SODM_RAT
ID SODM_RAT Reviewed; 222 AA.
AC P07895;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=Sod2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3697077; DOI=10.1093/nar/15.23.10070;
RA Ho Y.-S., Crapo J.D.;
RT "Nucleotide sequences of cDNAs coding for rat manganese-containing
RT superoxide dismutase.";
RL Nucleic Acids Res. 15:10070-10070(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2001291; DOI=10.1165/ajrcmb/4.3.278;
RA Ho Y.-S., Howard A.J., Crapo J.D.;
RT "Molecular structure of a functional rat gene for manganese-containing
RT superoxide dismutase.";
RL Am. J. Respir. Cell Mol. Biol. 4:278-286(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 54-68; 76-108; 135-154 AND 203-216, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP NITRATION, AND FUNCTION DURING OXIDATIVE STRESS.
RX PubMed=12791589; DOI=10.1152/ajpheart.00096.2003;
RA Guo W., Adachi T., Matsui R., Xu S., Jiang B., Zou M.H., Kirber M.,
RA Lieberthal W., Cohen R.A.;
RT "Quantitative assessment of tyrosine nitration of manganese superoxide
RT dismutase in angiotensin II-infused rat kidney.";
RL Am. J. Physiol. 285:H1396-H1403(2003).
RN [6]
RP NITRATION AT TYR-58.
RX PubMed=16399855; DOI=10.1152/ajpheart.01293.2005;
RA Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H.,
RA Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.;
RT "Detection of sequence-specific tyrosine nitration of manganese SOD and
RT SERCA in cardiovascular disease and aging.";
RL Am. J. Physiol. 290:H2220-H2227(2006).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000269|PubMed:12791589}.
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Nitrated under oxidative stress. Nitration coupled with oxidation
CC inhibits the catalytic activity. {ECO:0000269|PubMed:12791589,
CC ECO:0000269|PubMed:16399855}.
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}.
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DR EMBL; Y00497; CAA68549.1; -; mRNA.
DR EMBL; X56600; CAA39937.1; -; Genomic_DNA.
DR EMBL; BC070913; AAH70913.1; -; mRNA.
DR PIR; S21661; DSRTN.
DR RefSeq; NP_058747.1; NM_017051.2.
DR AlphaFoldDB; P07895; -.
DR SMR; P07895; -.
DR BioGRID; 246911; 1.
DR IntAct; P07895; 1.
DR STRING; 10116.ENSRNOP00000025794; -.
DR iPTMnet; P07895; -.
DR PhosphoSitePlus; P07895; -.
DR SwissPalm; P07895; -.
DR World-2DPAGE; 0004:P07895; -.
DR jPOST; P07895; -.
DR PaxDb; P07895; -.
DR PRIDE; P07895; -.
DR Ensembl; ENSRNOT00000025794; ENSRNOP00000025794; ENSRNOG00000019048.
DR GeneID; 24787; -.
DR KEGG; rno:24787; -.
DR CTD; 6648; -.
DR RGD; 3732; Sod2.
DR eggNOG; KOG0876; Eukaryota.
DR GeneTree; ENSGT00390000011877; -.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; P07895; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; P07895; -.
DR TreeFam; TF105132; -.
DR BRENDA; 1.15.1.1; 5301.
DR Reactome; R-RNO-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:P07895; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019048; Expressed in heart and 19 other tissues.
DR Genevisible; P07895; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0030145; F:manganese ion binding; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0019825; F:oxygen binding; IDA:RGD.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:RGD.
DR GO; GO:0003069; P:acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; ISO:RGD.
DR GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0003032; P:detection of oxygen; ISO:RGD.
DR GO; GO:0048773; P:erythrophore differentiation; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:RGD.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IMP:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:RGD.
DR GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:1902631; P:negative regulation of membrane hyperpolarization; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0032364; P:oxygen homeostasis; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:1905932; P:positive regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:RGD.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; ISO:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0035900; P:response to isolation stress; IEP:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071000; P:response to magnetism; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; ISO:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0034021; P:response to silicon dioxide; IEP:RGD.
DR GO; GO:0000303; P:response to superoxide; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0042554; P:superoxide anion generation; ISO:RGD.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Manganese; Metal-binding;
KW Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT CHAIN 25..222
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032874"
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:0000269|PubMed:16399855"
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 114
FT /note="N6-acetyllysine"
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 167
FT /note="Q -> H (in Ref. 1; CAA68549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24674 MW; 8CCC1E0E857B3138 CRC64;
MLCRAACSAG RRLGPAASTA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHATYVN
NLNVTEEKYH EALAKGDVTT QVALQPALKF NGGGHINHSI FWTNLSPKGG GEPKGELLEA
IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVSQRYIVC KK
