VPS29
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| Vacuolar protein sorting 29 homolog (S. cerevisiae) | |||||||||||||
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 PDB rendering based on 1w24. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | VPS29; DC15; PEP11 | ||||||||||||
| External IDs | OMIM: 606932 MGI: 1928344 HomoloGene: 9433 GeneCards: VPS29 Gene | ||||||||||||
| EC number | 3.1.3.3 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 51699 | 56433 | |||||||||||
| Ensembl | ENSG00000111237 | ENSMUSG00000029462 | |||||||||||
| UniProt | Q9UBQ0 | Q9QZ88 | |||||||||||
| RefSeq (mRNA) | NM_016226 | NM_019780 | |||||||||||
| RefSeq (protein) | NP_057310 | NP_062754 | |||||||||||
| Location (UCSC) | Chr 12: 110.93 – 110.94 Mb | Chr 5: 122.35 – 122.36 Mb | |||||||||||
| PubMed search | |||||||||||||
VPS29 is a human gene coding for the vacuolar protein sorting protein Vps29, a component of the retromer complex.[1]
Yeast homolog
The homologous protein (one that performs the same function) in yeast is Vacuolar protein sorting 29 homolog (S. cerevisiae).[2]
Function
VPS29 belongs to a group of genes coding for vacuolar protein sorting (VPS) proteins that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases.[3] The protein encoded by this gene, Vps29, is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. Vps29 may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment.[4] Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.[2]
References
- ↑ Edgar AJ, Polak JM (November 2000). "Human homologues of yeast vacuolar protein sorting 29 and 35". Biochem. Biophys. Res. Commun. 277 (3): 622–30. doi:10.1006/bbrc.2000.3727. PMID 11062004.
- ↑ 2.0 2.1 "Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)".
- ↑ Haft CR, de la Luz Sierra M, Bafford R, Lesniak MA, Barr VA, Taylor SI (December 2000). "Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes". Mol. Biol. Cell 11 (12): 4105–16. PMC 15060. PMID 11102511.
- ↑ Bonifacino JS, Hurley JH (August 2008). "Retromer". Curr. Opin. Cell Biol. 20 (4): 427–36. doi:10.1016/j.ceb.2008.03.009. PMC 2833274. PMID 18472259.
Further reading
- Seaman MN, McCaffery JM, Emr SD (1998). "A Membrane Coat Complex Essential for Endosome-to-Golgi Retrograde Transport in Yeast". J. Cell Biol. 142 (3): 665–81. doi:10.1083/jcb.142.3.665. PMC 2148169. PMID 9700157.
- Edgar AJ, Polak JM (2000). "Human homologues of yeast vacuolar protein sorting 29 and 35". Biochem. Biophys. Res. Commun. 277 (3): 622–30. doi:10.1006/bbrc.2000.3727. PMID 11062004.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Haft CR, de la Luz Sierra M, Bafford R et al. (2001). "Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes". Mol. Biol. Cell 11 (12): 4105–16. PMC 15060. PMID 11102511.
- Wiemann S, Weil B, Wellenreuther R et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
- Simpson JC, Wellenreuther R, Poustka A et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
- 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.
- Vergés M, Luton F, Gruber C et al. (2004). "The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor". Nat. Cell Biol. 6 (8): 763–9. doi:10.1038/ncb1153. PMID 15247922.
- Mingot JM, Bohnsack MT, Jäkle U, Görlich D (2005). "Exportin 7 defines a novel general nuclear export pathway". EMBO J. 23 (16): 3227–36. doi:10.1038/sj.emboj.7600338. PMC 514512. PMID 15282546.
- 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.
- Wiemann S, Arlt D, Huber W et al. (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
- Wang D, Guo M, Liang Z et al. (2005). "Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites". J. Biol. Chem. 280 (24): 22962–7. doi:10.1074/jbc.M500464200. PMID 15788412.
- Mehrle A, Rosenfelder H, Schupp I et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
- Damen E, Krieger E, Nielsen JE et al. (2006). "The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide". Biochem. J. 398 (3): 399–409. doi:10.1042/BJ20060033. PMC 1559457. PMID 16737443.
- Rojas R, Kametaka S, Haft CR, Bonifacino JS (2007). "Interchangeable but Essential Functions of SNX1 and SNX2 in the Association of Retromer with Endosomes and the Trafficking of Mannose 6-Phosphate Receptors". Mol. Cell. Biol. 27 (3): 1112–24. doi:10.1128/MCB.00156-06. PMC 1800681. PMID 17101778.
- Hierro A, Rojas AL, Rojas R et al. (2007). "Functional architecture of the retromer cargo-recognition complex". Nature 449 (7165): 1063–7. doi:10.1038/nature06216. PMC 2377034. PMID 17891154.
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