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Protein-coding gene in the species Homo sapiens
VPS29 is a human gene coding for the vacuolar protein sorting protein Vps29, a component of the retromer complex.[ 5]
The homologous protein (one that performs the same function) in yeast is Vacuolar protein sorting 29 homolog (S. cerevisiae) .[ 6]
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 .[ 7] 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.[ 8] Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.[ 6]
^ a b c GRCh38: Ensembl release 89: ENSG00000111237 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029462 – 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 .^ 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 . ^ a b "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. doi :10.1091/mbc.11.12.4105 . 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 .
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. doi :10.1091/mbc.11.12.4105 . 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. Bibcode :2002PNAS...9916899M . 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 . S2CID 22296469 . 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. Bibcode :2007Natur.449.1063H . doi :10.1038/nature06216 . PMC 2377034 PMID 17891154 .
PDB gallery
1w24 : CRYSTAL STRUCTURE OF HUMAN VPS29
1z2w : Crystal structure of mouse Vps29 complexed with Mn2+
1z2x : Crystal structure of mouse Vps29
