ERO1A
entrez
30001
canonical
uniprot
Q96HE7
canonical
ensembl
ENSG00000197930
resolver
ensp
ENSP00000379042
resolver
ensp
ENSP00000580796
resolver
ensp
ENSP00000580797
resolver
ensp
ENSP00000634687
resolver
ensp
ENSP00000634688
resolver
ensp
ENSP00000788546
resolver
enst
ENST00000395686
resolver
genesymbol
ERO1A
resolver
genesymbol_syn
ERO1L
resolver
hgnc
HGNC:13280
resolver
uniprot
A8K9X4
resolver
uniprot
A8MYW1
resolver
uniprot
Q7LD45
resolver
uniprot
Q9P1Q9
resolver
uniprot
Q9UKV6
resolver
uniprot_entry
ERO1A_HUMAN
resolver
uniprot_sec
A8K9X4
resolver
uniprot_sec
A8MYW1
resolver
uniprot_sec
Q7LD45
resolver
uniprot_sec
Q9P1Q9
resolver
uniprot_sec
Q9UKV6
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-131, and between Cys-99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. {ECO:0000269|PubMed:15161913, ECO:0000269|PubMed:18833192, ECO:0000269|PubMed:18971943}.
uniprot
proteins
amino_acid_sequence
MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH
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 (PubMed:29858230). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:12403808, ECO:0000269|PubMed:18833192, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870, ECO:0000269|PubMed:29858230}.
uniprot
proteins
mass_dalton
54393
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="C->A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 85; /note="C->S: Induces a decrease in activity."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 94; /note="C->S: Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 99; /note="C->A: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 104; /note="C->A: No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870"; MUTAGEN 104; /note="C->S: No effect."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870"; MUTAGEN 131; /note="C->A: Loss of regulatory disulfide bond formation and increased activity towards P4HB. Loss of regulatory disulfide bond formation and strongly increased activity towards P4HB; when associated with A-85. Loss of regulatory disulfide bond formation, strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-104."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18833192, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870"; MUTAGEN 145; /note="S->A: Abolishes phosphorylation. Does not affect interaction with ERP44."; /evidence="ECO:0000269|PubMed:29858230"; MUTAGEN 145; /note="S->E: Phosphomimetic mutant. Does not affect interaction with ERP44. Shows two-fold increase in enzyme activity. Accelerates immunoglobulin folding."; /evidence="ECO:0000269|PubMed:29858230"; MUTAGEN 166; /note="C->A: No effect."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 208; /note="C->A,S: No effect."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 241; /note="C->A,S: No effect."; /evidence="ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18971943"; MUTAGEN 280; /note="N->A: No effect on activity."; /evidence="ECO:0000269|PubMed:15136577"; MUTAGEN 384; /note="N->A: No effect on activity."; /evidence="ECO:0000269|PubMed:15136577"; MUTAGEN 391; /note="C->A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB."; /evidence="ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:15136577"; MUTAGEN 394; /note="C->A: Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB."; /evidence="ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:15136577, ECO:0000269|PubMed:18833192"; MUTAGEN 395; /note="F->D: Increased catalytical activity."; /evidence="ECO:0000269|PubMed:21091435"; MUTAGEN 397; /note="C->A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB."; /evidence="ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:15136577
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:19159218}.; PTM: The Cys-94/Cys-99 and Cys-394/Cys-397 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-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870). {ECO:0000250, ECO:0000269|PubMed:23027870}.; PTM: Phosphorylated on Ser-145 by FAM20C in the Golgi which increases its enzymatic activity (PubMed:29858230). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (PubMed:29858230). {ECO:0000250|UniProtKB:Q8R180, ECO:0000269|PubMed:29858230}.
uniprot
proteins
protein_family
EROs family
uniprot
proteins
pubmed
10671517
uniprot
proteins
pubmed
10818100
uniprot
proteins
pubmed
10970843
uniprot
proteins
pubmed
11707280
uniprot
proteins
pubmed
11707400
uniprot
proteins
pubmed
11847130
uniprot
proteins
pubmed
12403808
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12752442
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14517240
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15136577
uniprot
proteins
pubmed
15161913
uniprot
proteins
pubmed
15475357
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18833192
uniprot
proteins
pubmed
18971943
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20834232
uniprot
proteins
pubmed
21091435
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23027870
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29858230
uniprot
proteins
sequence_length
468
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Peripheral membrane protein {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Lumenal side {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}. Golgi apparatus lumen {ECO:0000269|PubMed:29858230}. Secreted {ECO:0000269|PubMed:29858230}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (PubMed:29858230). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000269|PubMed:29858230}.
uniprot
proteins