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Q4AEI2 (GPX1_HYLLA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismHylobates lar (Common gibbon)
Taxonomic identifier9580 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeHylobates

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Protects the hemoglobin in erythrocytes from oxidative breakdown By similarity.

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homotetramer. Interacts with MIEN1 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glutathione peroxidase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   Molecular functionOxidoreductase
Peroxidase
   PTMAcetylation
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Glutathione peroxidase 1
PRO_0000066611

Sites

Active site471 By similarity

Amino acid modifications

Non-standard residue471Selenocysteine
Modified residue1461N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4AEI2 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 2ACA430A3E45AEBF

FASTA20121,990
        10         20         30         40         50         60 
MCAARLAAAA AQSVYAFSAR PLTGGEPVSL GSLRGKILLI ENVASLUGTT VRDYTQMNEL 

        70         80         90        100        110        120 
QRRLGPRGLV VLGFPCNQFG HQENAKNEEI LNSLKYVRPG GGFEPNFMLF EKCEVNGAGA 

       130        140        150        160        170        180 
HPLFAFLREA LPAPSDDATA LMTDPKLITW SPVCRNDVAW NFEKFLVGPD GVPLRRYSRR 

       190        200 
FQTIDIEPDI EALLSQGPSC A 

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References

[1]"Structure, gene expression, and evolution of primate glutathione peroxidases."
Fukuhara R., Kageyama T.
Comp. Biochem. Physiol. 141B:428-436(2005) [PubMed: 15967696] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB120998 mRNA. Translation: BAE17008.1.

3D structure databases

ProteinModelPortalQ4AEI2.
ModBaseSearch...

Protein family/group databases

PeroxiBase3696. HlGPx01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004333.

Family and domain databases

InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_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.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPX1_HYLLA
AccessionPrimary (citable) accession number: Q4AEI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: February 26, 2008
Last modified: December 14, 2011
This is version 39 of the entry and version 2 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