Ero1a
entrez
171562
canonical
uniprot
Q8R4A1
canonical
ensembl
ENSRNOG00000006462
resolver
ensembl
ENSRNOG00055026863
resolver
ensembl
ENSRNOG00060028887
resolver
ensembl
ENSRNOG00065032122
resolver
ensp
ENSRNOP00000094430
resolver
genesymbol
Ero1a
resolver
genesymbol_syn
Ero1l
resolver
genesymbol_syn
Giig11
resolver
uniprot
Q8VH29
resolver
uniprot
Q8VH30
resolver
uniprot_entry
ERO1A_RAT
resolver
uniprot_sec
Q8VH29
resolver
uniprot_sec
Q8VH30
resolver
activity_regulation
ACTIVITY REGULATION: Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-130, and between Cys-99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MGRGWGLLVGLLGVVWLLRSGQGEEQQQETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLRKPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSKEANLLEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDSFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWRIWSVIYEENCFKPQTIQRPLASGQGKHKENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDNWLEKKWGHNVTEFQQRFDGVLTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKVQDVENKELLLEILHEVKSFPLHFDENSFFAGDKNEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFQLTRQEIVSLFNAFGRISTSVRELENFRHLLQNVH
uniprot
proteins
ec_number
1.8.3.2
uniprot
proteins
function
FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000250|UniProtKB:Q96HE7}.
uniprot
proteins
mass_dalton
54018
uniprot
proteins
post_translational_modification
PTM: N-glycosylated.; PTM: The Cys-94/Cys-99 and Cys-390/Cys-393 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-390/Cys-393. The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-130 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on Ser-144 by FAM20C in the Golgi which increases its enzymatic activity (By similarity). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (By similarity). {ECO:0000250|UniProtKB:Q8R180, ECO:0000250|UniProtKB:Q96HE7}.
uniprot
proteins
protein_family
EROs family
uniprot
proteins
pubmed
12694393
uniprot
proteins
pubmed
12752442
uniprot
proteins
pubmed
24090084
uniprot
proteins
sequence_length
464
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q96HE7}. Secreted {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite {ECO:0000269|PubMed:12694393}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (PubMed:12694393). {ECO:0000250|UniProtKB:Q96HE7, ECO:0000269|PubMed:12694393}.
uniprot
proteins