VPS29: Difference between revisions

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{{Infobox_gene}}
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'''VPS29''' is a human [[gene]] coding for the vacuolar protein sorting [[protein]] Vps29, a component of the [[retromer]] complex.<ref name="pmid11062004">{{cite journal |vauthors=Edgar AJ, Polak JM | title = Human homologues of yeast vacuolar protein sorting 29 and 35 | journal = Biochem. Biophys. Res. Commun. | volume = 277 | issue = 3 | pages = 622–30 |date=November 2000 | pmid = 11062004 | doi = 10.1006/bbrc.2000.3727 | url = }}</ref>
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==Yeast homolog==
{{GNF_Protein_box
The homologous protein (one that performs the same function) in yeast is '''Vacuolar protein sorting 29 homolog (S. cerevisiae)'''.<ref name="entrez">{{cite web | title = Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51699| accessdate = }}</ref>
| image = PBB_Protein_VPS29_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1w24.
| PDB = {{PDB2|1w24}}, {{PDB2|1z2w}}, {{PDB2|1z2x}}
| Name = Vacuolar protein sorting 29 homolog (S. cerevisiae)
| HGNCid = 14340
| Symbol = VPS29
| AltSymbols =; DC15; DC7; DKFZp564F0223; FLJ20492; PEP11
| OMIM = 606932
| ECnumber = 
| Homologene = 9433
| MGIid = 1928344
| Function =
| Component = {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51699
    | Hs_Ensembl = ENSG00000111237
    | Hs_RefseqProtein = NP_057310
    | Hs_RefseqmRNA = NM_016226
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 109414117
    | Hs_GenLoc_end = 109421734
    | Hs_Uniprot = Q9UBQ0
    | Mm_EntrezGene = 56433
    | Mm_Ensembl = ENSMUSG00000029462
    | Mm_RefseqmRNA = NM_019780
    | Mm_RefseqProtein = NP_062754
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 122620630
    | Mm_GenLoc_end = 122623539
    | Mm_Uniprot = Q9QZ88
  }}
}}
'''Vacuolar protein sorting 29 homolog (S. cerevisiae)''', also known as '''VPS29''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51699| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Function==
{{PBB_Summary
VPS29 belongs to a group of genes coding for vacuolar protein sorting (VPS) proteins that, when functionally impaired, disrupt the efficient delivery of [[vacuole|vacuolar]] [[hydrolase]]s.<ref name="pmid11102511">{{cite journal |vauthors=Haft CR, de la Luz Sierra M, Bafford R, Lesniak MA, Barr VA, Taylor SI | title = Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes | journal = Mol. Biol. Cell | volume = 11 | issue = 12 | pages = 4105–16 |date=December 2000 | pmid = 11102511 | pmc = 15060 | doi = 10.1091/mbc.11.12.4105| url = http://www.molbiolcell.org/cgi/pmidlookup?view=long&pmid=11102511 }}</ref> 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 [[Golgi apparatus|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.<ref name="pmid18472259">{{cite journal |vauthors=Bonifacino JS, Hurley JH | title = Retromer | journal = Curr. Opin. Cell Biol. | volume = 20 | issue = 4 | pages = 427–36 |date=August 2008 | pmid = 18472259 | doi = 10.1016/j.ceb.2008.03.009 | url = | pmc = 2833274 }}</ref> [[Alternative splicing|Alternative splice]] variants encoding different isoforms, and usage of multiple [[polyadenylation]] sites have been found for this gene.<ref name="entrez" />
| section_title =  
| summary_text = This gene belongs to a group of vacuolar protein sorting (VPS) genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene 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. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51699| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Seaman MN, McCaffery JM, Emr SD |title=A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. |journal=J. Cell Biol. |volume=142 |issue= 3 |pages= 665-81 |year= 1998 |pmid= 9700157 |doi=  }}
*{{cite journal  |vauthors=Seaman MN, McCaffery JM, Emr SD |title=A Membrane Coat Complex Essential for Endosome-to-Golgi Retrograde Transport in Yeast |journal=J. Cell Biol. |volume=142 |issue= 3 |pages= 665–81 |year= 1998 |pmid= 9700157 |doi=10.1083/jcb.142.3.665  | pmc=2148169 }}
*{{cite journal  | author=Edgar AJ, Polak JM |title=Human homologues of yeast vacuolar protein sorting 29 and 35. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 3 |pages= 622-30 |year= 2000 |pmid= 11062004 |doi= 10.1006/bbrc.2000.3727 }}
*{{cite journal  |vauthors=Edgar AJ, Polak JM |title=Human homologues of yeast vacuolar protein sorting 29 and 35 |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 3 |pages= 622–30 |year= 2000 |pmid= 11062004 |doi= 10.1006/bbrc.2000.3727 }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Haft CR, de la Luz Sierra M, Bafford R, ''et al.'' |title=Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. |journal=Mol. Biol. Cell |volume=11 |issue= 12 |pages= 4105-16 |year= 2001 |pmid= 11102511 |doi=  }}
