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Q5FB29 (SODC_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1
Gene names
Name:SOD1
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Capra

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
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 By similarity
Chain2 – 152151Superoxide dismutase [Cu-Zn]
PRO_0000164052

Sites

Metal binding451Copper; catalytic By similarity
Metal binding471Copper; catalytic By similarity
Metal binding621Copper; catalytic By similarity
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity
Metal binding791Zinc; structural By similarity
Metal binding821Zinc; structural By similarity
Metal binding1191Copper; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue1211N6-acetyllysine By similarity
Disulfide bond56 ↔ 145 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FB29 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B0257980664C1CD2

FASTA15215,653
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGTIH FEAKGDKVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG 

        70         80         90        100        110        120 
PHFNPLSKKH GGPKDEERHV GDLGNVKADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE 

       130        140        150 
KPDDLGRGGN EESTKTGNAG SCLACGVIGI AP

« Hide

References

[1]"Mammalian superoxide dismutase."
Fukuhara R., Kageyama T.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB201469 mRNA. Translation: BAD89543.1.

3D structure databases

ProteinModelPortalQ5FB29.
SMRQ5FB29. Positions 2-151.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000062.

Family and domain databases

InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_CAPHI
AccessionPrimary (citable) accession number: Q5FB29
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 23, 2007
Last modified: July 27, 2011
This is version 42 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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