Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB Subcellular Location vocabulary mapping

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000116

Gene Ontology annotation based on RHEA mapping of reactions

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10671517

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.

ERO1-L is an ER-localized, glycosylated membrane-associated protein that complements the yeast ero1-1 mutant and is involved in oxidative ER protein folding; activity requires Cys-394/Cys-397.

PMID:11707400

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.

Human Ero1-Lalpha and Ero1-Lbeta facilitate disulfide bond formation in immunoglobulin subunits by selectively oxidizing PDI, standing at a crucial point of an electron flow from nascent secretory proteins through PDI; ERp57 redox state is not affected.

PMID:17170699

ERp57 is essential for efficient folding of glycoproteins sharing common structural domains.

PMID:19946888

Defining the membrane proteome of NK cells.

PMID:20802462

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated.

PMID:25416956

A proteome-scale map of the human interactome network.

PMID:29858230

Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α.

FAM20C phosphorylates ERO1A at Ser145 in the Golgi, increasing its enzymatic activity; phosphomimetic S145E doubles activity and accelerates immunoglobulin folding; ERO1A is required for proper immunoglobulin folding and is retained in the ER via ERP44.

PMID:32296183

A reference map of the human binary protein interactome.

Reactome:R-HSA-3341296

Reactome ER-lumen oxidative folding annotation for ERO1A

file:human/ERO1A/ERO1A-uniprot.txt

UniProt entry Q96HE7 (ERO1A_HUMAN), ERO1-like protein alpha

FAD-dependent ER sulfhydryl oxidase (EC 1.8.3.2) that reoxidizes P4HB/PDI to drive disulfide-bond formation and passes electrons to O2 generating H2O2; peripheral ER membrane protein on the lumenal side retained by ERP44; activity tightly regulated by regulatory disulfides and FAM20C phosphorylation; hypoxia-induced.

file:human/ERO1A/ERO1A-deep-research-falcon.md

Falcon deep research report for ERO1A

ERO1A re-oxidizes reduced PDI by accepting electrons through its FAD cofactor, with molecular oxygen as the terminal electron acceptor, producing H2O2; it binds PDI with highest affinity (Kd 1.7 uM) relative to other ER thiol isomerases, and is induced by HIF-1alpha under hypoxia and by the PERK-eIF2alpha-ATF4-CHOP UPR branch.