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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_BOVIN              Reviewed;         152 AA.
P00442; Q3ZCF4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1 {ECO:0000269|PubMed:518876};
Name=SOD1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2263495; DOI=10.1093/nar/18.23.7171;
Gibbs L.S., Shaffer J.B.;
"Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA
generated by the polymerase chain reaction.";
Nucleic Acids Res. 18:7171-7171(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1958215; DOI=10.1016/S0006-291X(05)81443-3;
Hallewell R.A., Imlay K.C., Lee P., Fong N.M., Gallegos C.,
Getzoff E.D., Tainer J.A., Cabelli D.E., Tekamp-Olson P.,
Mullenbach G.T., Cousens L.S.;
"Thermostabilization of recombinant human and bovine CuZn superoxide
dismutases by replacement of free cysteines.";
Biochem. Biophys. Res. Commun. 181:474-480(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-152, AND ACETYLATION AT ALA-2.
PubMed=4279916;
Steinman H.M., Naik V.R., Abernethy J.L., Hill R.L.;
"Bovine erythrocyte superoxide dismutase. Complete amino acid
sequence.";
J. Biol. Chem. 249:7326-7338(1974).
[5]
DISULFIDE BOND.
PubMed=4436313;
Abernethy J.L., Steinman H.M., Hill R.L.;
"Bovine erythrocyte superoxide dismutase. Subunit structure and
sequence location of the intrasubunit disulfide bond.";
J. Biol. Chem. 249:7339-7347(1974).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION.
PubMed=518876; DOI=10.1021/bi00593a023;
Malinowski D.P., Friedovich I.;
"Chemical modification of arginine at the active site of the bovine
erythrocyte superoxide dismutase.";
Biochemistry 18:5909-5917(1979).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=1055410; DOI=10.1073/pnas.72.4.1349;
Richardson J.S., Thomas K.A., Rubin B.H., Richardson D.C.;
"Crystal structure of bovine Cu,Zn superoxide dismutase at 3-A
resolution: chain tracing and metal ligands.";
Proc. Natl. Acad. Sci. U.S.A. 72:1349-1353(1975).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=7175933; DOI=10.1016/0022-2836(82)90174-7;
Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S.,
Richardson D.C.;
"Determination and analysis of the 2 A-structure of copper, zinc
superoxide dismutase.";
J. Mol. Biol. 160:181-217(1982).
[9]
STRUCTURE, AND MECHANISM.
PubMed=6316150; DOI=10.1038/306284a0;
Tainer J.A., Getzoff E.D., Richardson J.S., Richardson D.C.;
"Structure and mechanism of copper, zinc superoxide dismutase.";
Nature 306:284-287(1983).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=1619651; DOI=10.1016/0022-2836(92)90135-7;
Djinovic K., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M.,
Rotilio G., Bolognesi M.;
"Crystal structure solution and refinement of the semisynthetic
cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0-A
resolution.";
J. Mol. Biol. 226:227-238(1992).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=7643403; DOI=10.1006/jmbi.1995.0434;
Rypniewski W.R., Mangani S., Bruni B., Orioli P.L., Casati M.,
Wilson K.S.;
"Crystal structure of reduced bovine erythrocyte superoxide dismutase
at 1.9-A resolution.";
J. Mol. Biol. 251:282-296(1995).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=10092461; DOI=10.1006/jmbi.1999.2610;
Hough M.A., Hasnain S.S.;
"Crystallographic structures of bovine copper-zinc superoxide
dismutase reveal asymmetry in two subunits: functionally important
three and five coordinate copper sites captured in the same crystal.";
J. Mol. Biol. 287:579-592(1999).
[13]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
IONS, AND SUBUNIT.
PubMed=12906825; DOI=10.1016/S0969-2126(03)00155-2;
Hough M.A., Hasnain S.S.;
"Structure of fully reduced bovine copper zinc superoxide dismutase at
1.15 A.";
Structure 11:937-946(2003).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
{ECO:0000269|PubMed:518876}.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
{ECO:0000269|PubMed:518876}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 1 copper ion per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12906825}.
-!- INTERACTION:
P62998:RAC1; NbExp=2; IntAct=EBI-6654424, EBI-6654511;
-!- 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}.
-!- MISCELLANEOUS: Chemical modification of Arg-142 reduces activity
by 80-90%. {ECO:0000269|PubMed:518876}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/SODBE/";
-----------------------------------------------------------------------
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EMBL; X54799; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M81129; AAA73164.1; -; mRNA.
EMBL; BC102432; AAI02433.1; -; mRNA.
PIR; I45883; DSBOCZ.
RefSeq; NP_777040.1; NM_174615.2.
UniGene; Bt.49637; -.
PDB; 1CB4; X-ray; 2.30 A; A/B=2-152.
PDB; 1CBJ; X-ray; 1.65 A; A/B=2-152.
PDB; 1COB; X-ray; 2.00 A; A/B=2-152.
PDB; 1E9O; X-ray; 1.85 A; A/B=2-152.
PDB; 1E9P; X-ray; 1.70 A; A/B=2-151.
PDB; 1E9Q; X-ray; 1.75 A; A/B=2-152.
PDB; 1Q0E; X-ray; 1.15 A; A/B=2-152.
PDB; 1SDA; X-ray; 2.50 A; B/G/O/Y=2-152.
PDB; 1SXA; X-ray; 1.90 A; A/B=2-152.
PDB; 1SXB; X-ray; 2.00 A; A/B=2-152.
PDB; 1SXC; X-ray; 1.90 A; A/B=2-152.
