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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_RAT                Reviewed;         154 AA.
P07632;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 171.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Name=Sod1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3628012; DOI=10.1093/nar/15.16.6746;
Ho Y.-S., Crapo J.D.;
"cDNA and deduced amino acid sequence of rat copper-zinc-containing
superoxide dismutase.";
Nucleic Acids Res. 15:6746-6746(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=2703531; DOI=10.1172/JCI114007;
Hass M.A., Iqbal J., Clerch L.B., Frank L., Massaro D.;
"Rat lung Cu,Zn superoxide dismutase. Isolation and sequence of a
full-length cDNA and studies of enzyme induction.";
J. Clin. Invest. 83:1241-1246(1989).
[3]
NUCLEOTIDE SEQUENCE.
PubMed=1379810; DOI=10.1016/0006-291X(92)90836-A;
Hsu J.L., Visner G.A., Burr I.A., Nick H.S.;
"Rat copper/zinc superoxide dismutase gene: isolation,
characterization, and species comparison.";
Biochem. Biophys. Res. Commun. 186:936-943(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8224914; DOI=10.1016/0378-1119(93)90650-R;
Kim Y.H., Yoo H.Y., Jung G., Kim J.Y., Rho H.M.;
"Isolation and analysis of the rat genomic sequence encoding Cu/Zn
superoxide dismutase.";
Gene 133:267-271(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-154.
PubMed=3790250;
Steffens G.J., Michelson A.M., Puget K., Flohe L.;
"The amino-acid sequence of rat Cu-Zn superoxide dismutase.";
Biol. Chem. Hoppe-Seyler 367:1017-1024(1986).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-154.
TISSUE=Liver;
PubMed=3595611; DOI=10.1111/j.1432-1033.1987.tb13500.x;
Delabar J.-M., Nicole A., D'Auriol L., Jacob Y., Meunier-Rotival M.,
Galibert F., Sinet P.-M., Jerome H.;
"Cloning and sequencing of a rat CuZn superoxide dismutase cDNA.
Correlation between CuZn superoxide dismutase mRNA level and enzyme
activity in rat and mouse tissues.";
Eur. J. Biochem. 166:181-187(1987).
[8]
PROTEIN SEQUENCE OF 2-21 AND 93-103.
PubMed=8837775; DOI=10.1038/383434a0;
Wang X., Culotta V.C., Klee C.B.;
"Superoxide dismutase protects calcineurin from inactivation.";
Nature 383:434-437(1996).
[9]
PROTEIN SEQUENCE OF 11-24; 81-116 AND 145-154, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-106 AND SER-108,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
-!- PTM: Palmitoylation helps nuclear targeting and decreases
catalytic activity. {ECO:0000250}.
-!- PTM: Succinylation, adjacent to copper catalytic site, probably
inhibits activity. Desuccinylation by SIRT5 enhances activity.
{ECO:0000250|UniProtKB:P00441}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA42160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA79925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y00404; CAA68465.1; -; mRNA.
EMBL; M25157; AAA42160.1; ALT_INIT; mRNA.
EMBL; X05634; CAA29121.1; -; mRNA.
EMBL; Z21917; CAA79925.1; ALT_INIT; Genomic_DNA.
EMBL; Z21918; CAA79925.1; JOINED; Genomic_DNA.
EMBL; Z21919; CAA79925.1; JOINED; Genomic_DNA.
EMBL; Z21920; CAA79925.1; JOINED; Genomic_DNA.
EMBL; BC082800; AAH82800.1; -; mRNA.
PIR; JC1192; JC1192.
RefSeq; NP_058746.1; NM_017050.1.
UniGene; Rn.6059; -.
ProteinModelPortal; P07632; -.
SMR; P07632; -.
BioGrid; 246910; 4.
IntAct; P07632; 1.
MINT; P07632; -.
STRING; 10116.ENSRNOP00000002885; -.
CarbonylDB; P07632; -.
iPTMnet; P07632; -.
PhosphoSitePlus; P07632; -.
PaxDb; P07632; -.
PRIDE; P07632; -.
Ensembl; ENSRNOT00000002885; ENSRNOP00000002885; ENSRNOG00000002115.
GeneID; 24786; -.
KEGG; rno:24786; -.
UCSC; RGD:3731; rat.
CTD; 6647; -.
RGD; 3731; Sod1.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; P07632; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG091G0OG2; -.
PhylomeDB; P07632; -.
TreeFam; TF105131; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:P07632; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000002115; -.
Genevisible; P07632; RN.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
GO; GO:0031045; C:dense core granule; IDA:RGD.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:CACAO.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; IMP:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
GO; GO:0004784; F:superoxide dismutase activity; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0071318; P:cellular response to ATP; IEP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
GO; GO:0035865; P:cellular response to potassium ion; IEP:RGD.
GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:RGD.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; IDA:RGD.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0097332; P:response to antipsychotic drug; IEP:RGD.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
GO; GO:0046688; P:response to copper ion; IMP:RGD.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
GO; GO:0006801; P:superoxide metabolic process; IDA:RGD.
GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00442,
ECO:0000269|PubMed:3790250,
ECO:0000269|PubMed:8837775}.
CHAIN 2 154 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164067.
METAL 47 47 Copper; catalytic. {ECO:0000250}.
METAL 49 49 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Zinc; structural. {ECO:0000250}.
METAL 72 72 Zinc; structural. {ECO:0000250}.
METAL 81 81 Zinc; structural. {ECO:0000250}.
METAL 84 84 Zinc; structural. {ECO:0000250}.
METAL 121 121 Copper; catalytic. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P00442}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 92 92 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 123 123 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 137 137 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 137 137 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
DISULFID 58 147 {ECO:0000250}.
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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