNA.
DR   PIR; S48831; S48831.
DR   PIR; S55346; S48832.
DR   ProteinModelPortal; P41981; -.
DR   SMR; P41981; -.
DR   PRIDE; P41981; -.
DR   EnsemblMetazoa; OVOC1096a; OVOC1096a; WBGene00237905.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    223       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032878.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       184    184       Manganese. {ECO:0000250}.
FT   METAL       188    188       Manganese. {ECO:0000250}.
FT   VARIANT       7      7       V -> I.
SQ   SEQUENCE   223 AA;  25021 MW;  F6B78DAC10E02D92 CRC64;
     MNLIIGVAGR LLVGKNYCLN TQRLKHVLPD LPYDYGALEP ILSAEIMQVH HGKHHAAYVN
     ALNQAEEKVK EALAKGDTQA AVAGTKLMNF NTGGHINHTL FWEGLTAVKN SGEPNSELMT
     AIKKDFGSLE TMIDKLNAKT IAIQGSGWGW LAYDKEMKRL QLACCPNQDL LEPTTGLIPL
     FCIDVWEHAY YLQYKNLRPD FVKAIWKIAN WKIISDRYIK ARG
//
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