[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Pituitary; DOI=10.1093/protein/2.3.239; PubMed=2976939 [NCBI, ExPASy, EBI, Israel, Japan] Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Tainer J.A., Hallewell R.A.; "Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases."; Protein Eng. 2:239-246(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 8-205. TISSUE=Erythrocyte; PubMed=6714945 [NCBI, ExPASy, EBI, Israel, Japan] Gunzler W.A., Steffens G.J., Grossmann A., Kim S.-M.A., Otting F., Wendel A., Flohe L.; "The amino-acid sequence of bovine glutathione peroxidase."; Hoppe-Seyler's Z. Physiol. Chem. 365:195-212(1984).
[4]	GLYCATION AT LYS-117, AND ABSENCE OF GLYCATION AT LYS-41; LYS-91; LYS-100; LYS-124; LYS-151; LYS-169. DOI=10.1016/0167-4838(94)00202-R; PubMed=7873592 [NCBI, ExPASy, EBI, Israel, Japan] Baldwin J.S., Lee L., Leung T.K., Muruganandam A., Mutus B.; "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."; Biochim. Biophys. Acta 1247:60-64(1995).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=6852035 [NCBI, ExPASy, EBI, Israel, Japan] Epp O., Ladenstein R., Wendel A.; "The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution."; Eur. J. Biochem. 133:51-69(1983).

Comments

FUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown.
CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the glutathione peroxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13684; CAB40806.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC149308; AAI49309.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S04872; OPBOE.

NP_776501.1; -.

3D structure databases

PDB

1GP1; X-ray; 2.00 A; A/B=8-205.

[ExPASy / RCSB / EBI]

PDBsum

1GP1; -.

ModBase

P00435.

Protein family/group databases

PeroxiBase

3635; BtGPx01.

Family and domain databases

InterPro

IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR11592; Glut_peroxidase; 1.

Pfam

PF00255; GSHPx; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000303; Glutathion_perox; 1.

PRINTS

PR01011; GLUTPROXDASE.

PROSITE

PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P00435.

Genome annotation databases

Ensembl

ENSBTAG00000004274; Bos taurus. [Contig view]

GeneID

281209; -.

KEGG

bta:281209; -.

Phylogenomic databases

HOVERGEN

P00435; -.

Other

P00435; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Glycation; Glycoprotein; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 205`	`205`	`Glutathione peroxidase 1.`	`PRO_0000066608`
`ACT_SITE`	`52 52`
`SITE`	`41 41`	`1`	`Not glycated.`
`SITE`	`91 91`	`1`	`Not glycated.`
`SITE`	`100 100`	`1`	`Not glycated.`
`SITE`	`124 124`	`1`	`Not glycated.`
`SITE`	`151 151`	`1`	`Not glycated.`
`SITE`	`169 169`	`1`	`Not glycated.`
`NON_STD`	`52 52`		`Selenocysteine.`
`MOD_RES`	`151 151`		`N6-acetyllysine (By similarity).`
`CARBOHYD`	`117 117`		`N-linked (Glc) (glycation); in vitro.`
`CONFLICT`	`96 96`		`L -> P (in Ref. 2; AAI49309).`
`HELIX`	`19 21`	`3`
`HELIX`	`35 38`	`4`
`STRAND`	`41 48`	`8`
`STRAND`	`50 52`	`3`
`HELIX`	`55 69`	`15`
`HELIX`	`70 72`	`3`
`STRAND`	`74 80`	`7`
`TURN`	`83 86`	`4`
`HELIX`	`92 94`	`3`
`HELIX`	`95 101`	`7`
`STRAND`	`111 115`	`5`
`STRAND`	`119 122`	`4`
`HELIX`	`127 135`	`9`
`HELIX`	`150 152`	`3`
`STRAND`	`155 157`	`3`
`STRAND`	`169 172`	`4`
`STRAND`	`178 182`	`5`
`HELIX`	`188 191`	`4`
`HELIX`	`192 199`	`8`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 22659 Da [This is the MW of the unprocessed precursor]

CRC64: 7CBDF736CAAA92F6 [This is a checksum on the sequence]

        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

P00435 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools