GenomeNet

Database: UniProt/SWISS-PROT
Entry: SODC_BOVIN
LinkDB: SODC_BOVIN
Original site: SODC_BOVIN 
ID   SODC_BOVIN              Reviewed;         152 AA.
AC   P00442; Q3ZCF4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   12-SEP-2018, entry version 174.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1 {ECO:0000269|PubMed:518876};
GN   Name=SOD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2263495; DOI=10.1093/nar/18.23.7171;
RA   Gibbs L.S., Shaffer J.B.;
RT   "Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA
RT   generated by the polymerase chain reaction.";
RL   Nucleic Acids Res. 18:7171-7171(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1958215; DOI=10.1016/S0006-291X(05)81443-3;
RA   Hallewell R.A., Imlay K.C., Lee P., Fong N.M., Gallegos C.,
RA   Getzoff E.D., Tainer J.A., Cabelli D.E., Tekamp-Olson P.,
RA   Mullenbach G.T., Cousens L.S.;
RT   "Thermostabilization of recombinant human and bovine CuZn superoxide
RT   dismutases by replacement of free cysteines.";
RL   Biochem. Biophys. Res. Commun. 181:474-480(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 2-152, AND ACETYLATION AT ALA-2.
RX   PubMed=4279916;
RA   Steinman H.M., Naik V.R., Abernethy J.L., Hill R.L.;
RT   "Bovine erythrocyte superoxide dismutase. Complete amino acid
RT   sequence.";
RL   J. Biol. Chem. 249:7326-7338(1974).
RN   [5]
RP   DISULFIDE BOND.
RX   PubMed=4436313;
RA   Abernethy J.L., Steinman H.M., Hill R.L.;
RT   "Bovine erythrocyte superoxide dismutase. Subunit structure and
RT   sequence location of the intrasubunit disulfide bond.";
RL   J. Biol. Chem. 249:7339-7347(1974).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION.
RX   PubMed=518876; DOI=10.1021/bi00593a023;
RA   Malinowski D.P., Friedovich I.;
RT   "Chemical modification of arginine at the active site of the bovine
RT   erythrocyte superoxide dismutase.";
RL   Biochemistry 18:5909-5917(1979).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=1055410; DOI=10.1073/pnas.72.4.1349;
RA   Richardson J.S., Thomas K.A., Rubin B.H., Richardson D.C.;
RT   "Crystal structure of bovine Cu,Zn superoxide dismutase at 3-A
RT   resolution: chain tracing and metal ligands.";
RL   Proc. Natl. Acad. Sci. U.S.A. 72:1349-1353(1975).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=7175933; DOI=10.1016/0022-2836(82)90174-7;
RA   Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S.,
RA   Richardson D.C.;
RT   "Determination and analysis of the 2 A-structure of copper, zinc
RT   superoxide dismutase.";
RL   J. Mol. Biol. 160:181-217(1982).
RN   [9]
RP   STRUCTURE, AND MECHANISM.
RX   PubMed=6316150; DOI=10.1038/306284a0;
RA   Tainer J.A., Getzoff E.D., Richardson J.S., Richardson D.C.;
RT   "Structure and mechanism of copper, zinc superoxide dismutase.";
RL   Nature 306:284-287(1983).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=1619651; DOI=10.1016/0022-2836(92)90135-7;
RA   Djinovic K., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M.,
RA   Rotilio G., Bolognesi M.;
RT   "Crystal structure solution and refinement of the semisynthetic
RT   cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0-A
RT   resolution.";
RL   J. Mol. Biol. 226:227-238(1992).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=7643403; DOI=10.1006/jmbi.1995.0434;
RA   Rypniewski W.R., Mangani S., Bruni B., Orioli P.L., Casati M.,
RA   Wilson K.S.;
RT   "Crystal structure of reduced bovine erythrocyte superoxide dismutase
RT   at 1.9-A resolution.";
RL   J. Mol. Biol. 251:282-296(1995).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=10092461; DOI=10.1006/jmbi.1999.2610;
RA   Hough M.A., Hasnain S.S.;
RT   "Crystallographic structures of bovine copper-zinc superoxide
RT   dismutase reveal asymmetry in two subunits: functionally important
RT   three and five coordinate copper sites captured in the same crystal.";
RL   J. Mol. Biol. 287:579-592(1999).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
RP   IONS, AND SUBUNIT.
