GPX7
entrez
2882
canonical
uniprot
Q96SL4
canonical
ensembl
ENSG00000116157
resolver
ensp
ENSP00000354677
resolver
enst
ENST00000361314
resolver
genesymbol
GPX7
resolver
genesymbol_syn
GPX6
resolver
hgnc
HGNC:4559
resolver
uniprot
O95337
resolver
uniprot
Q5T501
resolver
uniprot_entry
GPX7_HUMAN
resolver
uniprot_sec
O95337
resolver
uniprot_sec
Q5T501
resolver
amino_acid_sequence
MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFTDQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAVTGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLILLKREDL
uniprot
proteins
disease_involvement
DISEASE: Barrett esophagus (BE) [MIM:614266]: A 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. {ECO:0000269|PubMed:22157330}. Note=The disease is caused by variants 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.
uniprot
proteins
ec_number
5.3.4.1
uniprot
proteins
function
FUNCTION: Acts as an endoplasmic reticulum (ER) thiol peroxidase that maintains ER redox homeostasis and supports oxidative protein folding (PubMed:32719007). Rapidly reacts with hydrogen peroxide to form sulfenylated/disulfide intermediates and oxidizes protein disulfide isomerase (PDI) family members, promoting disulfide-bond formation (PubMed:21215271). Functions in a redox relay with ERO1A, using ERO1A-generated H(2)O(2) to drive PDI oxidation, linking peroxide detoxification to productive disulfide formation (PubMed:23919619). Protects esophageal epithelia from hydrogen peroxide-induced oxidative stress by reducing reactive oxygen species (ROS) and preventing oxidative DNA damage and double-strand breaks (PubMed:22157330). {ECO:0000269|PubMed:21215271, ECO:0000269|PubMed:22157330, ECO:0000269|PubMed:23919619, ECO:0000269|PubMed:32719007}.
uniprot
proteins
mass_dalton
20996
uniprot
proteins
mutagenesis
MUTAGEN 57; /note="C->A: Complete loss of PDI oxidation activity."; /evidence="ECO:0000269|PubMed:23919619"; MUTAGEN 86; /note="C->A: No loss of PDI oxidation activity."; /evidence="ECO:0000269|PubMed:23919619"; MUTAGEN 92; /note="Q->S: Strong loss of PDI oxidation activity."; /evidence="ECO:0000269|PubMed:32719007
uniprot
proteins
post_translational_modification
PTM: H(2)O(2) oxidizes Cys-57 to sulfenic acid, which can be resolved by Cys-86 to form an intramolecular disulfide bond. {ECO:0000269|PubMed:21215271}.
uniprot
proteins
protein_family
Glutathione peroxidase family
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
21215271
uniprot
proteins
pubmed
22157330
uniprot
proteins
pubmed
23919619
uniprot
proteins
pubmed
32719007
uniprot
proteins
sequence_length
187
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:21215271}.
uniprot
proteins