ERO1L

ERO1A

Available structures

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

MGI: 1354385 HomoloGene: 49392 GeneCards: ERO1A

Gene ontology
Molecular function	• oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor • 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

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

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

ERO1-like protein alpha is a protein that in humans is encoded by the ERO1L gene.^[3]^[4]

Interactions

ERO1L has been shown to interact with TXNDC4^[5] and P4HB.^[5]^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 10671517. doi:10.1074/jbc.275.7.4827.
↑ "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)".
1 2 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. ISSN 0261-4189. PMC 125352 . PMID 11847130. doi:10.1093/emboj/21.4.835.
↑ 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. ISSN 0261-4189. PMC 125306 . PMID 11707400. doi:10.1093/emboj/20.22.6288.

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. PMID 10818100. doi:10.1074/jbc.M003061200.
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. PMC 302061 . PMID 10970843. doi:10.1093/emboj/19.17.4493.
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. PMID 11707280. doi:10.1016/S0014-5793(01)03034-4.
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. PMC 125306 . PMID 11707400. doi:10.1093/emboj/20.22.6288.
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. PMC 125352 . PMID 11847130. doi:10.1093/emboj/21.4.835.
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. PMC 2173060 . PMID 12403808. doi:10.1083/jcb.200207120.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12752442. doi:10.1046/j.1432-1033.2003.03590.x.
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. PMC 403697 . PMID 12975309. doi:10.1101/gr.1293003.
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. PMC 204474 . PMID 14517240. doi:10.1093/emboj/cdg491.
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. PMID 15136577. doi:10.1074/jbc.M403192200.
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. PMID 15161913. doi:10.1074/jbc.M404992200.
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. PMID 15475357. doi:10.1074/jbc.M408651200.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
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. PMID 15592500. doi:10.1038/sj.onc.1208325.
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. PMID 16677073. doi:10.1089/ars.2006.8.274.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

ERO1L

Interactions

References

Further reading