RX   PubMed=12906825; DOI=10.1016/S0969-2126(03)00155-2;
RA   Hough M.A., Hasnain S.S.;
RT   "Structure of fully reduced bovine copper zinc superoxide dismutase at
RT   1.15 A.";
RL   Structure 11:937-946(2003).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000269|PubMed:518876}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000269|PubMed:518876}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12906825}.
CC   -!- INTERACTION:
CC       P62998:RAC1; NbExp=2; IntAct=EBI-6654424, EBI-6654511;
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   -!- MISCELLANEOUS: Chemical modification of Arg-142 reduces activity
CC       by 80-90%. {ECO:0000269|PubMed:518876}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/SODBE/";
DR   EMBL; X54799; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M81129; AAA73164.1; -; mRNA.
DR   EMBL; BC102432; AAI02433.1; -; mRNA.
DR   PIR; I45883; DSBOCZ.
DR   RefSeq; NP_777040.1; NM_174615.2.
DR   UniGene; Bt.49637; -.
DR   PDB; 1CB4; X-ray; 2.30 A; A/B=2-152.
DR   PDB; 1CBJ; X-ray; 1.65 A; A/B=2-152.
DR   PDB; 1COB; X-ray; 2.00 A; A/B=2-152.
DR   PDB; 1E9O; X-ray; 1.85 A; A/B=2-152.
DR   PDB; 1E9P; X-ray; 1.70 A; A/B=2-151.
DR   PDB; 1E9Q; X-ray; 1.75 A; A/B=2-152.
DR   PDB; 1Q0E; X-ray; 1.15 A; A/B=2-152.
DR   PDB; 1SDA; X-ray; 2.50 A; B/G/O/Y=2-152.
DR   PDB; 1SXA; X-ray; 1.90 A; A/B=2-152.
DR   PDB; 1SXB; X-ray; 2.00 A; A/B=2-152.
DR   PDB; 1SXC; X-ray; 1.90 A; A/B=2-152.
DR   PDB; 1SXN; X-ray; 1.90 A; A/B=2-152.
DR   PDB; 1SXS; X-ray; 2.00 A; A/B=2-152.
DR   PDB; 1SXZ; X-ray; 2.05 A; A/B=2-152.
DR   PDB; 2AEO; X-ray; 1.80 A; A/B=2-152.
DR   PDB; 2SOD; X-ray; 2.00 A; B/G/O/Y=2-152.
DR   PDB; 2Z7U; X-ray; 2.10 A; A/B=2-152.
DR   PDB; 2Z7W; X-ray; 1.80 A; A/B=2-152.
DR   PDB; 2Z7Y; X-ray; 1.55 A; A/B=2-152.
DR   PDB; 2Z7Z; X-ray; 1.85 A; A/B=2-152.
DR   PDB; 2ZOW; X-ray; 1.45 A; A/B=2-152.
DR   PDB; 3HW7; X-ray; 2.00 A; A/B=2-152.
DR   PDB; 3SOD; X-ray; 2.10 A; B/G/O/Y=2-152.
DR   PDBsum; 1CB4; -.
DR   PDBsum; 1CBJ; -.
DR   PDBsum; 1COB; -.
DR   PDBsum; 1E9O; -.
DR   PDBsum; 1E9P; -.
DR   PDBsum; 1E9Q; -.
DR   PDBsum; 1Q0E; -.
DR   PDBsum; 1SDA; -.
DR   PDBsum; 1SXA; -.
DR   PDBsum; 1SXB; -.
DR   PDBsum; 1SXC; -.
DR   PDBsum; 1SXN; -.
DR   PDBsum; 1SXS; -.
DR   PDBsum; 1SXZ; -.
DR   PDBsum; 2AEO; -.
DR   PDBsum; 2SOD; -.
DR   PDBsum; 2Z7U; -.
DR   PDBsum; 2Z7W; -.
DR   PDBsum; 2Z7Y; -.
DR   PDBsum; 2Z7Z; -.
