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P15107

- SOD1B_XENLA

UniProt

P15107 - SOD1B_XENLA

Protein

Superoxide dismutase [Cu-Zn] B

Gene

sod1-b

Organism
Xenopus laevis (African clawed frog)
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; catalytic
    Metal bindingi47 – 471Copper; catalytic
    Metal bindingi62 – 621Copper; catalytic
    Metal bindingi62 – 621Zinc; structural
    Metal bindingi70 – 701Zinc; structural
    Metal bindingi79 – 791Zinc; structural
    Metal bindingi82 – 821Zinc; structural
    Metal bindingi118 – 1181Copper; catalytic

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] B (EC:1.15.1.1)
    Short name:
    XSODB
    Gene namesi
    Name:sod1-b
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6254670. sod1.

    Subcellular locationi

    Cytoplasm. 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 – 11Removed2 Publications
    Chaini2 – 151150Superoxide dismutase [Cu-Zn] BPRO_0000164077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi6 – 61S-palmitoyl cysteineBy similarity
    Disulfide bondi56 ↔ 144

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Palmitate

    Proteomic databases

    PRIDEiP15107.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer of Superoxide dismutase [Cu-Zn] A and B.1 Publication

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Beta strandi11 – 133
    Beta strandi15 – 239
    Beta strandi28 – 369
    Beta strandi39 – 4810
    Helixi55 – 595
    Beta strandi76 – 783
    Beta strandi82 – 898
    Beta strandi92 – 10110
    Beta strandi103 – 1064
    Beta strandi113 – 1208
    Beta strandi127 – 1293
    Helixi132 – 1354
    Beta strandi141 – 1466

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XSOX-ray1.49A/B2-151[»]
    ProteinModelPortaliP15107.
    SMRiP15107. Positions 2-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15107.

    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.
    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.

    P15107-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKAVCVLAG SGDVKGVVHF EQQDEGAVSV EGKIEGLTDG LHGFHIHVFG    50
    DNTNGCMSAG SHFNPENKNH GAPGDTDRHV GDLGNVTAEG GVAQFKITDS 100
    LISLKGPNSI IGRTAVVHEK ADDLGKGGND ESLKTGNAGG RLACGVIGYS 150
    P 151
    Length:151
    Mass (Da):15,418
    Last modified:January 23, 2007 - v3
    Checksum:i8DA6A8FDA1C7FB36
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611S → P AA sequence (PubMed:2751312)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51518 mRNA. Translation: CAA35890.1.
    BC070696 mRNA. Translation: AAH70696.1.
    PIRiS09568.
    RefSeqiNP_001080933.1. NM_001087464.1.
    UniGeneiXl.42.

    Genome annotation databases

    GeneIDi394274.
    KEGGixla:394274.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51518 mRNA. Translation: CAA35890.1 .
    BC070696 mRNA. Translation: AAH70696.1 .
    PIRi S09568.
    RefSeqi NP_001080933.1. NM_001087464.1.
    UniGenei Xl.42.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XSO X-ray 1.49 A/B 2-151 [» ]
    ProteinModelPortali P15107.
    SMRi P15107. Positions 2-151.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P15107.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 394274.
    KEGGi xla:394274.

    Organism-specific databases

    CTDi 394274.
    Xenbasei XB-GENE-6254670. sod1.

    Phylogenomic databases

    HOVERGENi HBG000062.
    KOi K04565.

    Miscellaneous databases

    EvolutionaryTracei P15107.

    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. "Xenopus laevis Cu,Zn superoxide dismutase B cDNA sequence."
      Carri M.T., Battistoni A., Mariottini P., Rotilio G.
      Nucleic Acids Res. 18:1641-1641(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Tadpole.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Gastrula.
    3. "Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis."
      Schinina M.E., Barra D., Bossa F., Calabrese L., Montesano L., Carri M.T., Mariottini P., Amaldi F., Rotilio G.
      Arch. Biochem. Biophys. 272:507-515(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-151.
    4. "The Cu,Zn superoxide dismutase isoenzymes of Xenopus laevis: purification, identification of a heterodimer and differential heat sensitivity."
      Capo C.R., Polticelli F., Calabrese L., Schinina M.E., Carri M.T., Rotilio G.
      Biochem. Biophys. Res. Commun. 173:1186-1193(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31, SUBUNIT.
    5. "Modelling the three-dimensional structure and electrostatic potential field of the two Cu,Zn superoxide dismutase variants from Xenopus laevis."
      Falconi M., Rotilio G., Desideri A.
      Proteins 10:149-155(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    6. "Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5-A resolution."
      Djinovic Carugo K., Battistoni A., Carri M.T., Polticelli F., Desideri A., Rotilio G., Coda A., Wilson K.S., Bolognesi M.
      Acta Crystallogr. D 52:176-188(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS).

    Entry informationi

    Entry nameiSOD1B_XENLA
    AccessioniPrimary (citable) accession number: P15107
    Secondary accession number(s): Q5D025
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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