P00435 (GPX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Selenocysteine
Molecular function	Oxidoreductase Peroxidase
PTM	Acetylation Glycation Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

Glutathione peroxidase 1

PRO_0000066608

Sites

Active site

52

1

Site

41

1

Not glycated

Site

52

1

Subject to oxidation and hydroselenide loss to dehydroalanine By similarity

Site

91

1

Not glycated

Site

100

1

Not glycated

Site

124

1

Not glycated

Site

151

1

Not glycated

Site

169

1

Not glycated

Amino acid modifications

Non-standard residue

52

1

Selenocysteine

Modified residue

151

1

N6-acetyllysine By similarity

Glycosylation

117

1

N-linked (Glc) (glycation); in vitro Ref.4

Experimental info

Sequence conflict

96

1

L → P in AAI49309. Ref.2

Secondary structure

1

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205

Helix Strand Turn

Details...

Helix

19 – 21

3

Helix

35 – 38

4

Beta strand

41 – 48

8

Beta strand

50 – 52

3

Helix

55 – 69

15

Helix

70 – 72

3

Beta strand

74 – 80

7

Turn

83 – 86

4

Helix

92 – 94

3

Helix

95 – 101

7

Beta strand

111 – 115

5

Beta strand

119 – 122

4

Helix

127 – 135

9

Helix

150 – 152

3

Beta strand

155 – 157

3

Beta strand

169 – 172

4

Beta strand

178 – 182

5

Helix

188 – 191

4

Helix

192 – 199

8

Sequences

	Sequence		Length	Mass (Da)
	P00435 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: 7CBDF736CAAA92F6	FASTA	205	22,659
	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

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00686183.

PIR

OPBOE. S04872.

RefSeq

NP_776501.1. NM_174076.3.

UniGene

Bt.4317.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GP1	X-ray	2.00	A/B	8-205	[»]

ProteinModelPortal

P00435.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000005597.

Protein family/group databases

PeroxiBase

3635. BtGPx01.

Proteomic databases

PaxDb

P00435.

PRIDE

P00435.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

281209.

KEGG

bta:281209.

Organism-specific databases

CTD

2876.

Phylogenomic databases

eggNOG

COG0386.

HOVERGEN

HBG004333.

InParanoid

P00435.

KO

K00432.

OrthoDB

EOG4SBF08.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR11592. PTHR11592. 1 hit.

Pfam

PF00255. GSHPx. 1 hit.
[Graphical view]

PIRSF

PIRSF000303. Glutathion_perox. 1 hit.

PRINTS

PR01011. GLUTPROXDASE.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00435.

NextBio

20805264.

Entry information

Entry name

GPX1_BOVIN

Accession

Primary (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:	April 3, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program