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P15107 (SOD1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn] B
Short name=XSODB
EC=1.15.1.1
Gene names
Name:sod1-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer, and heterodimer of Superoxide dismutase [Cu-Zn] A and B. Ref.4

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 151150Superoxide dismutase [Cu-Zn] B
PRO_0000164077

Sites

Metal binding451Copper; catalytic
Metal binding471Copper; catalytic
Metal binding621Copper; catalytic
Metal binding621Zinc; structural
Metal binding701Zinc; structural
Metal binding791Zinc; structural
Metal binding821Zinc; structural
Metal binding1181Copper; catalytic

Amino acid modifications

Disulfide bond56 ↔ 144

Experimental info

Sequence conflict611S → P AA sequence Ref.3

Secondary structure

1 ............................. 151
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15107 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8DA6A8FDA1C7FB36

FASTA15115,418
        10         20         30         40         50         60 
MVKAVCVLAG SGDVKGVVHF EQQDEGAVSV EGKIEGLTDG LHGFHIHVFG DNTNGCMSAG 

        70         80         90        100        110        120 
SHFNPENKNH GAPGDTDRHV GDLGNVTAEG GVAQFKITDS LISLKGPNSI IGRTAVVHEK 

       130        140        150 
ADDLGKGGND ESLKTGNAGG RLACGVIGYS P

« Hide

References

« Hide 'large scale' references
[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51518 mRNA. Translation: CAA35890.1.
BC070696 mRNA. Translation: AAH70696.1.
PIRS09568.
RefSeqNP_001080933.1. NM_001087464.1.
UniGeneXl.42.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSOX-ray1.49A/B2-151[»]
ProteinModelPortalP15107.
SMRP15107. Positions 2-151.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID394274.
KEGGxla:394274.

Organism-specific databases

CTD394274.
XenbaseXB-GENE-6254670. sod1.

Phylogenomic databases

HOVERGENHBG000062.
KOK04565.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15107.

Entry information

Entry nameSOD1B_XENLA
AccessionPrimary (citable) accession number: P15107
Secondary accession number(s): Q5D025
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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