Ero1a
entrez
50527
canonical
uniprot
Q8R180
canonical
ensembl
ENSMUSG00000021831
resolver
ensp
ENSMUSP00000022378
resolver
enst
ENSMUST00000022378
resolver
genesymbol
Ero1a
resolver
genesymbol_syn
Ero1l
resolver
uniprot
Q4FK57
resolver
uniprot
Q9CV47
resolver
uniprot
Q9QY03
resolver
uniprot_entry
ERO1A_MOUSE
resolver
uniprot_entry
Q4FK57_MOUSE
resolver
uniprot_sec
Q9CV47
resolver
uniprot_sec
Q9QY03
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
MGRAWGLLVGLLGVVWLLRLGHGEERRPETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLKKPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSEEANRIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDSFCEIDDIQSPDAEYVDLLLNPERYTGYKGPDAWRIWSVIYEENCFKPQTIQRPLASGRGKSKENTFYNWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDTWLEKKWGHNVTEFQQRFDGILTEGEGPRRLRNLYFLYLIELRALSKVLPFFERPDFQLFTGNKVQDAENKALLLEILHEIKSFPLHFDENSFFAGDKNEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFQLTRQEIVSLFNAFGRISTSVRELENFRHLLQNVH
uniprot
proteins
ec_number
1.8.3.2
uniprot
proteins
function
FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum (PubMed:20308425). 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 (By similarity). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1 (PubMed:19752026). {ECO:0000250|UniProtKB:Q96HE7, ECO:0000269|PubMed:19752026, ECO:0000269|PubMed:20308425}.
uniprot
proteins
mass_dalton
54084
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250}.; 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 (PubMed:29858230). It is also induced by hypoxia and reductive stress (By similarity). {ECO:0000250|UniProtKB:Q96HE7, ECO:0000269|PubMed:29858230}.
uniprot
proteins
protein_family
EROs family
uniprot
proteins
pubmed
10671517
uniprot
proteins
pubmed
12752442
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19752026
uniprot
proteins
pubmed
20308425
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29858230
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:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000250|UniProtKB:Q96HE7}.
uniprot
proteins