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Database: UniProt/SWISS-PROT
Entry: SODC_RAT
LinkDB: SODC_RAT
Original site: SODC_RAT 
ID   SODC_RAT                Reviewed;         154 AA.
AC   P07632;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-OCT-2017, entry version 166.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=Sod1;
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=3628012; DOI=10.1093/nar/15.16.6746;
RA   Ho Y.-S., Crapo J.D.;
RT   "cDNA and deduced amino acid sequence of rat copper-zinc-containing
RT   superoxide dismutase.";
RL   Nucleic Acids Res. 15:6746-6746(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=2703531; DOI=10.1172/JCI114007;
RA   Hass M.A., Iqbal J., Clerch L.B., Frank L., Massaro D.;
RT   "Rat lung Cu,Zn superoxide dismutase. Isolation and sequence of a
RT   full-length cDNA and studies of enzyme induction.";
RL   J. Clin. Invest. 83:1241-1246(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1379810; DOI=10.1016/0006-291X(92)90836-A;
RA   Hsu J.L., Visner G.A., Burr I.A., Nick H.S.;
RT   "Rat copper/zinc superoxide dismutase gene: isolation,
RT   characterization, and species comparison.";
RL   Biochem. Biophys. Res. Commun. 186:936-943(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8224914; DOI=10.1016/0378-1119(93)90650-R;
RA   Kim Y.H., Yoo H.Y., Jung G., Kim J.Y., Rho H.M.;
RT   "Isolation and analysis of the rat genomic sequence encoding Cu/Zn
RT   superoxide dismutase.";
RL   Gene 133:267-271(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [6]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=3790250;
RA   Steffens G.J., Michelson A.M., Puget K., Flohe L.;
RT   "The amino-acid sequence of rat Cu-Zn superoxide dismutase.";
RL   Biol. Chem. Hoppe-Seyler 367:1017-1024(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-154.
RC   TISSUE=Liver;
RX   PubMed=3595611; DOI=10.1111/j.1432-1033.1987.tb13500.x;
RA   Delabar J.-M., Nicole A., D'Auriol L., Jacob Y., Meunier-Rotival M.,
RA   Galibert F., Sinet P.-M., Jerome H.;
RT   "Cloning and sequencing of a rat CuZn superoxide dismutase cDNA.
RT   Correlation between CuZn superoxide dismutase mRNA level and enzyme
RT   activity in rat and mouse tissues.";
RL   Eur. J. Biochem. 166:181-187(1987).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-21 AND 93-103.
RX   PubMed=8837775; DOI=10.1038/383434a0;
RA   Wang X., Culotta V.C., Klee C.B.;
RT   "Superoxide dismutase protects calcineurin from inactivation.";
RL   Nature 383:434-437(1996).
RN   [9]
RP   PROTEIN SEQUENCE OF 11-24; 81-116 AND 145-154, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-106 AND SER-108,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic activity. {ECO:0000250}.
CC   -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC       inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC       {ECO:0000250|UniProtKB:P00441}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA79925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; Y00404; CAA68465.1; -; mRNA.
DR   EMBL; M25157; AAA42160.1; ALT_INIT; mRNA.
DR   EMBL; X05634; CAA29121.1; -; mRNA.
DR   EMBL; Z21917; CAA79925.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z21918; CAA79925.1; JOINED; Genomic_DNA.
DR   EMBL; Z21919; CAA79925.1; JOINED; Genomic_DNA.
DR   EMBL; Z21920; CAA79925.1; JOINED; Genomic_DNA.
DR   EMBL; BC082800; AAH82800.1; -; mRNA.
DR   PIR; JC1192; JC1192.
DR   RefSeq; NP_058746.1; NM_017050.1.
DR   UniGene; Rn.6059; -.
DR   ProteinModelPortal; P07632; -.
DR   SMR; P07632; -.
DR   BioGrid; 246910; 4.
DR   IntAct; P07632; 1.
DR   MINT; MINT-6612994; -.
DR   STRING; 10116.ENSRNOP00000002885; -.
DR   iPTMnet; P07632; -.
DR   PhosphoSitePlus; P07632; -.
DR   PaxDb; P07632; -.
DR   PRIDE; P07632; -.
DR   Ensembl; ENSRNOT00000002885; ENSRNOP00000002885; ENSRNOG00000002115.
DR   GeneID; 24786; -.
DR   KEGG; rno:24786; -.
DR   UCSC; RGD:3731; rat.
DR   CTD; 6647; -.
DR   RGD; 3731; Sod1.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P07632; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; P07632; -.
DR   TreeFam; TF105131; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P07632; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000002115; -.
DR   Genevisible; P07632; RN.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031045; C:dense core granule; IDA:RGD.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:CACAO.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IDA:RGD.
DR   GO; GO:0030141; C:secretory granule; IDA:RGD.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IMP:RGD.
DR   GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
DR   GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0071318; P:cellular response to ATP; IEP:RGD.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR   GO; GO:0035865; P:cellular response to potassium ion; IEP:RGD.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:RGD.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
DR   GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; IDA:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR   GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEP:RGD.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
DR   GO; GO:0046688; P:response to copper ion; IMP:RGD.
DR   GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
DR   GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR   GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0006801; P:superoxide metabolic process; IDA:RGD.
DR   GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
KW   Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00442,
FT                                ECO:0000269|PubMed:3790250,
FT                                ECO:0000269|PubMed:8837775}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164067.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; structural. {ECO:0000250}.
FT   METAL        72     72       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL        84     84       Zinc; structural. {ECO:0000250}.
FT   METAL       121    121       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      10     10       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      92     92       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      99     99       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     137    137       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     137    137       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
SQ   SEQUENCE   154 AA;  15912 MW;  B7D93A135E9279E9 CRC64;
     MAMKAVCVLK GDGPVQGVIH FEQKASGEPV VVSGQITGLT EGEHGFHVHQ YGDNTQGCTT
     AGPHFNPHSK KHGGPADEER HVGDLGNVAA GKDGVANVSI EDRVISLSGE HSIIGRTMVV
     HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ
//
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