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P33431 (SODC_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. 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
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length153 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 By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

anterograde axon cargo transport

Inferred from electronic annotation. Source: Compara

apoptotic DNA fragmentation

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell stereocilium organization

Inferred from sequence or structural similarity. Source: UniProtKB

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

embryo implantation

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

heart contraction

Inferred from sequence or structural similarity. Source: UniProtKB

hydrogen peroxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid cell homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neurofilament cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

ovarian follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

peripheral nervous system myelin maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: UniProtKB

relaxation of vascular smooth muscle

Inferred from sequence or structural similarity. Source: UniProtKB

removal of superoxide radicals

Inferred from sequence or structural similarity. Source: UniProtKB

response to axon injury

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

response to ethanol

Inferred from sequence or structural similarity. Source: UniProtKB

response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

retina homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde axon cargo transport

Inferred from electronic annotation. Source: Compara

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide anion generation

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Compara

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide dismutase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 153152Superoxide dismutase [Cu-Zn]
PRO_0000164053

Sites

Metal binding461Copper; catalytic By similarity
Metal binding481Copper; catalytic By similarity
Metal binding631Copper; catalytic By similarity
Metal binding631Zinc; structural By similarity
Metal binding711Zinc; structural By similarity
Metal binding801Zinc; structural By similarity
Metal binding831Zinc; structural By similarity
Metal binding1201Copper; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue701N6-acetyllysine By similarity
Modified residue981Phosphoserine By similarity
Modified residue1221N6-acetyllysine By similarity
Disulfide bond57 ↔ 146 By similarity

Experimental info

Sequence conflict103 – 1042LI → IL AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P33431 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B82C13327FACF227

FASTA15315,670
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGIIH FEQKANGPVV VKGRITGLVE GKHGFHVHEF GDNTQGCTSA 

        70         80         90        100        110        120 
GPHFNPLSKK HGGPQDEERH VGDLGNVTAG ADGVANVSIE DSLISLSGAN SIIGRTMVVH 

       130        140        150 
EKPDDLGKGG NEESTKTGNA GSRLACGVIG IAQ 

« Hide

References

[1]"Differential patterns of antioxidant enzyme mRNA expression in guinea pig lung and liver during development."
Yuan H.T., Bingle C.D., Kelly F.J.
Biochim. Biophys. Acta 1305:163-171(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Hartley.
Tissue: Lung.
[2]"Taxonomical classification of the guinea pig based on its Cu/Zn superoxide dismutase sequence."
Wolf B., Reinecke K., Aumann K.-D., Brigelius-Flohe R., Flohe L.
Biol. Chem. Hoppe-Seyler 374:641-649(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-153.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39844 mRNA. Translation: AAC52720.1.
PIRS36108.
RefSeqXP_003467296.1. XM_003467248.1.

3D structure databases

ProteinModelPortalP33431.
SMRP33431. Positions 4-153.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000012815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135622.

Organism-specific databases

CTD6647.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
HOVERGENHBG000062.
InParanoidP33431.
OrthoDBEOG45HRZM.

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...

Entry information

Entry nameSODC_CAVPO
AccessionPrimary (citable) accession number: P33431
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 100 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