Reviewed, UniProtKB/Swiss-Prot Q4AEI2 (GPX1_HYLLA)

Names and origin

Protein names

Recommended name:
    Glutathione peroxidase 1
      Short name=GSHPx-1
      Short name=GPx-1
    EC=1.11.1.9
Alternative name(s):
    Cellular glutathione peroxidase

Gene names

Name:

GPX1

Organism

Hylobates lar (Common gibbon)

Taxonomic identifier

9580 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hylobatidae › Hylobates

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glutathione peroxidase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Selenocysteine
Ligand	Selenium
Molecular function	Oxidoreductase Peroxidase
PTM	Acetylation
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC selenium binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 201	201	Glutathione peroxidase 1		PRO_0000066611
Sites
	Active site	47	1	By similarity
Amino acid modifications
	Non-standard residue	47	1	Selenocysteine
	Modified residue	146	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4AEI2-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: 2ACA430A3E45AEBF	FASTA	201	21,990
	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

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
ModBase	Search...
Protein family/group databases
PeroxiBase	3696. HlGPx01.
Phylogenomic databases
HOVERGEN	Q4AEI2.
Enzyme and pathway databases
BRENDA	1.11.1.9. 285274.
Family and domain databases
InterPro	IPR000889. Glutathione_peroxidase. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR11592. Glut_peroxidase. 1 hit.
Pfam	PF00255. GSHPx. 1 hit. [Graphical view]
PIRSF	PIRSF000303. Glutathion_perox. 1 hit.
PRINTS	PR01011. GLUTPROXDASE.
PROSITE	PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPX1_HYLLA

Accession

Primary (citable) accession number: Q4AEI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	February 26, 2008
Last modified:	February 9, 2010
This is version 29 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)