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P00442

- SODC_BOVIN

UniProt

P00442 - SODC_BOVIN

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Protein
Superoxide dismutase [Cu-Zn]
Gene
SOD1
Organism
Bos taurus (Bovine)
Status
Reviewed - 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

Binds 1 copper ion per subunit.
Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Copper; catalytic1 Publication
Metal bindingi47 – 471Copper; catalytic1 Publication
Metal bindingi62 – 621Copper; catalytic1 Publication
Metal bindingi62 – 621Zinc; structural1 Publication
Metal bindingi70 – 701Zinc; structural1 Publication
Metal bindingi79 – 791Zinc; structural1 Publication
Metal bindingi82 – 821Zinc; structural1 Publication
Metal bindingi119 – 1191Copper; catalytic1 Publication

GO - Molecular functioni

  1. chaperone binding Source: UniProtKB
  2. copper ion binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. protein phosphatase 2B binding Source: UniProtKB
  5. superoxide dismutase activity Source: UniProtKB
  6. ubiquitin-protein transferase activity Source: UniProtKB
  7. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. apoptotic DNA fragmentation Source: UniProtKB
  3. auditory receptor cell stereocilium organization Source: UniProtKB
  4. cell aging Source: UniProtKB
  5. cellular iron ion homeostasis Source: UniProtKB
  6. double-strand break repair Source: UniProtKB
  7. embryo implantation Source: UniProtKB
  8. glutathione metabolic process Source: UniProtKB
  9. heart contraction Source: UniProtKB
  10. hydrogen peroxide biosynthetic process Source: UniProtKB
  11. interspecies interaction between organisms Source: UniProtKB
  12. locomotory behavior Source: UniProtKB
  13. muscle cell cellular homeostasis Source: UniProtKB
  14. myeloid cell homeostasis Source: UniProtKB
  15. negative regulation of cholesterol biosynthetic process Source: UniProtKB
  16. negative regulation of neuron apoptotic process Source: UniProtKB
  17. neurofilament cytoskeleton organization Source: UniProtKB
  18. ovarian follicle development Source: UniProtKB
  19. peripheral nervous system myelin maintenance Source: UniProtKB
  20. positive regulation of catalytic activity Source: UniProtKB
  21. positive regulation of cytokine production Source: UniProtKB
  22. positive regulation of nitric-oxide synthase biosynthetic process Source: UniProtKB
  23. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  24. protein polyubiquitination Source: UniProtKB
  25. reactive oxygen species metabolic process Source: UniProtKB
  26. regulation of blood pressure Source: UniProtKB
  27. regulation of cytokine production Source: UniProtKB
  28. regulation of mitochondrial membrane potential Source: UniProtKB
  29. regulation of multicellular organism growth Source: UniProtKB
  30. regulation of protein kinase activity Source: UniProtKB
  31. relaxation of vascular smooth muscle Source: UniProtKB
  32. removal of superoxide radicals Source: UniProtKB
  33. response to axon injury Source: UniProtKB
  34. response to drug Source: UniProtKB
  35. response to ethanol Source: UniProtKB
  36. response to heat Source: UniProtKB
  37. response to hydrogen peroxide Source: UniProtKB
  38. response to organic substance Source: UniProtKB
  39. response to superoxide Source: UniProtKB
  40. retina homeostasis Source: UniProtKB
  41. sensory perception of sound Source: UniProtKB
  42. spermatogenesis Source: UniProtKB
  43. superoxide metabolic process Source: UniProtKB
  44. transmission of nerve impulse Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_204534. 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: Chromosome 1

Subcellular locationi

Cytoplasm. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. dendrite cytoplasm Source: UniProtKB
  5. extracellular matrix Source: UniProtKB
  6. extracellular space Source: UniProtKB
  7. mitochondrion Source: UniProtKB
  8. neuronal cell body Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. 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-succinyllysine By similarity
Lipidationi7 – 71S-palmitoyl cysteine By similarity
Modified residuei10 – 101N6-succinyllysine By similarity
Disulfide bondi56 ↔ 1451 Publication
Modified residuei90 – 901N6-succinyllysine By similarity
Modified residuei121 – 1211N6-acetyllysine; alternate By similarity
Modified residuei121 – 1211N6-succinyllysine; alternate By similarity
Modified residuei135 – 1351N6-acetyllysine; alternate By similarity
Modified residuei135 – 1351N6-succinyllysine; alternate By 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.

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP00442.
PRIDEiP00442.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

IntActiP00442. 1 interaction.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00442.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2032.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiP00442.
KOiK04565.
OMAiNDPNAKR.
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

MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG    50
DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD 100
PLISLSGEYS IIGRTMVVHE KPDDLGRGGN EESTKTGNAG SRLACGVIGI 150
AK 152
Length:152
Mass (Da):15,683
Last modified:January 23, 2007 - v2
Checksum:iA467EE17E4C31CCD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X54799 mRNA. No translation available.
M81129 mRNA. Translation: AAA73164.1 .
BC102432 mRNA. Translation: AAI02433.1 .
PIRi I45883. DSBOCZ.
RefSeqi NP_777040.1. NM_174615.2.
UniGenei Bt.49637.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-152 [» ]
1E9P X-ray 1.70 A/B 2-151 [» ]
1E9Q X-ray 1.75 A/B 2-152 [» ]
1Q0E X-ray 1.15 A/B 2-152 [» ]
1SDA X-ray 2.50 B/G/O/Y 2-152 [» ]
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 2-152 [» ]
1SXZ X-ray 2.05 A/B 2-152 [» ]
2AEO X-ray 1.80 A/B 2-152 [» ]
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 2-152 [» ]
ProteinModelPortali P00442.
SMRi P00442. Positions 2-152.
ModBasei Search...

Protein-protein interaction databases

IntActi P00442. 1 interaction.

Proteomic databases

PaxDbi P00442.
PRIDEi P00442.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000032452 ; ENSBTAP00000032384 ; ENSBTAG00000018854 .
GeneIDi 281495.
KEGGi bta:281495.

Organism-specific databases

CTDi 6647.

Phylogenomic databases

eggNOGi COG2032.
GeneTreei ENSGT00530000063226.
HOGENOMi HOG000263447.
HOVERGENi HBG000062.
InParanoidi P00442.
KOi K04565.
OMAi NDPNAKR.
OrthoDBi EOG776SR4.
TreeFami TF105131.

Enzyme and pathway databases

Reactomei REACT_204534. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTracei P00442.
NextBioi 20805469.

Family and domain databases

Gene3Di 2.60.40.200. 1 hit.
InterProi IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view ]
Pfami PF00080. Sod_Cu. 1 hit.
[Graphical view ]
PRINTSi PR00068. CUZNDISMTASE.
SUPFAMi SSF49329. SSF49329. 1 hit.
PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 145 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

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