Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00435 (GPX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione peroxidase 1

Short name=GPx-1
Short name=GSHPx-1
EC=1.11.1.9
Alternative name(s):
Cellular glutathione peroxidase
Gene names
Name:GPX1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homotetramer. Interacts with MIEN1.

Subcellular location

Cytoplasm.

Post-translational modification

During periods of oxidative stress, Sec-52 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine By similarity.

Sequence similarities

Belongs to the glutathione peroxidase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   Molecular functionOxidoreductase
Peroxidase
   PTMAcetylation
Glycation
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Glutathione peroxidase 1
PRO_0000066608

Sites

Active site521
Site411Not glycated
Site521Subject to oxidation and hydroselenide loss to dehydroalanine By similarity
Site911Not glycated
Site1001Not glycated
Site1241Not glycated
Site1511Not glycated
Site1691Not glycated

Amino acid modifications

Non-standard residue521Selenocysteine
Modified residue911N6-acetyllysine By similarity
Modified residue1171N6-acetyllysine; alternate By similarity
Modified residue1171N6-succinyllysine; alternate By similarity
Modified residue1241N6-acetyllysine By similarity
Modified residue1511N6-acetyllysine By similarity
Glycosylation1171N-linked (Glc) (glycation); in vitro Ref.4

Experimental info

Sequence conflict961L → P in AAI49309. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00435 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13684 mRNA. Translation: CAB40806.1.
BC149308 mRNA. Translation: AAI49309.1.
PIROPBOE. S04872.
RefSeqNP_776501.1. NM_174076.3.
UniGeneBt.4317.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GP1X-ray2.00A/B8-205[»]
ProteinModelPortalP00435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000005597.

Protein family/group databases

PeroxiBase3635. BtGPx01.

Proteomic databases

PaxDbP00435.
PRIDEP00435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281209.
KEGGbta:281209.

Organism-specific databases

CTD2876.

Phylogenomic databases

eggNOGCOG0386.
HOVERGENHBG004333.
InParanoidP00435.
KOK00432.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11592. PTHR11592. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00435.
NextBio20805264.

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: March 19, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references