ERO1L

Protein-coding gene in the species Homo sapiens

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; OMA:ERO1A - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q22.1	Start	52,639,915 bp^[1]
Band	14q22.1	End	52,695,900 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 14 (mouse)^[2]

Band	14\|14 C1	Start	45,520,544 bp^[2]
Band	14\|14 C1	End	45,556,228 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

oral cavity

buccal mucosa cell

mucosa of pharynx

body of tongue

pericardium

tonsil

gums

amniotic fluid

islet of Langerhans

vena cava

Top expressed in

cumulus cell

epithelium of stomach

pyloric antrum

mucous cell of stomach

decidua

gastrula

granulocyte

hair follicle

epithelium of small intestine

tail of embryo

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor protein binding oxidoreductase activity protein-disulfide reductase 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 cofactor-dependent protein refolding endoplasmic reticulum unfolded protein response intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress protein folding brown fat cell differentiation cellular response to hypoxia response to temperature stimulus apoptotic process protein folding in endoplasmic reticulum cellular response to oxidative stress
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


30001


50527

Ensembl


ENSG00000197930


ENSMUSG00000021831

UniProt


Q96HE7


Q8R180

RefSeq (mRNA)


NM_014584


NM_015774

RefSeq (protein)

NP_055399 NP_001369393 NP_001369394 NP_001369395 NP_001369396
NP_001369397 NP_001369398 NP_001369399 NP_001369400 NP_001369401 NP_001369402 NP_001369403 NP_001369404 NP_001369405


NP_056589

Location (UCSC)

Chr 14: 52.64 – 52.7 Mb

Chr 14: 45.52 – 45.56 Mb

PubMed search

^[3]

^[4]

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000197930 – Ensembl, May 2017
^ ^a ^b ^c 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)".
^ ^a ^b 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. S2CID 34968489.
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" (PDF). European Journal of Biochemistry. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442. Archived from the original (PDF) on 2021-10-16. Retrieved 2020-09-09.
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. S2CID 3919247.
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.