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P00442

- SODC_BOVIN

UniProt

P00442 - SODC_BOVIN

Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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; 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

    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

    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

    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

    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.

    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

    1
    152
    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.
    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 146 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