ERP29

Endoplasmic reticulum protein 29
PDB rendering based on 1g7e.
Available structures PDB 1g7e
Identifiers
Symbols	ERP29; C12orf8; ERp28; ERp31; PDI-DB; PDIA9
External IDs	OMIM: 602287 MGI: 1914647 HomoloGene: 4963 GeneCards: ERP29 Gene
Gene Ontology Molecular function • protein disulfide isomerase activity Cellular component • endoplasmic reticulum • endoplasmic reticulum lumen • melanosome Biological process • protein folding • intracellular protein transport • protein secretion Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10961	67397
Ensembl	ENSG00000089248	ENSMUSG00000029616
UniProt	P30040	P57759
RefSeq (mRNA)	NM_001034025.1	NM_026129.2
RefSeq (protein)	NP_001029197.1	NP_080405.1
Location (UCSC)	Chr 12: 112.45 – 112.46 Mb	Chr 5: 121.88 – 121.9 Mb
PubMed search	[1]	[2]

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

• Hubbard MJ (2003). "Functional proteomics: The goalposts are moving.". Proteomics 2 (9): 1069–78. doi:10.1002/1615-9861(200209)2:9<1069::AID-PROT1069>3.0.CO;2-R. PMID 12362325. 
• Mkrtchian S, Sandalova T (2006). "ERp29, an unusual redox-inactive member of the thioredoxin family.". Antioxid. Redox Signal. 8 (3–4): 325–37. doi:10.1089/ars.2006.8.325. PMID 16677078. 
• Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669. 
• Hughes GJ, Frutiger S, Paquet N, et al. (1994). "Human liver protein map: update 1993". Electrophoresis 14 (11): 1216–22. doi:10.1002/elps.11501401181. PMID 8313870. 
• Mkrtchian S, Fang C, Hellman U, Ingelman-Sundberg M (1998). "A stress-inducible rat liver endoplasmic reticulum protein, ERp29". Eur. J. Biochem. 251 (1–2): 304–13. doi:10.1046/j.1432-1327.1998.2510304.x. PMID 9492298. 
• Ferrari DM, Nguyen Van P, Kratzin HD, Söling HD (1998). "ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif". Eur. J. Biochem. 255 (3): 570–9. doi:10.1046/j.1432-1327.1998.2550570.x. PMID 9738895. 
• Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping". Electrophoresis 21 (17): 3785–96. doi:10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2. PMID 11271497. 
• Shnyder SD, Hubbard MJ (2002). "ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production". J. Histochem. Cytochem. 50 (4): 557–66. doi:10.1177/002215540205000413. PMID 11897809. 
• Sargsyan E, Baryshev M, Backlund M, et al. (2002). "Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29". Gene 285 (1–2): 127–39. doi:10.1016/S0378-1119(02)00417-1. PMID 12039039. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Basrur V, Yang F, Kushimoto T, et al. (2003). "Proteomic analysis of early melanosomes: identification of novel melanosomal proteins". J. Proteome Res. 2 (1): 69–79. doi:10.1021/pr025562r. PMID 12643545. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
• Cheretis C, Dietrich F, Chatzistamou I, et al. (2007). "Expression of ERp29, an endoplasmic reticulum secretion factor in basal-cell carcinoma". The American Journal of dermatopathology 28 (5): 410–2. doi:10.1097/01.dad.0000211521.49810.ac. PMID 17012915. 
• Zheng J, Liu X, Yan X, et al. (2006). "Purification and structural characterization of human ERp29". Protein Pept. Lett. 13 (8): 753–9. doi:10.2174/092986606777841190. PMID 17073718. 
• Chi A, Valencia JC, Hu ZZ, et al. (2007). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes". J. Proteome Res. 5 (11): 3135–44. doi:10.1021/pr060363j. PMID 17081065. 
• Lippert U, Diao D, Barak NN, Ferrari DM (2007). "Conserved structural and functional properties of D-domain containing redox-active and -inactive protein disulfide isomerase-related protein chaperones". J. Biol. Chem. 282 (15): 11213–20. doi:10.1074/jbc.M604440200. PMID 17296603.