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Reviewed, UniProtKB/Swiss-Prot P00435 (GPX1_BOVIN)

Last modified September 1, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutathione peroxidase 1
    EC=1.11.1.9
Alternative name(s):
    GSHPx-1
      Short name=GPx-1
    Cellular glutathione peroxidase
Gene names
Name: GPX1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutathione peroxidase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   LigandSelenium
   Molecular functionOxidoreductase
Peroxidase
   PTMAcetylation
Glycation
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglutathione peroxidase activity

Inferred from electronic annotation. Source: EC

selenium binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Glutathione peroxidase 1
PRO_0000066608

Sites

Active site521
Site411Not glycated
Site911Not glycated
Site1001Not glycated
Site1241Not glycated
Site1511Not glycated
Site1691Not glycated

Amino acid modifications

Non-standard residue521Selenocysteine
Modified residue1511N6-acetyllysine By similarity
Glycosylation1171N-linked (Glc) (glycation); in vitro

Experimental info

Sequence conflict961L → P in AAI49309. Ref.2

Secondary structure

1 .................................... 205
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00435-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: 7CBDF736CAAA92F6

FASTA20522,659
        10         20         30         40         50         60 
MCAAQRSAAA LAAAAPRTVY AFSARPLAGG EPFNLSSLRG KVLLIENVAS LUGTTVRDYT 

        70         80         90        100        110        120 
QMNDLQRRLG PRGLVVLGFP CNQFGHQENA KNEEILNCLK YVRPGGGFEP NFMLFEKCEV 

       130        140        150        160        170        180 
NGEKAHPLFA FLREVLPTPS DDATALMTDP KFITWSPVCR NDVSWNFEKF LVGPDGVPVR 

       190        200 
RYSRRFLTID IEPDIETLLS QGASA

« Hide

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References

« Hide 'large scale' references
[1]"Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases."
Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Tainer J.A., Hallewell R.A.
Protein Eng. 2:239-246(1988) [PubMed: 2976939] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.
[3]"The amino-acid sequence of bovine glutathione peroxidase."
Gunzler W.A., Steffens G.J., Grossmann A., Kim S.-M.A., Otting F., Wendel A., Flohe L.
Hoppe-Seyler's Z. Physiol. Chem. 365:195-212(1984) [PubMed: 6714945] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-205.
Tissue: Erythrocyte.
[4]"Identification of the site of non-enzymatic glycation of glutathione peroxidase: rationalization of the glycation-related catalytic alterations on the basis of three-dimensional protein structure."
Baldwin J.S., Lee L., Leung T.K., Muruganandam A., Mutus B.
Biochim. Biophys. Acta 1247:60-64(1995) [PubMed: 7873592] [Abstract]
Cited for: GLYCATION AT LYS-117, ABSENCE OF GLYCATION AT LYS-41; LYS-91; LYS-100; LYS-124; LYS-151; LYS-169.
[5]"The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution."
Epp O., Ladenstein R., Wendel A.
Eur. J. Biochem. 133:51-69(1983) [PubMed: 6852035] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

X13684 mRNA. Translation: CAB40806.1.
BC149308 mRNA. Translation: AAI49309.1.
IPIIPI00686183.
PIROPBOE. S04872.
RefSeqNP_776501.1.
UniGeneBt.102106
Bt.4317

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GP1X-ray2.00A/B8-205[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP00435.

Protein family/group databases

PeroxiBase3635. BtGPx01.

Genome annotation databases

EnsemblENSBTAT00000005597; ENSBTAP00000005597; ENSBTAG00000004274; Bos taurus. [Genome view]
GeneID281209.
KEGGbta:281209.

Organism-specific databases

CTD281209.

Phylogenomic databases

HOVERGENP00435.

Enzyme and pathway databases

BRENDA1.11.1.9. 251.

Family and domain databases

InterProIPR000889. Glutathione_peroxidase.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR11592. Glut_peroxidase. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGPX1_BOVIN
AccessionPrimary (citable) accession number: P00435
Secondary accession number(s): A6QPG3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 26, 2008
Last modified: September 1, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents