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E2RSF2 (E2RSF2_CANFA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family. RuleBase RU004477

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSCAFP00000000951

Ontologies

Keywords
   Molecular functionOxidoreductase RuleBase RU000414
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processage-dependent response to reactive oxygen species

Inferred from electronic annotation. Source: Ensembl

detection of oxygen

Inferred from electronic annotation. Source: Ensembl

erythrophore differentiation

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from electronic annotation. Source: Ensembl

oxygen homeostasis

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

respiratory electron transport chain

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

superoxide dismutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
E2RSF2 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: F57E4BD7B8365999

FASTA22224,845
        10         20         30         40         50         60 
MLSRAALSTS RTLVPALGCL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN 

        70         80         90        100        110        120 
NLNTIEEKYL EALEKGDITA QIALQPGLKF NGGGHINHSI FWTNLSPKGG GEPKGELLEA 

       130        140        150        160        170        180 
IKRDFGSFDK FKEKLTTVSV GVQGSGWGWL GFNKEQGRLQ IAACFNQDPL QGTTGLIPLL 

       190        200        210        220 
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence, comparative analysis and haplotype structure of the domestic dog."
Broad Sequencing Platform
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R. expand/collapse author list , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Boxer Ensembl ENSCAFP00000000951.
[2]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Boxer Ensembl ENSCAFP00000000951.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEX03000317 Genomic DNA. No translation available.
RefSeqXP_533463.3. XM_533463.4.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000001037; ENSCAFP00000000951; ENSCAFG00000000671.
GeneID476258.
KEGGcfa:476258.

Organism-specific databases

CTD6648.

Phylogenomic databases

GeneTreeENSGT00390000011877.
KOK04564.
OMAVENLINW.
OrthoDBEOG7FV3R5.
TreeFamTF105132.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20851956.

Entry information

Entry nameE2RSF2_CANFA
AccessionPrimary (citable) accession number: E2RSF2
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)