ERO1L

Endoplasmic reticulum oxidoreductase alpha
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3AHQ​, 3AHR​
Identifiers
Symbols	ERO1A ; ERO1-L; ERO1-L-alpha; ERO1-alpha; ERO1L; ERO1LA; Ero1alpha
External IDs	OMIM: 615435 MGI: 1354385 HomoloGene: 49392 ChEMBL: 1671609 GeneCards: ERO1A Gene
Gene ontology Molecular function • protein disulfide isomerase activity • protein binding • protein disulfide oxidoreductase activity • oxidoreductase activity • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Cellular component • endoplasmic reticulum • endoplasmic reticulum lumen • endoplasmic reticulum membrane • membrane • intracellular membrane-bounded organelle Biological process • response to reactive oxygen species • protein folding • cellular protein modification process • response to temperature stimulus • 4-hydroxyproline metabolic process • protein maturation by protein folding • extracellular matrix organization • endoplasmic reticulum unfolded protein response • response to endoplasmic reticulum stress • cellular protein metabolic process • cell redox homeostasis • brown fat cell differentiation • chaperone mediated protein folding requiring cofactor • release of sequestered calcium ion into cytosol • oxidation-reduction process • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	30001	50527
Ensembl	ENSG00000197930	ENSMUSG00000021831
UniProt	Q96HE7	Q8R180
RefSeq (mRNA)	NM_014584	NM_015774
RefSeq (protein)	NP_055399	NP_056589
Location (UCSC)	Chr 14: 52.64 – 52.7 Mb	Chr 14: 45.28 – 45.32 Mb
PubMed search

ERO1-like protein alpha is a protein that in humans is encoded by the ERO1L gene.^[1][2]

Interactions

ERO1L has been shown to interact with TXNDC4^[3] and P4HB.^[3][4]

References

1. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (Mar 2000). "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum". J Biol Chem 275 (7): 4827–33. doi:10.1074/jbc.275.7.4827. PMID 10671517.
2. "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)".
3. Anelli, Tiziana; Alessio Massimo; Mezghrani Alexandre; Simmen Thomas; Talamo Fabio; Bachi Angela; Sitia Roberto (Feb 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. (England) 21 (4): 835–44. doi:10.1093/emboj/21.4.835. ISSN 0261-4189. PMC 125352. PMID 11847130.
4. Mezghrani, A; Fassio A; Benham A; Simmen T; Braakman I; Sitia R (Nov 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. (England) 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. ISSN 0261-4189. PMC 125306. PMID 11707400.

Further reading

• Pagani M, Fabbri M, Benedetti C; et al. (2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response.". J. Biol. Chem. 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.
• Benham AM, Cabibbo A, Fassio A; et al. (2000). "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha.". EMBO J. 19 (17): 4493–502. doi:10.1093/emboj/19.17.4493. PMC 302061. PMID 10970843.
• Pagani M, Pilati S, Bertoli G; et al. (2001). "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function.". FEBS Lett. 508 (1): 117–20. doi:10.1016/S0014-5793(01)03034-4. PMID 11707280.
• Mezghrani A, Fassio A, Benham A; et al. (2002). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells.". EMBO J. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.
• Anelli T, Alessio M, Mezghrani A; et al. (2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family.". EMBO J. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
• Tsai B, Rapoport TA (2002). "Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1.". J. Cell Biol. 159 (2): 207–16. doi:10.1083/jcb.200207120. PMC 2173060. PMID 12403808.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gess B, Hofbauer KH, Wenger RH; et al. (2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha.". Eur. J. Biochem. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442.
• Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Anelli T, Alessio M, Bachi A; et al. (2003). "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44.". EMBO J. 22 (19): 5015–22. doi:10.1093/emboj/cdg491. PMC 204474. PMID 14517240.
• Bertoli G, Simmen T, Anelli T; et al. (2004). "Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.". J. Biol. Chem. 279 (29): 30047–52. doi:10.1074/jbc.M403192200. PMID 15136577.
• Molteni SN, Fassio A, Ciriolo MR; et al. (2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.". J. Biol. Chem. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913.
• van Lith M, Hartigan N, Hatch J, Benham AM (2005). "PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.". J. Biol. Chem. 280 (2): 1376–83. doi:10.1074/jbc.M408651200. PMID 15475357.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• May D, Itin A, Gal O; et al. (2005). "Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer.". Oncogene 24 (6): 1011–20. doi:10.1038/sj.onc.1208325. PMID 15592500.
• Otsu M, Bertoli G, Fagioli C; et al. (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44.". Antioxid. Redox Signal. 8 (3-4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.