Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione peroxidase 7

Gene

GPX7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks.1 Publication

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei57By similarity1

GO - Molecular functioni

  • catalase activity Source: CACAO
  • glutathione peroxidase activity Source: UniProtKB-EC
  • peroxidase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciZFISH:HS03989-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3606. HsGPx07.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 7 (EC:1.11.1.9)
Short name:
GPx-7
Short name:
GSHPx-7
Alternative name(s):
CL683
Gene namesi
Name:GPX7
Synonyms:GPX6
ORF Names:UNQ469/PRO828
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4559. GPX7.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Barrett esophagus (BE)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. The pathologic mechanisms leading to Barrett esophagus involve GPX7 dysfunction that results in higher levels of hydrogen peroxide and ROS-induced oxidative stress and DNA damage in esophageal cells.
Disease descriptionA condition characterized by a metaplastic change in which normal esophageal squamous epithelium is replaced by a columnar and intestinal-type epithelium. Patients with Barrett esophagus have an increased risk of esophageal adenocarcinoma. The main cause of Barrett esophagus is gastroesophageal reflux. The retrograde movement of acid and bile salts from the stomach into the esophagus causes prolonged injury to the esophageal epithelium and induces chronic esophagitis, which in turn is believed to trigger the pathologic changes.
See also OMIM:614266

Organism-specific databases

DisGeNETi2882.
MIMi614266. phenotype.
OpenTargetsiENSG00000116157.
PharmGKBiPA28955.

Chemistry databases

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX7.
DMDMi33516901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001308420 – 187Glutathione peroxidase 7Add BLAST168

Proteomic databases

EPDiQ96SL4.
MaxQBiQ96SL4.
PaxDbiQ96SL4.
PeptideAtlasiQ96SL4.
PRIDEiQ96SL4.

PTM databases

iPTMnetiQ96SL4.
PhosphoSitePlusiQ96SL4.

Expressioni

Tissue specificityi

Expressed in esophageal epithelial cells; expression is up-regulated after exposure to acidic bile acids.1 Publication

Gene expression databases

BgeeiENSG00000116157.
CleanExiHS_GPX6.
HS_GPX7.
GenevisibleiQ96SL4. HS.

Organism-specific databases

HPAiHPA025829.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ASNA1O436813EBI-749411,EBI-2515857
CEP70Q8NHQ13EBI-749411,EBI-739624
SGTAO437653EBI-749411,EBI-347996

Protein-protein interaction databases

BioGridi109139. 36 interactors.
IntActiQ96SL4. 6 interactors.
MINTiMINT-1466561.
STRINGi9606.ENSP00000354677.

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 27Combined sources3
Beta strandi29 – 32Combined sources4
Beta strandi37 – 39Combined sources3
Helixi40 – 43Combined sources4
Beta strandi46 – 53Combined sources8
Beta strandi55 – 57Combined sources3
Helixi60 – 74Combined sources15
Helixi75 – 77Combined sources3
Beta strandi79 – 85Combined sources7
Helixi97 – 108Combined sources12
Helixi127 – 136Combined sources10
Beta strandi146 – 149Combined sources4
Beta strandi155 – 159Combined sources5
Helixi165 – 173Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P31X-ray2.00A/B20-177[»]
ProteinModelPortaliQ96SL4.
SMRiQ96SL4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96SL4.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
InParanoidiQ96SL4.
KOiK00432.
OMAiCAQREQD.
OrthoDBiEOG091G0OJG.
PhylomeDBiQ96SL4.
TreeFamiTF331942.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR013376. Glut_perox_Gpx7.
IPR000889. 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.
TIGRFAMsiTIGR02540. gpx7. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96SL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAATVAAAW LLLWAAACAQ QEQDFYDFKA VNIRGKLVSL EKYRGSVSLV
60 70 80 90 100
VNVASECGFT DQHYRALQQL QRDLGPHHFN VLAFPCNQFG QQEPDSNKEI
110 120 130 140 150
ESFARRTYSV SFPMFSKIAV TGTGAHPAFK YLAQTSGKEP TWNFWKYLVA
160 170 180
PDGKVVGAWD PTVSVEEVRP QITALVRKLI LLKREDL
Length:187
Mass (Da):20,996
Last modified:December 1, 2001 - v1
Checksum:i0ACB80AC2522EFCD
GO

