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P00435

- GPX1_BOVIN

UniProt

P00435 - GPX1_BOVIN

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Protein

Glutathione peroxidase 1

Gene

GPX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 411Not glycated
Active sitei52 – 521
Sitei52 – 521Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity
Sitei91 – 911Not glycated
Sitei100 – 1001Not glycated
Sitei124 – 1241Not glycated
Sitei151 – 1511Not glycated
Sitei169 – 1691Not glycated

GO - Molecular functioni

  1. glutathione peroxidase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  1. glutathione metabolic process Source: ParkinsonsUK-UCL
  2. hydrogen peroxide catabolic process Source: ParkinsonsUK-UCL
  3. positive regulation of fibril organization Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Protein family/group databases

PeroxiBasei3635. BtGPx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1 (EC:1.11.1.9)
Short name:
GPx-1
Short name:
GSHPx-1
Alternative name(s):
Cellular glutathione peroxidase
Gene namesi
Name:GPX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Glutathione peroxidase 1PRO_0000066608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
Glycosylationi117 – 1171N-linked (Glc) (glycation); in vitro
Modified residuei124 – 1241N6-acetyllysineBy similarity
Modified residuei151 – 1511N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycation, Glycoprotein

Proteomic databases

PaxDbiP00435.
PRIDEiP00435.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005597.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 213
Helixi35 – 384
Beta strandi41 – 488
Helixi55 – 6915
Helixi70 – 723
Beta strandi74 – 807
Turni83 – 864
Helixi92 – 943
Helixi95 – 1017
Beta strandi111 – 1155
Beta strandi119 – 1224
Helixi127 – 1359
Helixi150 – 1523
Beta strandi155 – 1573
Beta strandi169 – 1724
Beta strandi178 – 1825
Helixi188 – 1914
Helixi192 – 1998

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GP1X-ray2.00A/B8-205[»]
ProteinModelPortaliP00435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00435.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiCOG0386.
HOVERGENiHBG004333.
InParanoidiP00435.
KOiK00432.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00435-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCAAQRSAAA LAAAAPRTVY AFSARPLAGG EPFNLSSLRG KVLLIENVAS
60 70 80 90 100
LUGTTVRDYT QMNDLQRRLG PRGLVVLGFP CNQFGHQENA KNEEILNCLK
110 120 130 140 150
YVRPGGGFEP NFMLFEKCEV NGEKAHPLFA FLREVLPTPS DDATALMTDP
160 170 180 190 200
KFITWSPVCR NDVSWNFEKF LVGPDGVPVR RYSRRFLTID IEPDIETLLS

QGASA
Length:205
Mass (Da):22,659
Last modified:February 26, 2008 - v3
Checksum:i7CBDF736CAAA92F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961L → P in AAI49309. 1 PublicationCurated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei52 – 521Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13684 mRNA. Translation: CAB40806.1.
BC149308 mRNA. Translation: AAI49309.1.
PIRiS04872. OPBOE.
RefSeqiNP_776501.1. NM_174076.3.
UniGeneiBt.4317.

Genome annotation databases

GeneIDi281209.
KEGGibta:281209.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13684 mRNA. Translation: CAB40806.1 .
BC149308 mRNA. Translation: AAI49309.1 .
PIRi S04872. OPBOE.
RefSeqi NP_776501.1. NM_174076.3.
UniGenei Bt.4317.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GP1 X-ray 2.00 A/B 8-205 [» ]
ProteinModelPortali P00435.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000005597.

Protein family/group databases

PeroxiBasei 3635. BtGPx01.

Proteomic databases

PaxDbi P00435.
PRIDEi P00435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281209.
KEGGi bta:281209.

Organism-specific databases

CTDi 2876.

Phylogenomic databases

eggNOGi COG0386.
HOVERGENi HBG004333.
InParanoidi P00435.
KOi K00432.

Miscellaneous databases

EvolutionaryTracei P00435.
NextBioi 20805264.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
PANTHERi PTHR11592. PTHR11592. 1 hit.
Pfami PF00255. GSHPx. 1 hit.
[Graphical view ]
PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
PRINTSi PR01011. GLUTPROXDASE.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiGPX1_BOVIN
AccessioniPrimary (citable) accession number: P00435
Secondary accession number(s): A6QPG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 26, 2008
Last modified: October 29, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3