ERO1L

Last updated
ERO1A
Available structures
PDB Ortholog search: PDBe RCSB
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
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_014584

NM_015774

RefSeq (protein)

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]

Related Research Articles

<span class="mw-page-title-main">Protein disulfide-isomerase</span> Class of enzymes

Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.

<span class="mw-page-title-main">Calnexin</span> Mammalian protein found in Homo sapiens

Calnexin (CNX) is a 67kDa integral protein of the endoplasmic reticulum (ER). It consists of a large N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short, acidic cytoplasmic tail. In humans, calnexin is encoded by the gene CANX.

<span class="mw-page-title-main">ER oxidoreductin</span>

ER oxidoreductin 1 (Ero1) is an oxidoreductase enzyme that catalyses the formation and isomerization of protein disulfide bonds in the endoplasmic reticulum (ER) of eukaryotes. ER Oxidoreductin 1 (Ero1) is a conserved, luminal, glycoprotein that is tightly associated with the ER membrane, and is essential for the oxidation of protein dithiols. Since disulfide bond formation is an oxidative process, the major pathway of its catalysis has evolved to utilise oxidoreductases, which become reduced during the thiol-disulfide exchange reactions that oxidise the cysteine thiol groups of nascent polypeptides. Ero1 is required for the introduction of oxidising equivalents into the ER and their direct transfer to protein disulfide isomerase (PDI), thereby ensuring the correct folding and assembly of proteins that contain disulfide bonds in their native state.

The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. It has been found to be conserved between mammalian species, as well as yeast and worm organisms.

<span class="mw-page-title-main">PDIA3</span> Protein-coding gene in the species Homo sapiens

Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme encoded by the autosomal gene PDIA3 in humans. This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) to modulate folding of newly synthesized glycoproteins. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.

<span class="mw-page-title-main">P4HB</span> Protein-coding gene in the species Homo sapiens

Protein disulfide-isomerase, also known as the beta-subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans encoded by the P4HB gene. The human P4HB gene is localized in chromosome 17q25. Unlike other prolyl 4-hydroxylase family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB is tightly regulated. Both dimer dissociation and substrate binding are likely to enhance its enzymatic activity during the catalysis process.

<span class="mw-page-title-main">SYVN1</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.

<span class="mw-page-title-main">KDELR1</span> Protein-coding gene in the species Homo sapiens

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1, also known as KDELR1, is a protein which in humans is encoded by the KDELR1 gene.

<span class="mw-page-title-main">SEC22B</span> Protein-coding gene in the species Homo sapiens

Vesicle-trafficking protein SEC22b is a protein that in humans is encoded by the SEC22B gene.

<span class="mw-page-title-main">ERP44</span> Protein-coding gene in the species Homo sapiens

Endoplasmic reticulum resident protein 44 (ERp44) also known as thioredoxin domain-containing protein 4 (TXNDC4) is a protein that in humans is encoded by the ERP44 gene.

<span class="mw-page-title-main">DPM1</span> Protein-coding gene in the species Homo sapiens

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.

<span class="mw-page-title-main">PIGC</span> Enzyme

Phosphatidylinositol N-acetylglucosaminyltransferase subunit C is an enzyme that in humans is encoded by the PIGC gene.

<span class="mw-page-title-main">ERO1LB</span> Protein-coding gene in the species Homo sapiens

ERO1-like protein beta is a protein that in humans is encoded by the ERO1LB gene.

<span class="mw-page-title-main">DNAJC10</span> Protein-coding gene in the species Homo sapiens

DnaJ homolog subfamily C member 10 is a protein that in humans is encoded by the DNAJC10 gene.

<span class="mw-page-title-main">PIGS (gene)</span> Protein-coding gene in the species Homo sapiens

GPI transamidase component PIG-S is an enzyme that in humans is encoded by the PIGS gene. This gene encodes a protein that is involved in GPI-anchor biosynthesis.

<span class="mw-page-title-main">PIGH</span> Protein-coding gene in the species Homo sapiens

Phosphatidylinositol N-acetylglucosaminyltransferase subunit H is an enzyme that in humans is encoded by the PIGH gene. The PIGH gene is located on the reverse strand of chromosome 14 in humans, and is neighbored by TMEM229B.

<span class="mw-page-title-main">DPM3</span> Protein-coding gene in the species Homo sapiens

dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.

<span class="mw-page-title-main">DPM2</span> Protein-coding gene in the species Homo sapiens

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.

A FFAT motif is a protein sequence motif of six defined amino acids plus neighbouring residues that binds to proteins in the VAP protein family.

<span class="mw-page-title-main">PDIA2</span> Protein-coding gene in the species Homo sapiens

Protein disulfide isomerase family A member 2 is a protein that in humans is encoded by the PDIA2 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000197930 - Ensembl, May 2017
  2. 1 2 3 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.
  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.
  6. "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)".
  7. 1 2 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.
  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.

Further reading