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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Copper; catalytic2 Publications
Metal bindingi47 – 471Copper; catalytic2 Publications
Metal bindingi62 – 621Copper; catalytic2 Publications
Metal bindingi62 – 621Zinc; structural1 Publication
Metal bindingi70 – 701Zinc; structural1 Publication
Metal bindingi79 – 791Zinc; structural1 Publication
Metal bindingi82 – 821Zinc; structural1 Publication
Metal bindingi119 – 1191Copper; catalytic2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.15.1.1. 908.
ReactomeiREACT_272065. Platelet degranulation.
REACT_296224. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 152151Superoxide dismutase [Cu-Zn]PRO_0000164049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei4 – 41N6-succinyllysineBy similarity
Lipidationi7 – 71S-palmitoyl cysteineBy similarity
Modified residuei10 – 101N6-succinyllysineBy similarity
Disulfide bondi56 ↔ 1451 Publication
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei121 – 1211N6-acetyllysine; alternateBy similarity
Modified residuei121 – 1211N6-succinyllysine; alternateBy similarity
Modified residuei135 – 1351N6-acetyllysine; alternateBy similarity
Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP00442.
PRIDEiP00442.

Expressioni

Gene expression databases

ExpressionAtlasiP00442. baseline.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAC1P629982EBI-6654424,EBI-6654511

Protein-protein interaction databases

IntActiP00442. 1 interaction.
STRINGi9913.ENSBTAP00000032384.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi12 – 143Combined sources
Beta strandi16 – 249Combined sources
Beta strandi27 – 3610Combined sources
Beta strandi39 – 4810Combined sources
Turni53 – 564Combined sources
Helixi57 – 593Combined sources
Beta strandi76 – 783Combined sources
Beta strandi82 – 887Combined sources
Turni90 – 923Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi114 – 1218Combined sources
Beta strandi128 – 1303Combined sources
Helixi133 – 1364Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi149 – 1524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00442.
SMRiP00442. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00442.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiCOG2032.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP00442.
KOiK04565.
OMAiQDGDAPT.
OrthoDBiEOG776SR4.
TreeFamiTF105131.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG
60 70 80 90 100
DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD
110 120 130 140 150
PLISLSGEYS IIGRTMVVHE KPDDLGRGGN EESTKTGNAG SRLACGVIGI

AK
Length:152
Mass (Da):15,683
Last modified:January 23, 2007 - v2
Checksum:iA467EE17E4C31CCD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54799 mRNA. No translation available.
M81129 mRNA. Translation: AAA73164.1.
BC102432 mRNA. Translation: AAI02433.1.
PIRiI45883. DSBOCZ.
RefSeqiNP_777040.1. NM_174615.2.
UniGeneiBt.49637.

Genome annotation databases

EnsembliENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
GeneIDi281495.
KEGGibta:281495.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54799 mRNA. No translation available.
M81129 mRNA. Translation: AAA73164.1.
BC102432 mRNA. Translation: AAI02433.1.
PIRiI45883. DSBOCZ.
RefSeqiNP_777040.1. NM_174615.2.
UniGeneiBt.49637.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00442.
SMRiP00442. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00442. 1 interaction.
STRINGi9913.ENSBTAP00000032384.

Proteomic databases

PaxDbiP00442.
PRIDEiP00442.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
GeneIDi281495.
KEGGibta:281495.

Organism-specific databases

CTDi6647.

Phylogenomic databases

eggNOGiCOG2032.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP00442.
KOiK04565.
OMAiQDGDAPT.
OrthoDBiEOG776SR4.
TreeFamiTF105131.

Enzyme and pathway databases

BRENDAi1.15.1.1. 908.
ReactomeiREACT_272065. Platelet degranulation.
REACT_296224. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiP00442.
NextBioi20805469.

Gene expression databases

ExpressionAtlasiP00442. baseline.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSODC_BOVIN
AccessioniPrimary (citable) accession number: P00442
Secondary accession number(s): Q3ZCF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.