ERO1B
entrez
56605
canonical
uniprot
Q86YB8
canonical
ensembl
ENSG00000086619
resolver
ensp
ENSP00000346635
resolver
genesymbol
ERO1B
resolver
genesymbol_syn
ERO1LB
resolver
hgnc
HGNC:14355
resolver
uniprot
B4DF57
resolver
uniprot
Q5T1H4
resolver
uniprot
Q8IZ11
resolver
uniprot
Q9NR62
resolver
uniprot_entry
ERO1B_HUMAN
resolver
uniprot_sec
B4DF57
resolver
uniprot_sec
Q5T1H4
resolver
uniprot_sec
Q8IZ11
resolver
uniprot_sec
Q9NR62
resolver
activity_regulation
ACTIVITY REGULATION: Glutathione may be required to regulate its activity in the endoplasmic reticulum. {ECO:0000269|PubMed:15161913}.
uniprot
proteins
amino_acid_sequence
MSQGVRRAGAGQGVAAAVQLLVTLSFLRSVVEAQVTGVLDDCLCDIDSIDNFNTYKIFPKIKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGHSNKYLKMANNTKELEDCEQANKLGAINSTLSNQSKEAFIDWARYDDSRDHFCELDDERSPAAQYVDLLLNPERYTGYKGTSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLCLEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFKHRFDPVETKGEGPRRLKNLYFLYLIELRALSKVAPYFERSIVDLYTGNAEEDADTKTLLLNIFQDTKSFPMHFDEKSMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEIQKLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRDLQNFKVLLQHSR
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. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis. {ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:21091435}.
uniprot
proteins
mass_dalton
53543
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="C->A: No effect on thiol oxidase activity when DTT is used as an electron donor; when associated with A-95. Loss of thiol oxidase activity when P4HB is used as an electron donor; when associated with A-95."; /evidence="ECO:0000269|PubMed:21091435"; MUTAGEN 95; /note="C->A: No effect on thiol oxidase activity when DTT is used as an electron donor; when associated with A-90. Loss of thiol oxidase activity when P4HB is used as an electron donor; when associated with A-90."; /evidence="ECO:0000269|PubMed:21091435"; MUTAGEN 100; /note="C->A: Slightly decreased thiol oxidase activity. Significant increased thiol oxidase activity; when associated with A-130."; /evidence="ECO:0000269|PubMed:21091435"; MUTAGEN 130; /note="C->A: Small increase in thiol oxidase activity. Significant increased thiol oxidase activity; when associated with A-130."; /evidence="ECO:0000269|PubMed:21091435"; MUTAGEN 390; /note="C->A: Strong decrease in P4HB-binding. Efficient homodimerization with both wild-type and A-390 mutated protein."; /evidence="ECO:0000269|PubMed:16012172"; MUTAGEN 393; /note="C->A: Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein. Loss of thiol oxidase activity when DTT or P4HB are used as an electron donor; when associated with A-396."; /evidence="ECO:0000269|PubMed:16012172, ECO:0000269|PubMed:21091435"; MUTAGEN 396; /note="C->A: Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein, but loss of homodimerization with A-396 mutated protein. Loss of thiol oxidase activity when DTT or P4HB are used as an electron donor; when associated with A-393."; /evidence="ECO:0000269|PubMed:16012172, ECO:0000269|PubMed:21091435
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10818100, ECO:0000269|PubMed:16263699}.; PTM: The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds constitute the redox-active center. The Cys-90/Cys-95 disulfide bond accepts electron from P4HB and funnel them to the active site disulfide Cys-393/Cys-396. The Cys-81/Cys-390 disulfide bond may be critical for structural stability. Two long-range disulfide bonds participate in loose feedback regulation. The Cys-90/Cys-130 disulfide bond may be the predominant regulatory switch to modulate the catalytic activity, while the Cys-100/Cys-262 disulfide bond may play an auxiliary regulatory role. {ECO:0000305|PubMed:21091435}.
uniprot
proteins
protein_family
EROs family
uniprot
proteins
pubmed
10818100
uniprot
proteins
pubmed
11707400
uniprot
proteins
pubmed
11847130
uniprot
proteins
pubmed
12752442
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15161913
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16012172
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
21091435
uniprot
proteins
sequence_length
467
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10818100}; Peripheral membrane protein {ECO:0000269|PubMed:10818100}; Lumenal side {ECO:0000269|PubMed:10818100}. Note=The association with ERP44 may be essential for its retention in the endoplasmic reticulum.
uniprot
proteins