EDEM1

EDEM1
Identifiers
Aliases	EDEM1 , EDEM, ER degradation enhancing alpha-mannosidase like protein 1
External IDs	OMIM: 607673 MGI: 2180139 HomoloGene: 33836 GeneCards: EDEM1
Gene location (Human)
Chr.	Chromosome 3 (human)
End	5,219,958 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	108,836,317 bp
RNA expression pattern
	Top expressed in
	bone marrow cells; ; thymus; ; liver; ; right lobe of liver; ; lymph node; ; appendix; ; thymus; ; stromal cell of endometrium; ; monocyte; ; cancellous bone;
	Top expressed in
	lacrimal gland; ; thymus; ; parotid gland; ; crypt of lieberkuhn of small intestine; ; left lobe of liver; ; submandibular gland; ; islet of Langerhans; ; seminal vesicula; ; jejunum; ; pyloric antrum;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calcium ion binding ; misfolded protein binding ; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity ; protein binding ; catalytic activity ;
Cellular component	integral component of membrane ; endoplasmic reticulum membrane ; membrane ; integral component of endoplasmic reticulum membrane ; endoplasmic reticulum ; endoplasmic reticulum quality control compartment ; Golgi membrane ; aggresome ;
Biological process	N-glycan processing ; positive regulation of retrograde protein transport, ER to cytosol ; trimming of terminal mannose on C branch ; IRE1-mediated unfolded protein response ; response to unfolded protein ; ubiquitin-dependent glycoprotein ERAD pathway ; mannose trimming involved in glycoprotein ERAD pathway ; ubiquitin-dependent ERAD pathway ;
	Sources:Amigo / QuickGO
Orthologs
	9695
	192193
	ENSG00000134109
	ENSMUSG00000030104
	Q92611
	Q925U4
	NM_014674
	NM_138677
	NP_055489
	NP_619618
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

ER degradation-enhancing alpha-mannosidase-like 1 is an enzyme that in humans is encoded by the EDEM1 gene.^[5]^[6]

Related Research Articles

Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail.

Endoplasmic-reticulum-associated protein degradation (ERAD) designates a cellular pathway which targets misfolded proteins of the endoplasmic reticulum for ubiquitination and subsequent degradation by a protein-degrading complex, called the proteasome.

Protein transport protein Sec61 subunit beta is a protein that in humans is encoded by the SEC61B gene.

Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene.

Translocon-associated protein subunit alpha is a protein that in humans is encoded by the SSR1 gene.

Derlin-1 also known as degradation in endoplasmic reticulum protein 1 is a membrane protein that in humans is encoded by the DERL1 gene. Derlin-1 is located in the membrane of the endoplasmic reticulum (ER) and is involved in retrotranslocation of specific misfolded proteins and in ER stress. Derlin-1 is widely expressed in thyroid, fat, bone marrow and many other tissues. The protein belongs to the Derlin-family proteins consisting of derlin-1, derlin-2 and derlin-3 that are components in the endoplasmic reticulum-associated protein degradation (ERAD) pathway. The derlins mediate degradation of misfolded lumenal proteins within ER, and are named ‘der’ for their ‘Degradation in the ER’. Derlin-1 is a mammalian homologue of the yeast DER1 protein, a protein involved in the yeast ERAD pathway. Moreover, derlin-1 is a member of the rhomboid-like clan of polytopic membrane proteins.

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase is an enzyme that in humans is encoded by the MAN1B1 gene.

Nucleoporin 160 (Nup160) is a protein that in humans is encoded by the NUP160 gene.

Protein transport protein Sec61 subunit alpha isoform 1 is a protein that in humans is encoded by the SEC61A1 gene.

Diacylglycerol kinase delta is an enzyme that in humans is encoded by the DGKD gene.

Derlin-2 is a protein that in humans is encoded by the DERL2 gene.

Glycoprotein endo-alpha-1,2-mannosidase is an enzyme that in humans is encoded by the MANEA gene.

Derlin-3 is a protein that in humans is encoded by the DERL3 gene.

Epididymis-specific alpha-mannosidase is an enzyme that in humans is encoded by the MAN2B2 gene.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA is an enzyme that in humans is encoded by the MAN1A1 gene.

ER degradation-enhancing alpha-mannosidase-like 2 is an enzyme that in humans is encoded by the EDEM2 gene.

ER degradation-enhancing alpha-mannosidase-like 3 is an enzyme that in humans is encoded by the EDEM3 gene.

Beta-mannosidase is an enzyme with systematic name beta-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene. This enzyme catalyses the following chemical reaction

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB is an enzyme that in humans is encoded by the MAN1A2 gene.

UGGT, or UDP-glucose:glycoprotein glucosyltransferase, is a soluble enzyme resident in the lumen of the endoplasmic reticulum (ER).

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000134109 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030104 - 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.
↑ Molinari M, Calanca V, Galli C, Lucca P, Paganetti P (Feb 2003). "Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle". Science. 299 (5611): 1397–400. doi:10.1126/science.1079474. PMID 12610306. S2CID 24092303.
↑ "Entrez Gene: EDEM1 ER degradation enhancer, mannosidase alpha-like 1".

Nagase T, Seki N, Ishikawa K, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain". DNA Res. 3 (5): 321–9, 341–54. doi: 10.1093/dnares/3.5.321 . PMID 9039502.
Hosokawa N, Wada I, Hasegawa K, et al. (2001). "A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation". EMBO Rep. 2 (5): 415–22. doi:10.1093/embo-reports/kve084. PMC 1083879 . PMID 11375934.
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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Oda Y, Hosokawa N, Wada I, Nagata K (2003). "EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin". Science. 299 (5611): 1394–7. doi:10.1126/science.1079181. PMID 12610305. S2CID 28716209.
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.
Olivari S, Galli C, Alanen H, et al. (2005). "A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation". J. Biol. Chem. 280 (4): 2424–8. doi: 10.1074/jbc.C400534200 . PMID 15579471.
Oda Y, Okada T, Yoshida H, et al. (2006). "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation". J. Cell Biol. 172 (3): 383–93. doi:10.1083/jcb.200507057. PMC 2063648 . PMID 16449189.
Hosokawa N, Wada I, Natsuka Y, Nagata K (2006). "EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin". Genes Cells. 11 (5): 465–76. doi:10.1111/j.1365-2443.2006.00957.x. PMID 16629899. S2CID 19832510.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.
Zuber C, Cormier JH, Guhl B, et al. (2007). "EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites". Proc. Natl. Acad. Sci. U.S.A. 104 (11): 4407–12. Bibcode:2007PNAS..104.4407Z. doi: 10.1073/pnas.0700154104 . PMC 1810509 . PMID 17360537.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000134109 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030104 - 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.

[pmid12610306-5] Molinari M, Calanca V, Galli C, Lucca P, Paganetti P (Feb 2003). "Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle". Science. 299 (5611): 1397–400. doi:10.1126/science.1079474. PMID 12610306. S2CID 24092303.

[entrez-6] "Entrez Gene: EDEM1 ER degradation enhancer, mannosidase alpha-like 1".

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EDEM1

Related Research Articles

References

Further reading