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ERO1-like protein beta; ERO1-L-beta; endoplasmic oxidoreductin-1-like protein B; oxidoreductin-1-L-beta (ERO1LB)
Function:
1) oxidoreductase
2) provides oxidizing equivalents in the endoplasmic reticulum (ER) for the formation of disulfide bonds
3) directly oxidizes P4HB/PDI isomerase via direct disulfide exchange
4) does NOT act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent
5) does not oxidize all PDI related proteins
a) can discriminate between PDI & related proteins.
b) associates with TXNDC4 but not with GRP54
6) reoxidation involves electron transfer to O2 via FAD
7) association with TXNDC4 retains ERO1LB in the ER
Cofactor: FAD
Structure:
- monomer & homodimer
- belongs to the EROs family
Compartment: endoplasmic reticulum, lumenal side
Expression:
- widely expressed at low level
- expressed at high level in lower digestive tract
- expressed in stomach & duodenum > esophagus
Pathology:
1) source of oxidative stress
2) produces reactive oxygen species (ROS) {H2O2}
3) induced by unfolded protein response
General
glycoprotein
oxidoreductase
Properties
SIZE: entity length = 467 aa
MW = 54 kD
COMPARTMENT: endoplasmic reticulum
MOTIF: signal sequence {1-33}
cysteine residue {C81}
MODIFICATION: cysteine residue {C390}
cysteine residue {C90}
MODIFICATION: cysteine residue {C95}
cysteine residue {C95}
MODIFICATION: cysteine residue {C90}
N-glycosylation site {N122}
N-glycosylation site {N140}
N-glycosylation site {N145}
binding site
SITE: 186-186
FOR-BINDING-OF: FAD
binding site
SITE: 188-188
FOR-BINDING-OF: FAD
binding site
SITE: 199-199
FOR-BINDING-OF: FAD
binding site
SITE: 251-251
FOR-BINDING-OF: FAD
binding site
SITE: 254-254
FOR-BINDING-OF: FAD
binding site
SITE: 286-286
FOR-BINDING-OF: FAD
N-glycosylation site {N383}
cysteine residue {C390}
MODIFICATION: cysteine residue {C81}
cysteine residue {C393}
MODIFICATION: cysteine residue {C396}
cysteine residue {C396}
MODIFICATION: cysteine residue {C393}
Database Correlations
UniProt Q86YB8
Pfam PF04137
Entrez Gene 56605
Kegg hsa:56605
References
UniProt :accession Q86YB8