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Q6LDS4 (Q6LDS4_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 62. Feed History...

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

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn] RuleBase RU000393

EC=1.15.1.1 RuleBase RU000393
Gene names
Name:Sod1 RGD 3731
OrganismRattus norvegicus (Rat) EMBL AAA40996.1
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
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 By similarity. RuleBase RU000393

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000393

Cofactor

Binds 1 copper ion per subunit By similarity. RuleBase RU000393

Binds 1 zinc ion per subunit By similarity. RuleBase RU000393

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family. RuleBase RU000393

Ontologies

Keywords
   LigandCopper RuleBase RU000393
Metal-binding RuleBase RU000393
Zinc RuleBase RU000393
   Molecular functionOxidoreductase RuleBase RU000393
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Compara

anterograde axon cargo transport

Inferred from electronic annotation. Source: Compara

apoptotic DNA fragmentation

Inferred from electronic annotation. Source: Compara

auditory receptor cell stereocilium organization

Inferred from electronic annotation. Source: Compara

cell aging

Inferred from electronic annotation. Source: Compara

cellular iron ion homeostasis

Inferred from electronic annotation. Source: Compara

double-strand break repair

Inferred from electronic annotation. Source: Compara

embryo implantation

Inferred from electronic annotation. Source: Compara

glutathione metabolic process

Inferred from electronic annotation. Source: Compara

heart contraction

Inferred from electronic annotation. Source: Compara

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Compara

locomotory behavior

Inferred from electronic annotation. Source: Compara

muscle cell homeostasis

Inferred from electronic annotation. Source: Compara

myeloid cell homeostasis

Inferred from electronic annotation. Source: Compara

negative regulation of cholesterol biosynthetic process

Inferred from electronic annotation. Source: Compara

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Compara

neurofilament cytoskeleton organization

Inferred from electronic annotation. Source: Compara

ovarian follicle development

Inferred from electronic annotation. Source: Compara

peripheral nervous system myelin maintenance

Inferred from electronic annotation. Source: Compara

positive regulation of cytokine production

Inferred from electronic annotation. Source: Compara

regulation of blood pressure

Inferred from electronic annotation. Source: Compara

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Compara

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Compara

relaxation of vascular smooth muscle

Inferred from electronic annotation. Source: Compara

removal of superoxide radicals

Inferred from electronic annotation. Source: Compara

response to axon injury

Inferred from electronic annotation. Source: Compara

response to drug

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to heat

Inferred from electronic annotation. Source: Compara

response to hydrogen peroxide

Inferred from electronic annotation. Source: Compara

retina homeostasis

Inferred from electronic annotation. Source: Compara

retrograde axon cargo transport

Inferred from electronic annotation. Source: Compara

sensory perception of sound

Inferred from electronic annotation. Source: Compara

spermatogenesis

Inferred from electronic annotation. Source: Compara

superoxide anion generation

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytoplasmic vesicle

Inferred from electronic annotation. Source: Compara

cytosol

Inferred from electronic annotation. Source: Compara

dendrite cytoplasm

Inferred from electronic annotation. Source: Compara

extracellular matrix

Inferred from electronic annotation. Source: Compara

extracellular space

Inferred from electronic annotation. Source: Compara

mitochondrion

Inferred from electronic annotation. Source: Compara

neuronal cell body

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from electronic annotation. Source: Compara

protein complex

Inferred from electronic annotation. Source: Compara

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: Compara

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q6LDS4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4630256A2B0F3CB4

FASTA15215,709
        10         20         30         40         50         60 
MKAVCVLKGD GPVQGVIHFE QKASGEPVVV SGQITGLTEG EHGFHVHQYG DNTQGCTTAG 

        70         80         90        100        110        120 
PHFNPHSKKH GGPADEERHV GDLGNVAAGK DGVANVSIED RVISLSGEHS IIGRTMVVHE 

       130        140        150 
KQDDLGKGGN EESTKTGNAG SRLACGVIGI AQ 

« Hide

References

[1]"Isolation and nucleotide sequence of rat Cu/Zn superoxide dismutase cDNA clones."
Puga A., Oates E.L.
Free Radic. Res. Commun. 3:337-346(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21060 mRNA. Translation: AAA40996.1.
IPIIPI00231643.
UniGeneRn.6059.

3D structure databases

HSSPHSSP built from PDB template 1AZV based on UniProtKB P00441.
ProteinModelPortalQ6LDS4.
SMRQ6LDS4. Positions 2-152.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6LDS4.

Proteomic databases

PRIDEQ6LDS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD3731. Sod1.

Phylogenomic databases

HOVERGENHBG000062.

Gene expression databases

ArrayExpressQ6LDS4.
GenevestigatorQ6LDS4.

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 nameQ6LDS4_RAT
AccessionPrimary (citable) accession number: Q6LDS4
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)