Biology:ERP29

Short description: Protein-coding gene in humans

Generic protein structure example

Endoplasmic reticulum protein 29 (ERp29) is a chaperone protein that in humans is encoded by the ERP29 gene.

Function

ERp29 is a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide-isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms.

Further reading

• "Functional proteomics: The goalposts are moving". Proteomics 2 (9): 1069–78. Sep 2002. doi:10.1002/1615-9861(200209)2:9<1069::AID-PROT1069>3.0.CO;2-R. PMID 12362325. 
• "ERp29, an unusual redox-inactive member of the thioredoxin family". Antioxidants & Redox Signaling 8 (3–4): 325–37. 2006. doi:10.1089/ars.2006.8.325. PMID 16677078. 
• "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. Dec 1992. doi:10.1002/elps.11501301201. PMID 1286669. 
• "Human liver protein map: update 1993". Electrophoresis 14 (11): 1216–22. Nov 1993. doi:10.1002/elps.11501401181. PMID 8313870. 
• "A stress-inducible rat liver endoplasmic reticulum protein, ERp29". European Journal of Biochemistry 251 (1–2): 304–13. Jan 1998. doi:10.1046/j.1432-1327.1998.2510304.x. PMID 9492298. 
• "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif". European Journal of Biochemistry 255 (3): 570–9. Aug 1998. doi:10.1046/j.1432-1327.1998.2550570.x. PMID 9738895. 
• "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping". Electrophoresis 21 (17): 3785–96. Nov 2000. doi:10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2. PMID 11271497. 
• "ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production". The Journal of Histochemistry and Cytochemistry 50 (4): 557–66. Apr 2002. doi:10.1177/002215540205000413. PMID 11897809. 
• "Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29". Gene 285 (1–2): 127–39. Feb 2002. doi:10.1016/S0378-1119(02)00417-1. PMID 12039039. 
• "Proteomic analysis of early melanosomes: identification of novel melanosomal proteins". Journal of Proteome Research 2 (1): 69–79. 2003. doi:10.1021/pr025562r. PMID 12643545. 
• "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. May 2006. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
• "Expression of ERp29, an endoplasmic reticulum secretion factor in basal-cell carcinoma". The American Journal of Dermatopathology 28 (5): 410–2. Oct 2006. doi:10.1097/01.dad.0000211521.49810.ac. PMID 17012915. 
• "Purification and structural characterization of human ERp29". Protein and Peptide Letters 13 (8): 753–9. 2006. doi:10.2174/092986606777841190. PMID 17073718. 
• "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes". Journal of Proteome Research 5 (11): 3135–44. Nov 2006. doi:10.1021/pr060363j. PMID 17081065. 
• "Conserved structural and functional properties of D-domain containing redox-active and -inactive protein disulfide isomerase-related protein chaperones". The Journal of Biological Chemistry 282 (15): 11213–20. Apr 2007. doi:10.1074/jbc.M604440200. PMID 17296603. http://pubman.mpdl.mpg.de/pubman/item/escidoc:595754/component/escidoc:595753/332702.pdf.