KDELR1

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1
Identifiers
Symbols	KDELR1 ; ERD2; ERD2.1; HDEL; PM23
External IDs	Template:OMIM5 Template:MGI HomoloGene: 86772
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE KDELR1 200922 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1, also known as KDELR1, is a human gene.

Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, which is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and functionally similar to the yeast ERD2 gene product.

See Also

KDELR2

Further reading

• Pelham HR (1997). "The dynamic organisation of the secretory pathway". Cell Struct. Funct. 21 (5): 413–9. PMID 9118249.
• Lewis MJ, Pelham HR (1992). "Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum". Cell. 68 (2): 353–64. PMID 1310258.
• Lewis MJ, Pelham HR (1990). "A human homologue of the yeast HDEL receptor". Nature. 348 (6297): 162–3. doi:10.1038/348162a0. PMID 2172835.
• Townsley FM, Wilson DW, Pelham HR (1993). "Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport". EMBO J. 12 (7): 2821–9. PMID 8392934.CS1 maint: Multiple names: authors list (link)
• Aoe T, Cukierman E, Lee A; et al. (1998). "The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1". EMBO J. 16 (24): 7305–16. doi:10.1093/emboj/16.24.7305. PMID 9405360.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Smith JS, Tachibana I, Pohl U; et al. (2000). "A transcript map of the chromosome 19q-arm glioma tumor suppressor region". Genomics. 64 (1): 44–50. doi:10.1006/geno.1999.6101. PMID 10708517.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Majoul I, Straub M, Hell SW; et al. (2001). "KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET". Dev. Cell. 1 (1): 139–53. PMID 11703931.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Matsuda A, Suzuki Y, Honda G; et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways". Oncogene. 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yamamoto K, Hamada H, Shinkai H; et al. (2003). "The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen-activated protein kinase signaling cascades". J. Biol. Chem. 278 (36): 34525–32. doi:10.1074/jbc.M304188200. PMID 12821650.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bard F, Mazelin L, Péchoux-Longin C; et al. (2004). "Src regulates Golgi structure and KDEL receptor-dependent retrograde transport to the endoplasmic reticulum". J. Biol. Chem. 278 (47): 46601–6. doi:10.1074/jbc.M302221200. PMID 12975382.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Breuza L, Halbeisen R, Jenö P; et al. (2004). "Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46". J. Biol. Chem. 279 (45): 47242–53. doi:10.1074/jbc.M406644200. PMID 15308636.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)