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Database: UniProt/SWISS-PROT
Entry: SODM_HORSE
LinkDB: SODM_HORSE
Original site: SODM_HORSE 
ID   SODM_HORSE              Reviewed;         222 AA.
AC   Q9XS41;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   15-MAR-2017, entry version 96.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   AltName: Full=Mn-SOD;
DE   Flags: Precursor;
GN   Name=SOD2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=10331206; DOI=10.1292/jvms.61.291;
RA   Ishida N., Katayama Y., Sato F., Hasegawa T., Mukoyama H.;
RT   "The cDNA sequences of equine antioxidative enzyme genes Cu/Zn-SOD and
RT   Mn-SOD, and these expressions in equine tissues.";
RL   J. Vet. Med. Sci. 61:291-294(1999).
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.
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}.
DR   EMBL; AB001693; BAA76922.1; -; mRNA.
DR   RefSeq; NP_001075986.1; NM_001082517.2.
DR   UniGene; Eca.420; -.
DR   ProteinModelPortal; Q9XS41; -.
DR   SMR; Q9XS41; -.
DR   STRING; 9796.ENSECAP00000009823; -.
DR   PaxDb; Q9XS41; -.
DR   PeptideAtlas; Q9XS41; -.
DR   GeneID; 100034223; -.
DR   KEGG; ecb:100034223; -.
DR   CTD; 6648; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; Q9XS41; -.
DR   KO; K04564; -.
DR   Proteomes; UP000002281; Unplaced.
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   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; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    222       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032868.
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;  24739 MW;  93A069481944E98C CRC64;
     MLCRAACSTS RKLVPALGSL GSRQKHSLPD LQYDYGALEP YINAQIMQLH HSKHHAAYVN
     NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHTI FWTNLSPNGG GEPKGKLLDA
     IKRDFGSFDK FKEKLTAVSA GVQGSGWGWL GFNKDQGRLQ IVACPNQDPL QGTTGLIPLL
     GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVSERYMAC KK
//
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