PDB; 1SXN; X-ray; 1.90 A; A/B=2-152.
PDB; 1SXS; X-ray; 2.00 A; A/B=2-152.
PDB; 1SXZ; X-ray; 2.05 A; A/B=2-152.
PDB; 2AEO; X-ray; 1.80 A; A/B=2-152.
PDB; 2SOD; X-ray; 2.00 A; B/G/O/Y=2-152.
PDB; 2Z7U; X-ray; 2.10 A; A/B=2-152.
PDB; 2Z7W; X-ray; 1.80 A; A/B=2-152.
PDB; 2Z7Y; X-ray; 1.55 A; A/B=2-152.
PDB; 2Z7Z; X-ray; 1.85 A; A/B=2-152.
PDB; 2ZOW; X-ray; 1.45 A; A/B=2-152.
PDB; 3HW7; X-ray; 2.00 A; A/B=2-152.
PDB; 3SOD; X-ray; 2.10 A; B/G/O/Y=2-152.
PDBsum; 1CB4; -.
PDBsum; 1CBJ; -.
PDBsum; 1COB; -.
PDBsum; 1E9O; -.
PDBsum; 1E9P; -.
PDBsum; 1E9Q; -.
PDBsum; 1Q0E; -.
PDBsum; 1SDA; -.
PDBsum; 1SXA; -.
PDBsum; 1SXB; -.
PDBsum; 1SXC; -.
PDBsum; 1SXN; -.
PDBsum; 1SXS; -.
PDBsum; 1SXZ; -.
PDBsum; 2AEO; -.
PDBsum; 2SOD; -.
PDBsum; 2Z7U; -.
PDBsum; 2Z7W; -.
PDBsum; 2Z7Y; -.
PDBsum; 2Z7Z; -.
PDBsum; 2ZOW; -.
PDBsum; 3HW7; -.
PDBsum; 3SOD; -.
ProteinModelPortal; P00442; -.
SMR; P00442; -.
IntAct; P00442; 1.
STRING; 9913.ENSBTAP00000032384; -.
iPTMnet; P00442; -.
PaxDb; P00442; -.
PeptideAtlas; P00442; -.
PRIDE; P00442; -.
Ensembl; ENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
GeneID; 281495; -.
KEGG; bta:281495; -.
CTD; 6647; -.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; P00442; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG091G0OG2; -.
TreeFam; TF105131; -.
BRENDA; 1.15.1.1; 908.
Reactome; R-BTA-114608; Platelet degranulation.
Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
EvolutionaryTrace; P00442; -.
Proteomes; UP000009136; Chromosome 1.
Bgee; ENSBTAG00000018854; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
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:0006302; P:double-strand break repair; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0044419; P:interspecies interaction between organisms; IDA:UniProtKB.
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: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:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; IDA:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA: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:UniProtKB.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
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:0010033; P:response to organic substance; ISS:UniProtKB.
GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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;
3D-structure; 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:0000269|PubMed:4279916}.
CHAIN 2 152 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164049.
METAL 45 45 Copper; catalytic.
{ECO:0000269|PubMed:1055410,
ECO:0000269|PubMed:12906825}.
METAL 47 47 Copper; catalytic.
{ECO:0000269|PubMed:1055410,
ECO:0000269|PubMed:12906825}.
METAL 62 62 Copper; catalytic.
{ECO:0000269|PubMed:1055410,
ECO:0000269|PubMed:12906825}.
METAL 62 62 Zinc; structural.
{ECO:0000269|PubMed:1055410}.
METAL 70 70 Zinc; structural.
{ECO:0000269|PubMed:1055410}.
METAL 79 79 Zinc; structural.
{ECO:0000269|PubMed:1055410}.
METAL 82 82 Zinc; structural.
{ECO:0000269|PubMed:1055410}.
METAL 119 119 Copper; catalytic.
{ECO:0000269|PubMed:1055410,
ECO:0000269|PubMed:12906825}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:4279916}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 90 90 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000250|UniProtKB:P07632}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 121 121 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 121 121 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 135 135 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 135 135 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
DISULFID 56 145 {ECO:0000269|PubMed:4436313}.
STRAND 4 10 {ECO:0000244|PDB:1Q0E}.
STRAND 12 14 {ECO:0000244|PDB:1Q0E}.
STRAND 16 24 {ECO:0000244|PDB:1Q0E}.
STRAND 27 36 {ECO:0000244|PDB:1Q0E}.
STRAND 39 48 {ECO:0000244|PDB:1Q0E}.
TURN 53 56 {ECO:0000244|PDB:1Q0E}.
HELIX 57 59 {ECO:0000244|PDB:1Q0E}.
STRAND 76 78 {ECO:0000244|PDB:2Z7Y}.
STRAND 82 88 {ECO:0000244|PDB:1Q0E}.
TURN 90 92 {ECO:0000244|PDB:2SOD}.
STRAND 94 102 {ECO:0000244|PDB:1Q0E}.
STRAND 104 107 {ECO:0000244|PDB:1Q0E}.
STRAND 114 121 {ECO:0000244|PDB:1Q0E}.
STRAND 128 130 {ECO:0000244|PDB:1Q0E}.
HELIX 133 136 {ECO:0000244|PDB:1Q0E}.
STRAND 141 147 {ECO:0000244|PDB:1Q0E}.
STRAND 149 152 {ECO:0000244|PDB:1SDA}.
SEQUENCE 152 AA; 15683 MW; A467EE17E4C31CCD CRC64;
MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG
PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE
KPDDLGRGGN EESTKTGNAG SRLACGVIGI AK


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