Superoxide dismutase [Cu-Zn] - Bos taurus (Bovine)

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P00442 (SODC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 132. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1

Gene names

Name:

SOD1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation 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 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 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 proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein polyubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. 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 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 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
Cellular_component	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_function	chaperone binding Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB 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 ligase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from direct assay PubMed 17381088. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 152

151

Superoxide dismutase [Cu-Zn]

PRO_0000164049

Sites

Metal binding

Copper; catalytic Ref.6

Metal binding

Copper; catalytic Ref.6

Metal binding

Copper; catalytic Ref.6

Metal binding

Zinc; structural Ref.6

Metal binding

Zinc; structural Ref.6

Metal binding

Zinc; structural Ref.6

Metal binding

Zinc; structural Ref.6

Metal binding

119

Copper; catalytic Ref.6

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Modified residue

N6-acetyllysine By similarity

Modified residue

121

N6-acetyllysine By similarity

Disulfide bond

56 ↔ 145

Ref.5

Secondary structure

152

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00442 [UniParc].

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

FASTA

152

15,683

        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' referencesShow '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.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54799 mRNA. No translation available.
M81129 mRNA. Translation: AAA73164.1.
BC102432 mRNA. Translation: AAI02433.1.

IPI

IPI00713547.

PIR

DSBOCZ. I45883.

RefSeq

NP_777040.1. NM_174615.2.

UniGene

Bt.49637.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CB4	X-ray	2.30	A/B	2-152	[»]
1CBJ	X-ray	1.65	A/B	2-152	[»]
1COB	X-ray	2.00	A/B	2-152	[»]
1E9O	X-ray	1.85	A/B	2-151	[»]
1E9P	X-ray	1.70	A/B	2-151	[»]
1E9Q	X-ray	1.75	A/B	2-151	[»]
1Q0E	X-ray	1.15	A/B	2-152	[»]
1SDA	X-ray	2.50	B/G/O/Y	2-151	[»]
1SXA	X-ray	1.90	A/B	2-152	[»]
1SXB	X-ray	2.00	A/B	2-152	[»]
1SXC	X-ray	1.90	A/B	2-152	[»]
1SXN	X-ray	1.90	A/B	2-152	[»]
1SXS	X-ray	2.00	A/B	2-151	[»]
1SXZ	X-ray	2.05	A/B	2-151	[»]
2AEO	X-ray	1.80	A/B	2-151	[»]
2SOD	X-ray	2.00	B/G/O/Y	2-152	[»]
2Z7U	X-ray	2.10	A/B	2-152	[»]
2Z7W	X-ray	1.80	A/B	2-152	[»]
2Z7Y	X-ray	1.55	A/B	2-152	[»]
2Z7Z	X-ray	1.85	A/B	2-152	[»]
2ZOW	X-ray	1.45	A/B	2-152	[»]
3HW7	X-ray	2.00	A/B	2-152	[»]
3SOD	X-ray	2.10	B/G/O/Y	2-151	[»]

ProteinModelPortal

P00442.

SMR

P00442. Positions 2-152.

ModBase

Search...

Proteomic databases

PaxDb

P00442.

PRIDE

P00442.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.

GeneID

281495.

KEGG

bta:281495.

Organism-specific databases

CTD

6647.

Phylogenomic databases

eggNOG

COG2032.

GeneTree

ENSGT00530000063226.

HOGENOM

HOG000263447.

HOVERGEN

HBG000062.

InParanoid

P00442.

K04565.

OMA

NDPNAER.

OrthoDB

EOG45HRZM.

Family and domain databases

Gene3D

2.60.40.200. 1 hit.

InterPro

IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

PANTHER

PTHR10003. PTHR10003. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

SUPFAM

SSF49329. SOD_Cu_Zn. 1 hit.

PROSITE

PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00442.

NextBio

20805469.

Entry information

Entry name

SODC_BOVIN

Accession

Primary (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:	April 3, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents