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P00442 (SODC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Gene names
Name:SOD1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer. Ref.12

Subcellular location

Cytoplasm. Nucleus By similarity.

Post-translational modification

Palmitoylation helps nuclear targeting and decreases catalytic activity By similarity.

Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic DNA fragmentation

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell stereocilium organization

Inferred from sequence or structural similarity. Source: UniProtKB

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

embryo implantation

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

heart contraction

Inferred from sequence or structural similarity. Source: UniProtKB

hydrogen peroxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

interspecies interaction between organisms

Inferred from direct assay PubMed 16930739. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell cellular homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neurofilament cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

ovarian follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

peripheral nervous system myelin maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catalytic activity

Inferred from direct assay PubMed 17324120. Source: UniProtKB

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 16930739. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein polyubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cytokine production

Inferred from direct assay PubMed 16930739. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from direct assay PubMed 16930739. Source: UniProtKB

regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

relaxation of vascular smooth muscle

Inferred from sequence or structural similarity. Source: UniProtKB

removal of superoxide radicals

Inferred from sequence or structural similarity. Source: UniProtKB

response to axon injury

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

response to ethanol

Inferred from sequence or structural similarity. Source: UniProtKB

response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

response to organic substance

Inferred from sequence or structural similarity. Source: UniProtKB

response to superoxide

Inferred from sequence or structural similarity. Source: UniProtKB

retina homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

transmission of nerve impulse

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite cytoplasm

Inferred from direct assay PubMed 17324120. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 17324120. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 17324120. Source: UniProtKB

   Molecular_functionchaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18219391. Source: IntAct

protein phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide dismutase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 17381088. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAC1P629982EBI-6654424,EBI-6654511

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 152151Superoxide dismutase [Cu-Zn]
PRO_0000164049

Sites

Metal binding451Copper; catalytic Ref.6
Metal binding471Copper; catalytic Ref.6
Metal binding621Copper; catalytic Ref.6
Metal binding621Zinc; structural Ref.6
Metal binding701Zinc; structural Ref.6
Metal binding791Zinc; structural Ref.6
Metal binding821Zinc; structural Ref.6
Metal binding1191Copper; catalytic Ref.6

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue41N6-succinyllysine By similarity
Modified residue101N6-succinyllysine By similarity
Modified residue901N6-succinyllysine By similarity
Modified residue1211N6-acetyllysine; alternate By similarity
Modified residue1211N6-succinyllysine; alternate By similarity
Modified residue1351N6-acetyllysine; alternate By similarity
Modified residue1351N6-succinyllysine; alternate By similarity
Lipidation71S-palmitoyl cysteine By similarity
Disulfide bond56 ↔ 145 Ref.5

Secondary structure

................................. 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00442 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A467EE17E4C31CCD

FASTA15215,683
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG 

        70         80         90        100        110        120 
PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE 

       130        140        150 
KPDDLGRGGN EESTKTGNAG SRLACGVIGI AK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA generated by the polymerase chain reaction."
Gibbs L.S., Shaffer J.B.
Nucleic Acids Res. 18:7171-7171(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines."
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.
Biochem. Biophys. Res. Commun. 181:474-480(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[4]"Bovine erythrocyte superoxide dismutase. Complete amino acid sequence."
Steinman H.M., Naik V.R., Abernethy J.L., Hill R.L.
J. Biol. Chem. 249:7326-7338(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-152.
[5]"Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond."
Abernethy J.L., Steinman H.M., Hill R.L.
J. Biol. Chem. 249:7339-7347(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[6]"Crystal structure of bovine Cu,Zn superoxide dismutase at 3-A resolution: chain tracing and metal ligands."
Richardson J.S., Thomas K.A., Rubin B.H., Richardson D.C.
Proc. Natl. Acad. Sci. U.S.A. 72:1349-1353(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]"Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase."
Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S., Richardson D.C.
J. Mol. Biol. 160:181-217(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"Structure and mechanism of copper, zinc superoxide dismutase."
Tainer J.A., Getzoff E.D., Richardson J.S., Richardson D.C.
Nature 306:284-287(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE, MECHANISM.
[9]"Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0-A resolution."
Djinovic K., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M., Rotilio G., Bolognesi M.
J. Mol. Biol. 226:227-238(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]"Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9-A resolution."
Rypniewski W.R., Mangani S., Bruni B., Orioli P.L., Casati M., Wilson K.S.
J. Mol. Biol. 251:282-296(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[11]"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."
Hough M.A., Hasnain S.S.
J. Mol. Biol. 287:579-592(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[12]"Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A."
Hough M.A., Hasnain S.S.
Structure 11:937-946(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54799 mRNA. No translation available.
M81129 mRNA. Translation: AAA73164.1.
BC102432 mRNA. Translation: AAI02433.1.
PIRDSBOCZ. I45883.
RefSeqNP_777040.1. NM_174615.2.
UniGeneBt.49637.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB4X-ray2.30A/B2-152[»]
1CBJX-ray1.65A/B2-152[»]
1COBX-ray2.00A/B2-152[»]
1E9OX-ray1.85A/B2-152[»]
1E9PX-ray1.70A/B2-151[»]
1E9QX-ray1.75A/B2-152[»]
1Q0EX-ray1.15A/B2-152[»]
1SDAX-ray2.50B/G/O/Y2-152[»]
1SXAX-ray1.90A/B2-152[»]
1SXBX-ray2.00A/B2-152[»]
1SXCX-ray1.90A/B2-152[»]
1SXNX-ray1.90A/B2-152[»]
1SXSX-ray2.00A/B2-152[»]
1SXZX-ray2.05A/B2-152[»]
2AEOX-ray1.80A/B2-152[»]
2SODX-ray2.00B/G/O/Y2-152[»]
2Z7UX-ray2.10A/B2-152[»]
2Z7WX-ray1.80A/B2-152[»]
2Z7YX-ray1.55A/B2-152[»]
2Z7ZX-ray1.85A/B2-152[»]
2ZOWX-ray1.45A/B2-152[»]
3HW7X-ray2.00A/B2-152[»]
3SODX-ray2.10B/G/O/Y2-152[»]
ProteinModelPortalP00442.
SMRP00442. Positions 2-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00442. 1 interaction.

Proteomic databases

PaxDbP00442.
PRIDEP00442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
GeneID281495.
KEGGbta:281495.

Organism-specific databases

CTD6647.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
HOGENOMHOG000263447.
HOVERGENHBG000062.
InParanoidP00442.
KOK04565.
OMANDPNAKR.
OrthoDBEOG776SR4.
TreeFamTF105131.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00442.
NextBio20805469.

Entry information

Entry nameSODC_BOVIN
AccessionPrimary (citable) accession number: P00442
Secondary accession number(s): Q3ZCF4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references