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ERO1L (human)

Overview ERO1L Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for 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. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. 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. Belongs to the EROs family. Note: This description may include information from UniProtKB. Protein type: Secreted; Secreted, signal peptide; Oxidoreductase; EC 1.8.4.- Cellular Component: endoplasmic reticulum membrane; membrane; intracellular membrane-bound organelle; endoplasmic reticulum lumen; endoplasmic reticulum Molecular Function: FAD binding; oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor Biological Process: response to temperature stimulus; protein thiol-disulfide exchange; protein folding; chaperone cofactor-dependent protein folding; unfolded protein response; release of sequestered calcium ion into cytosol; brown fat cell differentiation; protein modification process Reference #:  Q96HE7 (UniProtKB) Alt. Names/Synonyms: Endoplasmic oxidoreductin-1-like protein; ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1-like (S. cerevisiae); ERO1-like protein alpha; ERO1A; ERO1L; Oxidoreductin-1-L-alpha Gene Symbols: ERO1L Molecular weight: 54,393 Da Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below ERO1L 3AHQ - A=22-468 (human) 3AHR - A=22-468 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 3AHQ 3AHR  |  ENZYME  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		Y73-p	QKLLESDyFRYYKVN
0	1		S143-p	RLGAVDEsLSEETQk
0	1		K150-u	sLSEETQkAVLQWTK
0	1		Y248-p	CVEKRAFyRLISGLH
0	1		Y266-p	NVHLSARyLLQETWL
0	1		S353-p	EILHEIKsFPLHFDE

	mouse
Y73	QKLLESDYFRYYKVN
S142	RLGAVDESLSEETQK
K149	SLSEETQKAVLQWTK
Y244	CVEKRAFYRLISGLH
Y262	NVHLSARYLLQDTWL
S349	EILHEIKSFPLHFDE

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