Sequence cautioni

The sequence AAC72961 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75 – 77GPH → HED (Ref. 7) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320068 mRNA. Translation: AAN76501.1.
AY358402 mRNA. Translation: AAQ88768.1.
AK027683 mRNA. Translation: BAB55294.1.
DQ096732 Genomic DNA. Translation: AAY88741.1.
AL356976 Genomic DNA. Translation: CAI22476.1.
BC032788 mRNA. Translation: AAH32788.1.
AF091092 mRNA. Translation: AAC72961.1. Sequence problems.
CCDSiCCDS569.1.
RefSeqiNP_056511.2. NM_015696.4.
UniGeneiHs.43728.

Genome annotation databases

EnsembliENST00000361314; ENSP00000354677; ENSG00000116157.
GeneIDi2882.
KEGGihsa:2882.
UCSCiuc001cue.4. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320068 mRNA. Translation: AAN76501.1.
AY358402 mRNA. Translation: AAQ88768.1.
AK027683 mRNA. Translation: BAB55294.1.
DQ096732 Genomic DNA. Translation: AAY88741.1.
AL356976 Genomic DNA. Translation: CAI22476.1.
BC032788 mRNA. Translation: AAH32788.1.
AF091092 mRNA. Translation: AAC72961.1. Sequence problems.
CCDSiCCDS569.1.
RefSeqiNP_056511.2. NM_015696.4.
UniGeneiHs.43728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P31X-ray2.00A/B20-177[»]
ProteinModelPortaliQ96SL4.
SMRiQ96SL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109139. 36 interactors.
IntActiQ96SL4. 6 interactors.
MINTiMINT-1466561.
STRINGi9606.ENSP00000354677.

Chemistry databases

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3606. HsGPx07.

PTM databases

iPTMnetiQ96SL4.
PhosphoSitePlusiQ96SL4.

Polymorphism and mutation databases

BioMutaiGPX7.
DMDMi33516901.

Proteomic databases

EPDiQ96SL4.
MaxQBiQ96SL4.
PaxDbiQ96SL4.
PeptideAtlasiQ96SL4.
PRIDEiQ96SL4.

Protocols and materials databases

DNASUi2882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361314; ENSP00000354677; ENSG00000116157.
GeneIDi2882.
KEGGihsa:2882.
UCSCiuc001cue.4. human.

Organism-specific databases

CTDi2882.
DisGeNETi2882.
GeneCardsiGPX7.
HGNCiHGNC:4559. GPX7.
HPAiHPA025829.
MIMi614266. phenotype.
615784. gene.
neXtProtiNX_Q96SL4.
OpenTargetsiENSG00000116157.
PharmGKBiPA28955.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
HOVERGENiHBG004333.
InParanoidiQ96SL4.
KOiK00432.
OMAiCAQREQD.
OrthoDBiEOG091G0OJG.
PhylomeDBiQ96SL4.
TreeFamiTF331942.

Enzyme and pathway databases

BioCyciZFISH:HS03989-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGPX7. human.
EvolutionaryTraceiQ96SL4.
GeneWikiiGPX7.
GenomeRNAii2882.
PROiQ96SL4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116157.
CleanExiHS_GPX6.
HS_GPX7.
GenevisibleiQ96SL4. HS.

Family and domain databases

CDDicd00340. GSH_Peroxidase. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR013376. Glut_perox_Gpx7.
IPR000889. 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.
TIGRFAMsiTIGR02540. gpx7. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGPX7_HUMAN
AccessioniPrimary (citable) accession number: Q96SL4
Secondary accession number(s): O95337, Q5T501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.