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Database: UniProt/SWISS-PROT
Entry: SODM_BOVIN
LinkDB: SODM_BOVIN
Original site: SODM_BOVIN 
ID   SODM_BOVIN              Reviewed;         222 AA.
AC   P41976; Q2KJE8; Q5E9D2; Q862F8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-APR-2018, entry version 122.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Lung;
RX   PubMed=8292376; DOI=10.1165/ajrcmb.10.1.8292376;
RA   Meyrick B., Magnuson M.A.;
RT   "Identification and functional characterization of the bovine
RT   manganous superoxide dismutase promoter.";
RL   Am. J. Respir. Cell Mol. Biol. 10:113-121(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 93-201.
RX   PubMed=12658628; DOI=10.1002/mrd.10292;
RA   Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
RA   Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
RA   Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
RT   "Characterization of gene expression profiles in early bovine
RT   pregnancy using a custom cDNA microarray.";
RL   Mol. Reprod. Dev. 65:9-18(2003).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250|UniProtKB:P07895}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P04179};
CC       Note=Binds 1 Mn(2+) ion per subunit.
CC       {ECO:0000250|UniProtKB:P04179};
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.
CC       {ECO:0000250|UniProtKB:P07895}.
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).
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- PTM: Polyubiquitinated; leading to proteasomal degradation.
CC       Deubiquitinated by USP36 which increases protein stability.
CC       {ECO:0000250|UniProtKB:P04179}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA30655.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; L22092; AAA30655.1; ALT_INIT; mRNA.
DR   EMBL; L22093; AAA30656.1; -; Genomic_DNA.
DR   EMBL; S67818; AAC60522.2; -; mRNA.
DR   EMBL; S67819; AAD14001.1; -; Genomic_DNA.
DR   EMBL; BT020988; AAX09005.1; -; mRNA.
DR   EMBL; BC105378; AAI05379.1; -; mRNA.
DR   EMBL; AB099036; BAC56526.1; -; mRNA.
DR   PIR; I51918; I51918.
DR   RefSeq; NP_963285.2; NM_201527.2.
DR   RefSeq; XP_010807032.1; XM_010808730.1.
DR   UniGene; Bt.4748; -.
DR   ProteinModelPortal; P41976; -.
DR   SMR; P41976; -.
DR   BioGrid; 158821; 2.
DR   STRING; 9913.ENSBTAP00000008569; -.
DR   PaxDb; P41976; -.
DR   PeptideAtlas; P41976; -.
DR   PRIDE; P41976; -.
DR   GeneID; 104973000; -.
DR   GeneID; 281496; -.
DR   KEGG; bta:104973000; -.
DR   KEGG; bta:281496; -.
DR   CTD; 6648; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; P41976; -.
DR   KO; K04564; -.
DR   Proteomes; UP000009136; 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 by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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   Acetylation; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW   Transit peptide; Ubl conjugation.
FT   TRANSIT       1     24       Mitochondrion. {ECO:0000250}.
FT   CHAIN        25    222       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032866.
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     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}.
FT   CONFLICT      8      8       S -> R (in Ref. 1; AAD14001).
FT                                {ECO:0000305}.
FT   CONFLICT     14     14       V -> A (in Ref. 2; AAX09005).
FT                                {ECO:0000305}.
FT   CONFLICT     90     90       F -> V (in Ref. 1; AAC60522).
FT                                {ECO:0000305}.
FT   CONFLICT     94     95       GH -> AI (in Ref. 4; BAC56526).
FT                                {ECO:0000305}.
SQ   SEQUENCE   222 AA;  24638 MW;  806CC3FCB1A74413 CRC64;
     MLSRAACSTS RRLVPALSVL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
     NLNVAEEKYR EALEKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPQGELLEA
     IKRDFGSFAK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL
     GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTARYTAC SK
//
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