Reviewed, UniProtKB/Swiss-Prot P00442 (SODC_BOVIN)

Names and origin

Protein names

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

Gene names

Name:

SOD1

Organism

Bos taurus (Bovine)

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 Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptosis Inferred from sequence or structural similarity. Source: UniProtKB activation of MAPK activity 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. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB muscle homeostasis Inferred from sequence or structural similarity. Source: UniProtKB myelin maintenance in the peripheral nervous system 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 apoptosis 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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from direct assay. 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	cell soma Inferred from direct assay. 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. 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 nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW 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 zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 152

151

Superoxide dismutase [Cu-Zn]

PRO_0000164049

Sites

Metal binding

45

1

Copper; catalytic Ref.6

Metal binding

47

1

Copper; catalytic Ref.6

Metal binding

62

1

Copper; catalytic Ref.6

Metal binding

62

1

Zinc; structural Ref.6

Metal binding

70

1

Zinc; structural Ref.6

Metal binding

79

1

Zinc; structural Ref.6

Metal binding

82

1

Zinc; structural Ref.6

Metal binding

119

1

Copper; catalytic Ref.6

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

69

1

N6-acetyllysine By similarity

Modified residue

121

1

N6-acetyllysine By similarity

Disulfide bond

56 ↔ 145

Ref.5

Secondary structure

1

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152

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

12 – 14

3

Beta strand

16 – 24

9

Beta strand

27 – 36

10

Beta strand

39 – 48

10

Turn

53 – 56

4

Helix

57 – 59

3

Beta strand

82 – 88

7

Beta strand

94 – 102

9

Beta strand

104 – 107

4

Beta strand

114 – 121

8

Beta strand

128 – 130

3

Helix

133 – 136

4

Beta strand

141 – 147

7

Sequences

	Sequence		Length	Mass (Da)
	P00442-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A467EE17E4C31CCD	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

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: 2263495] [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: 1958215] [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: 4279916] [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: 4436313] [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: 1055410] [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: 7175933] [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: 6316150] [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: 1619651] [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: 7643403] [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: 10092461] [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: 12906825] [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.

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	2-151	[»]
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	[»]
3SOD	X-ray	2.10	B/G/O/Y	2-151	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P00442.

Proteomic databases

PRIDE

P00442.

Genome annotation databases

Ensembl

ENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854; Bos taurus. [Genome view]

GeneID

281495.

KEGG

bta:281495.

Organism-specific databases

CTD

281495.

Phylogenomic databases

eggNOG

maNOG19511.

HOVERGEN

P00442.

InParanoid

P00442.

OMA

SGTIWIT.

OrthoDB

EOG93JFQH.

PhylomeDB

P00442.

Enzyme and pathway databases

BRENDA

1.15.1.1. 251.

Family and domain databases

InterPro

IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]

Gene3D

G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.

PANTHER

PTHR10003. SOD_Cu_Zn. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

PROSITE

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

ProtoNet

Search...

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:	January 19, 2010
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)