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ERO1-like protein alpha; ERO1-L; ERO1-L-alpha; endoplasmic oxidoreductin-1-like protein; oxidoreductin-1-L-alpha (ERO1L)
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
8) involved in folding of immunoglobulins
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 upper digestive tract esophagus > stomach, duodenum
- induced by hypoxia
Pathology:
- release of unfolded cholera toxin (retrotranslocation) from reduced P4HB/PDI during infection by V.cholerae
General
glycoprotein
oxidoreductase
Properties
SIZE: entity length = 468 aa
MW = 54 kD
COMPARTMENT: endoplasmic reticulum
MOTIF: signal sequence {1-23}
cysteine residue {C35}
MODIFICATION: cysteine residue {C46}
cysteine residue {C37}
MODIFICATION: cysteine residue {C48}
cysteine residue {C46}
MODIFICATION: cysteine residue {C35}
cysteine residue {C48}
MODIFICATION: cysteine residue {C37}
cysteine residue {C85}
MODIFICATION: cysteine residue {C391}
cysteine residue {C94}
MODIFICATION: cysteine residue {C131}
cysteine residue {C94}
MODIFICATION: cysteine residue {C99}
cysteine residue {C99}
MODIFICATION: cysteine residue {C94}
cysteine residue {C99}
MODIFICATION: cysteine residue {C104}
cysteine residue {C104}
MODIFICATION: cysteine residue {C99}
cysteine residue {C131}
MODIFICATION: cysteine residue {C94}
binding site
SITE: 187-187
FOR-BINDING-OF: FAD
binding site
SITE: 189-189
FOR-BINDING-OF: FAD
binding site
SITE: 200-200
FOR-BINDING-OF: FAD
cysteine residue {C208}
MODIFICATION: cysteine residue {C241}
cysteine residue {C241}
MODIFICATION: cysteine residue {C208}
binding site
SITE: 252-252
FOR-BINDING-OF: FAD
binding site
SITE: 255-255
FOR-BINDING-OF: FAD
N-glycosylation site {N280}
binding site
SITE: 287-287
FOR-BINDING-OF: FAD
N-glycosylation site {N384}
cysteine residue {C391}
MODIFICATION: cysteine residue {C85}
cysteine residue {C394}
MODIFICATION: cysteine residue {C397}
cysteine residue {C397}
MODIFICATION: cysteine residue {C394}
Database Correlations
UniProt Q96HE7
Pfam PF04137
Entrez Gene 30001
Kegg hsa:30001
References
UniProt :accession Q96HE7