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 03-AUG-2022, entry version 192.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1 {ECO:0000305|PubMed:2703531};
GN Name=Sod1;
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=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], TISSUE SPECIFICITY, INDUCTION BY HYPOXIA, AND
RP CATALYTIC ACTIVITY.
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 full-
RT 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, characterization,
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=3790250; DOI=10.1515/bchm3.1986.367.2.1017;
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 MASS
RP 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, AND
RP 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., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT 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:
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 Evidence={ECO:0000305|PubMed:2703531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000305|PubMed:2703531};
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 -!- TISSUE SPECIFICITY: Expressed in lungs. {ECO:0000269|PubMed:2703531}.
CC -!- INDUCTION: Expression is induced by hypoxia.
CC {ECO:0000269|PubMed:2703531}.
CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic
CC 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; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA79925.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; P07632; -.
DR SMR; P07632; -.
DR BioGRID; 246910; 4.
DR IntAct; P07632; 1.
DR MINT; P07632; -.
DR STRING; 10116.ENSRNOP00000002885; -.
DR CarbonylDB; P07632; -.
DR iPTMnet; P07632; -.
DR PhosphoSitePlus; P07632; -.
DR jPOST; P07632; -.
DR PaxDb; P07632; -.
DR PRIDE; P07632; -.
DR GeneID; 24786; -.
DR KEGG; rno:24786; -.
DR UCSC; RGD:3731; rat.
DR CTD; 6647; -.
DR RGD; 3731; Sod1.
DR VEuPathDB; HostDB:ENSRNOG00000002115; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P07632; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P07632; -.
DR TreeFam; TF105131; -.
DR BRENDA; 1.15.1.1; 5301.
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; Expressed in kidney and 20 other tissues.
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:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
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: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:0032991; C:protein-containing 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; ISO:RGD.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; ISO:RGD.
DR GO; GO:0008089; P:anterograde axonal transport; ISO:RGD.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; 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: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:0050728; P:negative regulation of inflammatory response; ISO:RGD.
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:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:RGD.
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; ISO:RGD.
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 associated 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: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:0000302; P:response to reactive oxygen species; ISO:RGD.
DR GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
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; ISO:RGD.
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; Copper; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase;
KW Palmitate; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00442,
FT ECO:0000269|PubMed:3790250, ECO:0000269|PubMed:8837775"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164067"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00442"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 92
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 123
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 137
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 137
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 58..147
FT /evidence="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
