E2RSF2 (E2RSF2_CANFA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Superoxide dismutase RuleBase RU000414
EC=1.15.1.1 RuleBase RU000414

Gene names

Name:

SOD2 Ensembl ENSCAFP00000000951

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome] Ensembl ENSCAFP00000000951

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. RuleBase RU000414
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000414
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 function	Oxidoreductase RuleBase RU000414
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	age-dependent response to reactive oxygen species Inferred from electronic annotation. Source: Compara detection of oxygen Inferred from electronic annotation. Source: Compara erythrophore differentiation Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara hemopoiesis Inferred from electronic annotation. Source: Compara iron ion homeostasis Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara locomotory behavior Inferred from electronic annotation. Source: Compara negative regulation of fat cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara neuron development Inferred from electronic annotation. Source: Compara oxygen homeostasis Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara regulation of catalytic activity Inferred from electronic annotation. Source: Compara regulation of mitochondrial membrane potential Inferred from electronic annotation. Source: Compara release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara removal of superoxide radicals Inferred from electronic annotation. Source: Compara respiratory electron transport chain Inferred from electronic annotation. Source: Compara response to activity Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to hyperoxia Inferred from electronic annotation. Source: Compara superoxide anion generation Inferred from electronic annotation. Source: Compara vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: InterPro superoxide dismutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	E2RSF2 [UniParc]. Last modified November 30, 2010. Version 1. Checksum: F57E4BD7B8365999	FASTA	222	24,845
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_533463.3. XM_533463.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000001037; ENSCAFP00000000951; ENSCAFG00000000671.
GeneID	476258.
KEGG	cfa:476258.
Organism-specific databases
CTD	6648.
Phylogenomic databases
GeneTree	ENSGT00390000011877.
KO	K04564.
OMA	MAPPGKG.
Family and domain databases
InterPro	IPR001189. Mn/Fe_SOD. IPR019833. Mn/Fe_SOD_BS. IPR019832. Mn/Fe_SOD_C. IPR019831. Mn/Fe_SOD_N. [Graphical view]
PANTHER	PTHR11404. PTHR11404. 1 hit.
Pfam	PF02777. Sod_Fe_C. 1 hit. PF00081. Sod_Fe_N. 1 hit. [Graphical view]
PIRSF	PIRSF000349. SODismutase. 1 hit.
PRINTS	PR01703. MNSODISMTASE.
SUPFAM	SSF46609. SODismutase. 1 hit. SSF54719. SODismutase. 1 hit.
PROSITE	PS00088. SOD_MN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20851956.

Entry information

Entry name

E2RSF2_CANFA

Accession

Primary (citable) accession number: E2RSF2

Entry history

Integrated into UniProtKB/TrEMBL:	November 30, 2010
Last sequence update:	November 30, 2010
Last modified:	April 3, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)