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Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)

 SODM_BOVIN              Reviewed;         222 AA.
P41976; Q2KJE8; Q5E9D2; Q862F8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
16-JAN-2019, entry version 127.
RecName: Full=Superoxide dismutase [Mn], mitochondrial;
EC=1.15.1.1;
Flags: Precursor;
Name=SOD2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Lung;
PubMed=8292376; DOI=10.1165/ajrcmb.10.1.8292376;
Meyrick B., Magnuson M.A.;
"Identification and functional characterization of the bovine
manganous superoxide dismutase promoter.";
Am. J. Respir. Cell Mol. Biol. 10:113-121(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 93-201.
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems. {ECO:0000250|UniProtKB:P07895}.
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:18421; EC=1.15.1.1;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P04179};
Note=Binds 1 Mn(2+) ion per subunit.
{ECO:0000250|UniProtKB:P04179};
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- PTM: Nitrated under oxidative stress. Nitration coupled with
oxidation inhibits the catalytic activity.
{ECO:0000250|UniProtKB:P07895}.
-!- PTM: Acetylation at Lys-122 decreases enzymatic activity.
Deacetylated by SIRT3 upon exposure to ionizing radiations or
after long fasting (By similarity).
{ECO:0000250|UniProtKB:P04179}.
-!- PTM: Polyubiquitinated; leading to proteasomal degradation.
Deubiquitinated by USP36 which increases protein stability.
{ECO:0000250|UniProtKB:P04179}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA30655.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L22092; AAA30655.1; ALT_INIT; mRNA.
EMBL; L22093; AAA30656.1; -; Genomic_DNA.
EMBL; S67818; AAC60522.2; -; mRNA.
EMBL; S67819; AAD14001.1; -; Genomic_DNA.
EMBL; BT020988; AAX09005.1; -; mRNA.
EMBL; BC105378; AAI05379.1; -; mRNA.
EMBL; AB099036; BAC56526.1; -; mRNA.
PIR; I51918; I51918.
RefSeq; NP_963285.2; NM_201527.2.
RefSeq; XP_010807032.1; XM_010808730.1.
UniGene; Bt.4748; -.
ProteinModelPortal; P41976; -.
SMR; P41976; -.
BioGrid; 158821; 2.
STRING; 9913.ENSBTAP00000008569; -.
PaxDb; P41976; -.
PeptideAtlas; P41976; -.
PRIDE; P41976; -.
GeneID; 281496; -.
KEGG; bta:281496; -.
CTD; 6648; -.
eggNOG; KOG0876; Eukaryota.
eggNOG; COG0605; LUCA.
HOVERGEN; HBG004451; -.
InParanoid; P41976; -.
KO; K04564; -.
OrthoDB; 1353361at2759; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
GO; GO:0007568; P:aging; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
Gene3D; 1.10.287.990; -; 1.
Gene3D; 2.40.500.20; -; 1.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
InterPro; IPR036324; Mn/Fe_SOD_N_sf.
InterPro; IPR036314; SOD_C_sf.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
2: Evidence at transcript level;
Acetylation; Complete proteome; Manganese; Metal-binding;
Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
Transit peptide; Ubl conjugation.
TRANSIT 1 24 Mitochondrion. {ECO:0000250}.
CHAIN 25 222 Superoxide dismutase [Mn], mitochondrial.
/FTId=PRO_0000032866.
METAL 50 50 Manganese. {ECO:0000250}.
METAL 98 98 Manganese. {ECO:0000250}.
METAL 183 183 Manganese. {ECO:0000250}.
METAL 187 187 Manganese. {ECO:0000250}.
MOD_RES 58 58 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P04179}.
MOD_RES 68 68 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04179}.
MOD_RES 68 68 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 75 75 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 75 75 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 130 130 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04179}.
MOD_RES 130 130 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P09671}.
MOD_RES 202 202 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09671}.
CONFLICT 8 8 S -> R (in Ref. 1; AAD14001).
{ECO:0000305}.
CONFLICT 14 14 V -> A (in Ref. 2; AAX09005).
{ECO:0000305}.
CONFLICT 90 90 F -> V (in Ref. 1; AAC60522).
{ECO:0000305}.
CONFLICT 94 95 GH -> AI (in Ref. 4; BAC56526).
{ECO:0000305}.
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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Pathways :
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1263: Mitochondrial Gene Expression
WP1301: Mitochondrial Gene Expression
WP1368: Mitochondrial Gene Expression
WP1502: Mitochondrial biogenesis
WP1905: RNA Polymerase I, RNA Polymerase III, and Mitochondrial Transcription
WP296: TCA Cycle - biocyc
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP391: Mitochondrial Gene Expression
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP406: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP419: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP448: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP525: Mitochondrial Unfolded-Protein Response
WP62: Mitochondrial tRNA Synthetases
WP763: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP928: Mitochondrial Gene Expression
WP989: Mitochondrial LC-Fatty Acid Beta-Oxidation