DR   PDBsum; 2ZOW; -.
DR   PDBsum; 3HW7; -.
DR   PDBsum; 3SOD; -.
DR   ProteinModelPortal; P00442; -.
DR   SMR; P00442; -.
DR   IntAct; P00442; 2.
DR   STRING; 9913.ENSBTAP00000032384; -.
DR   BindingDB; P00442; -.
DR   iPTMnet; P00442; -.
DR   PaxDb; P00442; -.
DR   PeptideAtlas; P00442; -.
DR   PRIDE; P00442; -.
DR   Ensembl; ENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
DR   GeneID; 281495; -.
DR   KEGG; bta:281495; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P00442; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   TreeFam; TF105131; -.
DR   BRENDA; 1.15.1.1; 908.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
DR   EvolutionaryTrace; P00442; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000018854; Expressed in 10 organ(s), highest expression level in liver.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; 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: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; ISS:UniProtKB.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IDA:UniProtKB.
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: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:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
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:0001817; P:regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA: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:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
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:0010033; P:response to organic substance; ISS:UniProtKB.
DR   GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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   3D-structure; Acetylation; Antioxidant; Complete proteome; Copper;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; Lipoprotein;
KW   Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4279916}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164049.
FT   METAL        45     45       Copper; catalytic.
FT                                {ECO:0000269|PubMed:1055410,
FT                                ECO:0000269|PubMed:12906825}.
FT   METAL        47     47       Copper; catalytic.
FT                                {ECO:0000269|PubMed:1055410,
FT                                ECO:0000269|PubMed:12906825}.
FT   METAL        62     62       Copper; catalytic.
FT                                {ECO:0000269|PubMed:1055410,
FT                                ECO:0000269|PubMed:12906825}.
FT   METAL        62     62       Zinc; structural.
FT                                {ECO:0000269|PubMed:1055410}.
FT   METAL        70     70       Zinc; structural.
FT                                {ECO:0000269|PubMed:1055410}.
FT   METAL        79     79       Zinc; structural.
FT                                {ECO:0000269|PubMed:1055410}.
FT   METAL        82     82       Zinc; structural.
FT                                {ECO:0000269|PubMed:1055410}.
FT   METAL       119    119       Copper; catalytic.
FT                                {ECO:0000269|PubMed:1055410,
FT                                ECO:0000269|PubMed:12906825}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:4279916}.
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      90     90       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     121    121       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     121    121       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     135    135       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     135    135       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000269|PubMed:4436313}.
FT   STRAND        4     10       {ECO:0000244|PDB:1Q0E}.
FT   STRAND       12     14       {ECO:0000244|PDB:1Q0E}.
FT   STRAND       16     24       {ECO:0000244|PDB:1Q0E}.
FT   STRAND       27     36       {ECO:0000244|PDB:1Q0E}.
FT   STRAND       39     48       {ECO:0000244|PDB:1Q0E}.
FT   TURN         53     56       {ECO:0000244|PDB:1Q0E}.
FT   HELIX        57     59       {ECO:0000244|PDB:1Q0E}.
FT   STRAND       76     78       {ECO:0000244|PDB:2Z7Y}.
FT   STRAND       82     88       {ECO:0000244|PDB:1Q0E}.
FT   TURN         90     92       {ECO:0000244|PDB:2SOD}.
FT   STRAND       94    102       {ECO:0000244|PDB:1Q0E}.
FT   STRAND      104    107       {ECO:0000244|PDB:1Q0E}.
FT   STRAND      114    121       {ECO:0000244|PDB:1Q0E}.
FT   STRAND      128    130       {ECO:0000244|PDB:1Q0E}.
FT   HELIX       133    136       {ECO:0000244|PDB:1Q0E}.
FT   STRAND      141    147       {ECO:0000244|PDB:1Q0E}.
FT   STRAND      149    152       {ECO:0000244|PDB:1SDA}.
SQ   SEQUENCE   152 AA;  15683 MW;  A467EE17E4C31CCD CRC64;
     MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG
     PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE
     KPDDLGRGGN EESTKTGNAG SRLACGVIGI AK
//
DBGET integrated database retrieval system