Ero1b
entrez
67475
canonical
uniprot
Q8R2E9
canonical
ensembl
ENSMUSG00000057069
resolver
ensp
ENSMUSP00000071864
resolver
ensp
ENSMUSP00000152393
resolver
ensp
ENSMUSP00000294989
resolver
ensp
ENSMUSP00000294999
resolver
enst
ENSMUST00000071973
resolver
enst
ENSMUST00000221560
resolver
genesymbol
Ero1b
resolver
genesymbol_syn
Ero1lb
resolver
uniprot
A0A1Y7VNF4
resolver
uniprot
Q14DN0
resolver
uniprot_entry
A0A1Y7VNF4_MOUSE
resolver
uniprot_entry
ERO1B_MOUSE
resolver
uniprot_sec
Q14DN0
resolver
activity_regulation
ACTIVITY REGULATION: Glutathione may be required to regulate its activity in the endoplasmic reticulum. {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MSPGFRRAVTGQGAAAAVQLLVTLSFLSSLVKTQVTGVLDDCLCDIDSIDKFNTYKIFPKIKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGRSNKYSQAANSTKELDDCEQANKLGAINSTLSNESKEAFIDWARYDDSQDHFCELDDERSPAAQYVDLLLNPERYTGYKGSSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLCLEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFRRRFDPVETKGEGPRRLKNLYFLYLIELRALSKVAPYFERSIVDLYTGNVEDDADTKTLLLSIFQDTKSFPMHFDEKSMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEIQNLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRELQNFKALLQHRR
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, PDIA3, PDIA4, PDIA6 and NXNDC12. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). Involved in oxidative proinsulin folding in pancreatic cells, hence required for glucose homeostasis in vivo. {ECO:0000250, ECO:0000269|PubMed:20308425}.
uniprot
proteins
mass_dalton
53518
uniprot
proteins
mutagenesis
MUTAGEN 396; /note="C->A: Complete loss of disulfide oxidase activity in vitro."; /evidence="ECO:0000269|PubMed:20308425
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250}.; 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 may accept electron from P4HB and funnel them to the active site disulfide Cys-393/Cys-396 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
EROs family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16012172
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20308425
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
467
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Note=The association with ERP44 may be essential for its retention in the endoplasmic reticulum. {ECO:0000250}.
uniprot
proteins