VPS29

VPS29 is a human gene coding for the vacuolar protein sorting protein Vps29, a component of the retromer complex.[5]

VPS29
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1W24, 2R17
Identifiers
Aliases	VPS29, DC15, PEP11, DC7, VPS29 retromer complex component, retromer complex component
External IDs	OMIM: 606932 MGI: 1928344 HomoloGene: 9433 GeneCards: VPS29
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.11 Start 110,491,083 bp[1] End 110,502,111 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 F Start 122,354,369 bp[2] End 122,364,984 bp[2]
Gene ontology Molecular function • GO:0001948 protein binding • metal ion binding • zinc ion binding Cellular component • late endosome • early endosome • endosome membrane • membrane • intracellular membrane-bounded organelle • cytoplasm • cytosol • Retromer • retromer, cargo-selective complex • endosome Biological process • protein transport • retrograde transport, endosome to plasma membrane • Wnt signaling pathway • regulation of autophagy • intracellular protein transport • retrograde transport, endosome to Golgi • GO:0022415 viral process • endocytic recycling Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51699	56433
Ensembl	ENSG00000111237	ENSMUSG00000029462
UniProt	Q9UBQ0 Q05DG7	Q9QZ88
RefSeq (mRNA)	NM_001282150 NM_001282151 NM_016226 NM_057180	NM_019780 NM_001347453 NM_001359226
RefSeq (protein)	NP_001269079 NP_001269080 NP_057310 NP_476528	NP_001334382 NP_062754 NP_001346155
Location (UCSC)	Chr 12: 110.49 – 110.5 Mb	Chr 5: 122.35 – 122.36 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Yeast homolog

The homologous protein (one that performs the same function) in yeast is Vacuolar protein sorting 29 homolog (S. cerevisiae).[6]

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.[7] 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.[8] Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000111237 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029462 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)".
7. 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.
8. 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. 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. 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. doi:10.1038/nature06216. PMC 2377034. PMID 17891154.