Related Genes :
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[Sod2 Sod-2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[Sod2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[SOD1] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (hSod1)
[FSD2 APG8 At5g51100 MWD22.4] Superoxide dismutase [Fe] 2, chloroplastic (EC 1.15.1.1) (Protein ALBINO OR PALE GREEN 8) (Protein FE SUPEROXIDE DISMUTASE 2)
[SOD1 YJR104C J1968] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
[NECI] Nectarin-1 (EC 1.15.1.1) (Superoxide dismutase [Mn])
[sod-1 C15F1.7] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
[sodA sod] Superoxide dismutase [Mn/Fe] (EC 1.15.1.1)
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[sodB sod sodA Rv3846 MTCY01A6.22c] Superoxide dismutase [Fe] (EC 1.15.1.1)
[CSD3 At5g18100 MRG7.6] Superoxide dismutase [Cu-Zn] 3 (EC 1.15.1.1) (Copper/zinc superoxide dismutase 3)
[sod-1 NCU02133] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
[SOD5 PGA3 SOD31 CAALFM_C200680CA CaO19.2060 CaO19.9607] Cell surface Cu-only superoxide dismutase 5 (EC 1.15.1.1) (Predicted GPI-anchored protein 3)
[sod1 sod VNG_1190G] Superoxide dismutase [Mn] 1 (EC 1.15.1.1)
[sodC Rv0432 MTCY22G10.29] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (Mn-SOD)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[sodC DDB_G0282993] Extracellular superoxide dismutase [Cu-Zn] 3 (EC-SOD 3) (EC 1.15.1.1)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[sod-2 18F11.030 NCU01213] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (Fragment)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[SOD2 QnpA-14761] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[SOD6 PGA9 SOD33 CAALFM_C200240CA CaO19.2108 CaO19.9656] Cell surface superoxide dismutase [Cu-Zn] 6 (EC 1.15.1.1) (Predicted GPI-anchored protein 9)
[CCS At1g12520 F5O11.26 T12C24.6] Copper chaperone for superoxide dismutase, chloroplastic/cytosolic (AtCCS) (Superoxide dismutase copper chaperone)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)

Bibliography :
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[30597290] CuZnSOD and MnSOD from freshwater planarian Dugesia japonica: cDNA cloning, mRNA expression and enzyme activity in response to environmental pollutants.
[30587174] Mitochondria-targeted antioxidant SKQ1 protects cornea from oxidative damage induced by ultraviolet irradiation and mechanical injury.
[30582969] Fusaric acid induces NRF2 as a cytoprotective response to prevent NLRP3 activation in the liver derived HepG2 cell line.
[30554132] A step towards development of promising trypanocidal agents: Synthesis, characterization and in vitro biological evaluation of ferrocenyl Mannich base-type derivatives.
[30529917] Developmental neurotoxicity of maneb: Notochord defects, mitochondrial dysfunction and hypoactivity in zebrafish (Danio rerio) embryos and larvae.
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