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 03-AUG-2022, entry version 138.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 manganous
RT 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., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT 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 systems.
CC {ECO:0000250|UniProtKB:P07895}.
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;
CC Evidence={ECO:0000250|UniProtKB:P04179};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P04179};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Nitrated under oxidative stress. Nitration coupled with oxidation
CC inhibits the catalytic activity. {ECO:0000250|UniProtKB:P07895}.
CC -!- PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated
CC by SIRT3 upon exposure to ionizing radiations or after long fasting (By
CC similarity). {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 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30655.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; P41976; -.
DR SMR; P41976; -.
DR BioGRID; 158821; 2.
DR STRING; 9913.ENSBTAP00000008569; -.
DR PaxDb; P41976; -.
DR PeptideAtlas; P41976; -.
DR PRIDE; P41976; -.
DR GeneID; 281496; -.
DR KEGG; bta:281496; -.
DR CTD; 6648; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_2_3_1; -.
DR InParanoid; P41976; -.
DR OrthoDB; 1353361at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 3.55.40.20; -; 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; Manganese; Metal-binding; Mitochondrion; Nitration;
KW Oxidoreductase; Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 25..222
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032866"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 75
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 75
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 130
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 130
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT CONFLICT 8
FT /note="S -> R (in Ref. 1; AAD14001)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="V -> A (in Ref. 2; AAX09005)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="F -> V (in Ref. 1; AAC60522)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="GH -> AI (in Ref. 4; BAC56526)"
FT /evidence="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
