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Database: UniProt/SWISS-PROT
Entry: SODM_MACFA
LinkDB: SODM_MACFA
Original site: SODM_MACFA 
ID   SODM_MACFA              Reviewed;         222 AA.
AC   Q8HXP3; Q2PFT1;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 3.
DT   25-OCT-2017, entry version 76.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD2; ORFNames=QnpA-14761;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque
RT   cDNA oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-222.
RX   PubMed=12383507; DOI=10.1016/S0378-1119(02)00837-5;
RA   Fukuhara R., Tezuka T., Kageyama T.;
RT   "Structure, molecular evolution, and gene expression of primate
RT   superoxide dismutases.";
RL   Gene 296:99-109(2002).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- PTM: Nitrated under oxidative stress. Nitration coupled with
CC       oxidation inhibits the catalytic activity (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Acetylation at Lys-122 decreases enzymatic activity.
CC       Deacetylated by SIRT3 upon exposure to ionizing radiations or
CC       after long fasting (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC20357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AB220506; BAE73039.1; -; mRNA.
DR   EMBL; AB087278; BAC20357.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001274560.1; NM_001287631.1.
DR   RefSeq; XP_005551576.1; XM_005551519.2.
DR   RefSeq; XP_015303876.1; XM_015448390.1.
DR   UniGene; Mfa.5336; -.
DR   ProteinModelPortal; Q8HXP3; -.
DR   SMR; Q8HXP3; -.
DR   PRIDE; Q8HXP3; -.
DR   GeneID; 102123902; -.
DR   KEGG; mcf:102123902; -.
DR   CTD; 6648; -.
DR   HOVERGEN; HBG004451; -.
DR   KO; K04564; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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   Acetylation; Manganese; Metal-binding; Mitochondrion; Nitration;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    222       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000159953.
FT   METAL        50     50       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       183    183       Manganese. {ECO:0000250}.
FT   METAL       187    187       Manganese. {ECO:0000250}.
FT   MOD_RES      58     58       Nitrated tyrosine.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      68     68       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      68     68       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      75     75       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      75     75       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     114    114       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     122    122       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     122    122       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     130    130       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES     130    130       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     202    202       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09671}.
SQ   SEQUENCE   222 AA;  24697 MW;  C9F1A0FC5902B434 CRC64;
     MLSRAVCGTG RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
     NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA
     IKRDFGSFEK FKEKLTAASV GVQGSGWGWL GFNKERGQLQ IAACPNQDPL QGTTGLIPLL
     GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK
//
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