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Q8WNN6

- SODC_CANFA

UniProt

Q8WNN6 - SODC_CANFA

Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

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

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi46 – 461Copper; catalyticBy similarity
    Metal bindingi48 – 481Copper; catalyticBy similarity
    Metal bindingi63 – 631Copper; catalyticBy similarity
    Metal bindingi63 – 631Zinc; structuralBy similarity
    Metal bindingi71 – 711Zinc; structuralBy similarity
    Metal bindingi80 – 801Zinc; structuralBy similarity
    Metal bindingi83 – 831Zinc; structuralBy similarity
    Metal bindingi120 – 1201Copper; catalyticBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. superoxide dismutase activity Source: UniProtKB

    GO - Biological processi

    1. reactive oxygen species metabolic process Source: UniProtKB
    2. removal of superoxide radicals Source: GOC

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
    Gene namesi
    Name:SOD1
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 153152Superoxide dismutase [Cu-Zn]PRO_0000164051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41N6-succinyllysineBy similarity
    Lipidationi7 – 71S-palmitoyl cysteineBy similarity
    Modified residuei10 – 101N6-succinyllysineBy similarity
    Disulfide bondi57 ↔ 146By similarity
    Modified residuei91 – 911N6-succinyllysineBy similarity
    Modified residuei98 – 981PhosphoserineBy similarity
    Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-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, Phosphoprotein

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Phylogenomic databases

    HOVERGENiHBG000062.
    KOiK04565.

    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.
    PROSITEiPS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8WNN6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMKAVCVLK GQGPVEGTIH FVQKGSGPVV VSGTITGLTE GEHGFHVHQF    50
    EDXTQGCTSA GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE 100
    DSLIALSGDY SIIGRTMVVH EKRDDLGKGD NEESTQTGNA GSRLACGVIG 150
    IAQ 153
    Length:153
    Mass (Da):15,913
    Last modified:March 1, 2002 - v1
    Checksum:i0D7900E59C57E6B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF346417 mRNA. Translation: AAL61608.1.
    RefSeqiNP_001003035.1. NM_001003035.1.
    UniGeneiCfa.6360.

    Genome annotation databases

    GeneIDi403559.
    KEGGicfa:403559.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF346417 mRNA. Translation: AAL61608.1 .
    RefSeqi NP_001003035.1. NM_001003035.1.
    UniGenei Cfa.6360.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403559.
    KEGGi cfa:403559.

    Organism-specific databases

    CTDi 6647.

    Phylogenomic databases

    HOVERGENi HBG000062.
    KOi K04565.

    Miscellaneous databases

    NextBioi 20817068.

    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 PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure, chromosomal location, and analysis of the canine Cu/Zn superoxide dismutase (SOD1) gene."
      Green S.L., Tolwani R.J., Varma S., Quignon P., Galibert F., Cork L.C.
      J. Hered. 93:119-124(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiSODC_CANFA
    AccessioniPrimary (citable) accession number: Q8WNN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3