ERO1L

ERO1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3AHQ, 3AHR
Identifiers
Aliases	ERO1A, ERO1-alpha, ERO1LA, ERO1-L, ERO1-L-alpha, ERO1L, Ero1alpha, endoplasmic reticulum oxidoreductase alpha, endoplasmic reticulum oxidoreductase 1 alpha
External IDs	OMIM: 615435 MGI: 1354385 HomoloGene: 49392 GeneCards: ERO1A
Gene location (Human)
Chr.	Chromosome 14 (human)[1]
End	52,695,900 bp[1]
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)[2]
End	45,318,771 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; • GO:0001948 protein binding; • oxidoreductase activity; • protein disulfide oxidoreductase activity; • protein disulfide isomerase activity; • disulfide oxidoreductase activity;
Cellular component	• endoplasmic reticulum lumen; • membrane; • intracellular membrane-bounded organelle; • dendrite; • endoplasmic reticulum; • endoplasmic reticulum membrane;
Biological process	• release of sequestered calcium ion into cytosol; • 4-hydroxyproline metabolic process; • extracellular matrix organization; • protein maturation by protein folding; • cell redox homeostasis; • response to endoplasmic reticulum stress; • chaperone mediated protein folding requiring cofactor; • endoplasmic reticulum unfolded protein response; • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; • cellular protein modification process; • protein folding; • brown fat cell differentiation; • oxidation-reduction process; • cellular response to hypoxia; • response to temperature stimulus; • animal organ senescence; • apoptotic process; • protein folding in endoplasmic reticulum; • cellular response to oxidative stress;
	Sources:Amigo / QuickGO
Orthologs
	30001
	50527
	ENSG00000197930
	ENSMUSG00000021831
	Q96HE7
	Q8R180
	NM_014584
	NM_015774
	NP_055399
	NP_056589
	Wikidata
View/Edit Human	View/Edit Mouse

ERO1-like protein alpha is a protein that in humans is encoded by the ERO1L gene.[5][6]

Interactions

ERO1L has been shown to interact with TXNDC4[7] and P4HB.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000197930 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000021831 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (February 2000). "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum". The Journal of Biological Chemistry. 275 (7): 4827–33. doi:10.1074/jbc.275.7.4827. PMID 10671517.
"Entrez Gene: ERO1L ERO1-like (S. cerevisiae)".
Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (February 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (November 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.

Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R (August 2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". The Journal of Biological Chemistry. 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.
Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, Braakman I (September 2000). "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha". The EMBO Journal. 19 (17): 4493–502. doi:10.1093/emboj/19.17.4493. PMC 302061. PMID 10970843.
Pagani M, Pilati S, Bertoli G, Valsasina B, Sitia R (November 2001). "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function". FEBS Letters. 508 (1): 117–20. doi:10.1016/S0014-5793(01)03034-4. PMID 11707280.
Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (November 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.
Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (February 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
Tsai B, Rapoport TA (October 2002). "Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1". The Journal of Cell Biology. 159 (2): 207–16. doi:10.1083/jcb.200207120. PMC 2173060. PMID 12403808.
Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A (May 2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha". European Journal of Biochemistry. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442.
Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A (October 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Research. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R (October 2003). "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44". The EMBO Journal. 22 (19): 5015–22. doi:10.1093/emboj/cdg491. PMC 204474. PMID 14517240.
Bertoli G, Simmen T, Anelli T, Molteni SN, Fesce R, Sitia R (July 2004). "Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum". The Journal of Biological Chemistry. 279 (29): 30047–52. doi:10.1074/jbc.M403192200. PMID 15136577.
Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R (July 2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum" (PDF). The Journal of Biological Chemistry. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913.
van Lith M, Hartigan N, Hatch J, Benham AM (January 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". The Journal of Biological Chemistry. 280 (2): 1376–83. doi:10.1074/jbc.M408651200. PMID 15475357.
May D, Itin A, Gal O, Kalinski H, Feinstein E, Keshet E (February 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, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxidants & Redox Signaling. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000197930 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021831 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10671517-5] Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (February 2000). "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum". The Journal of Biological Chemistry. 275 (7): 4827–33. doi:10.1074/jbc.275.7.4827. PMID 10671517.

[entrez-6] "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)".

[pmid11847130-7] Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (February 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.

[pmid11707400-8] Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (November 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.

ERO1L

Interactions

References

Further reading