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Protein

Superoxide dismutase [Cu-Zn]

Gene

ECSOD

Organism
Bos taurus (Bovine)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.UniRule annotation

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Cu cationUniRule annotationNote: Binds 1 copper ion per subunit.UniRule annotation
  • Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

GO - Molecular functioni

  1. copper ion binding Source: GO_Central
  2. superoxide dismutase activity Source: GO_Central
  3. zinc ion binding Source: GO_Central

GO - Biological processi

  1. removal of superoxide radicals Source: GO_Central
  2. response to hypoxia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

CopperUniRule annotation, Metal-bindingUniRule annotation, ZincUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_204534. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn]UniRule annotation (EC:1.15.1.1UniRule annotation)
Gene namesi
Name:ECSODImported
Synonyms:SOD3Imported
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 6

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. extracellular matrix Source: Ensembl
  3. extracellular space Source: GO_Central
  4. extracellular vesicular exosome Source: Ensembl
  5. trans-Golgi network Source: Ensembl
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018580.

Structurei

3D structure databases

ProteinModelPortaliA3KLR9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2032.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
TreeFamiTF105133.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003:SF36. PTHR10003:SF36. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3KLR9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLALLCASVV LVAYASADQI QQQMGSNTEE QIRDMHAKVT EIWQEMMQRQ
60 70 80 90 100
AAAIDPDAAL HAVCRVLPSA TLEAEQPRVS GLVLFRQLRP GALLEAFFHL
110 120 130 140 150
EGFPNEPNGT NRAIHVHQFG DLSQGCDSTG PHYNPMSVPH PQHPGDFGNF
160 170 180 190 200
AVRDGQVWKY RSGLAASLTG PHSIAGRAVV VHAGEDDMGR GGNQASLENG
210 220 230 240
NAGRRLACCV VGLCGPGPWA RQTQEHAERK KRRRESECKA V
Length:241
Mass (Da):26,177
Last modified:April 3, 2007 - v1
Checksum:iE5FA9F77770A4D49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02017144 Genomic DNA. No translation available.
AY957404 mRNA. Translation: AAY28415.1.
RefSeqiNP_001076079.1. NM_001082610.1.
XP_005207845.1. XM_005207788.1.
XP_005207846.1. XM_005207789.1.
UniGeneiBt.1616.

Genome annotation databases

EnsembliENSBTAT00000018580; ENSBTAP00000018580; ENSBTAG00000013980.
GeneIDi532481.
KEGGibta:532481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02017144 Genomic DNA. No translation available.
AY957404 mRNA. Translation: AAY28415.1.
RefSeqiNP_001076079.1. NM_001082610.1.
XP_005207845.1. XM_005207788.1.
XP_005207846.1. XM_005207789.1.
UniGeneiBt.1616.

3D structure databases

ProteinModelPortaliA3KLR9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018580; ENSBTAP00000018580; ENSBTAG00000013980.
GeneIDi532481.
KEGGibta:532481.

Organism-specific databases

CTDi6649.

Phylogenomic databases

eggNOGiCOG2032.
GeneTreeiENSGT00530000063226.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
TreeFamiTF105133.

Enzyme and pathway databases

ReactomeiREACT_204534. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi20875707.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003:SF36. PTHR10003:SF36. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural studies of bovine extracellular superoxide dismutase."
    Kristensen T., Enghild J.J.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LiverImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HerefordImported.
  3. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: HerefordImported.

Entry informationi

Entry nameiA3KLR9_BOVIN
AccessioniPrimary (citable) accession number: A3KLR9
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: February 4, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.