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Database: UniProt/SWISS-PROT
Entry: SODM_RAT
LinkDB: SODM_RAT
Original site: 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   07-NOV-2018, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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
RP   IDENTIFICATION 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
RT   and 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
CC       systems. {ECO:0000269|PubMed:12791589}.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Nitrated under oxidative stress. Nitration coupled with
CC       oxidation inhibits the catalytic activity.
CC       {ECO:0000269|PubMed:12791589, ECO:0000269|PubMed:16399855}.
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}.
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   UniGene; Rn.10488; -.
DR   ProteinModelPortal; 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   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   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOGENOM; HOG000013583; -.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; P07895; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; EOG091G0MVL; -.
DR   PhylomeDB; P07895; -.
DR   TreeFam; TF105132; -.
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 10 organ(s), highest expression level in heart.
DR   Genevisible; P07895; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
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; IDA:RGD.
DR   GO; GO:0030145; F:manganese ion binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
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; IEA:Ensembl.
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:0071361; P:cellular response to ethanol; IEP:RGD.
DR   GO; GO:0003032; P:detection of oxygen; IEA:Ensembl.
DR   GO; GO:0048773; P:erythrophore differentiation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0019430; P:removal of superoxide radicals; IDA:RGD.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR   GO; GO:0009409; P:response to cold; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IDA:RGD.
DR   GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
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:0010269; P:response to selenium ion; IEP:RGD.
DR   GO; GO:0034021; P:response to silicon dioxide; IEP:RGD.
DR   GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Mitochondrion; Nitration; Oxidoreductase;
KW   Reference proteome; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     24       Mitochondrion.
FT   CHAIN        25    222       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032874.
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:0000269|PubMed:16399855}.
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}.
FT   CONFLICT    167    167       Q -> H (in Ref. 1; CAA68549).
FT                                {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
//
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