*{{cite journal  | author=Haft CR |title=Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes |journal=Mol. Biol. Cell |volume=11 |issue= 12 |pages= 4105–16 |year= 2001 |pmid= 11102511 |doi=  10.1091/mbc.11.12.4105| pmc=15060 |name-list-format=vanc| author2=de la Luz Sierra M  | author3=Bafford R | display-authors=3  | last4=Lesniak  | first4=MA  | last5=Barr  | first5=VA  | last6=Taylor  | first6=SI  }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | author=Wiemann S |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072  |name-list-format=vanc| author2=Weil B | author3=Wellenreuther R  | display-authors=3  | last4=Gassenhuber  | first4=J  | last5=Glassl  | first5=S | last6=Ansorge  | first6=W  | last7=Böcher  | first7=M  | last8=Blöcker  | first8=H  | last9=Bauersachs  | first9=S }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | author=Simpson JC |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732  |name-list-format=vanc| author2=Wellenreuther R  | author3=Poustka A  | display-authors=3  | last4=Pepperkok  | first4=R  | last5=Wiemann  | first5=S }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Vergés M, Luton F, Gruber C, ''et al.'' |title=The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor. |journal=Nat. Cell Biol. |volume=6 |issue= 8 |pages= 763-9 |year= 2004 |pmid= 15247922 |doi= 10.1038/ncb1153 }}
*{{cite journal  | author=Vergés M |title=The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor |journal=Nat. Cell Biol. |volume=6 |issue= 8 |pages= 763–9 |year= 2004 |pmid= 15247922 |doi= 10.1038/ncb1153  |name-list-format=vanc| author2=Luton F  | author3=Gruber C  | display-authors=3  | last4=Tiemann  | first4=Frank  | last5=Reinders  | first5=Lorri G.  | last6=Huang  | first6=Lan  | last7=Burlingame  | first7=Alma L. | last8=Haft  | first8=Carol R.  | last9=Mostov  | first9=Keith E. }}
*{{cite journal | author=Mingot JM, Bohnsack MT, Jäkle U, Görlich D |title=Exportin 7 defines a novel general nuclear export pathway. |journal=EMBO J. |volume=23 |issue= 16 |pages= 3227-36 |year= 2005 |pmid= 15282546 |doi= 10.1038/sj.emboj.7600338 }}
*{{cite journal  |vauthors=Mingot JM, Bohnsack MT, Jäkle U, Görlich D |title=Exportin 7 defines a novel general nuclear export pathway |journal=EMBO J. |volume=23 |issue= 16 |pages= 3227–36 |year= 2005 |pmid= 15282546 |doi= 10.1038/sj.emboj.7600338  | pmc=514512 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Wiemann S |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704  | pmc=528930  |name-list-format=vanc| author2=Arlt D  | author3=Huber W  | display-authors=3  | last4=Wellenreuther  | first4=R  | last5=Schleeger  | first5=S  | last6=Mehrle  | first6=A  | last7=Bechtel  | first7=S  | last8=Sauermann  | first8=M  | last9=Korf  | first9=U }}
*{{cite journal | author=Wang D, Guo M, Liang Z, ''et al.'' |title=Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 22962-7 |year= 2005 |pmid= 15788412 |doi= 10.1074/jbc.M500464200 }}
*{{cite journal  | author=Wang D |title=Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 22962–7 |year= 2005 |pmid= 15788412 |doi= 10.1074/jbc.M500464200  |name-list-format=vanc| author2=Guo M  | author3=Liang Z  | display-authors=3  | last4=Fan  | first4=J  | last5=Zhu  | first5=Z  | last6=Zang  | first6=J  | last7=Zhu  | first7=Z  | last8=Li  | first8=X  | last9=Teng  | first9=M }}
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
*{{cite journal  | author=Mehrle A |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139  | pmc=1347501  |name-list-format=vanc| author2=Rosenfelder H  | author3=Schupp I  | display-authors=3  | last4=Del Val  | first4=C  | last5=Arlt  | first5=D  | last6=Hahne  | first6=F  | last7=Bechtel  | first7=S  | last8=Simpson  | first8=J  | last9=Hofmann  | first9=O }}
*{{cite journal | author=Damen E, Krieger E, Nielsen JE, ''et al.'' |title=The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide. |journal=Biochem. J. |volume=398 |issue= 3 |pages= 399-409 |year= 2006 |pmid= 16737443 |doi= 10.1042/BJ20060033 }}
*{{cite journal  | author=Damen E |title=The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide |journal=Biochem. J. |volume=398 |issue= 3 |pages= 399–409 |year= 2006 |pmid= 16737443 |doi= 10.1042/BJ20060033  | pmc=1559457  |name-list-format=vanc| author2=Krieger E  | author3=Nielsen JE  | display-authors=3  | last4=Eygensteyn  | first4=Jelle  | last5=Van Leeuwen  | first5=Jeroen E. M. }}
*{{cite journal  | author=Rojas R, Kametaka S, Haft CR, Bonifacino JS |title=Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. |journal=Mol. Cell. Biol. |volume=27 |issue= 3 |pages= 1112-24 |year= 2007 |pmid= 17101778 |doi= 10.1128/MCB.00156-06 }}
*{{cite journal  |vauthors=Rojas R, Kametaka S, Haft CR, Bonifacino JS |title=Interchangeable but Essential Functions of SNX1 and SNX2 in the Association of Retromer with Endosomes and the Trafficking of Mannose 6-Phosphate Receptors |journal=Mol. Cell. Biol. |volume=27 |issue= 3 |pages= 1112–24 |year= 2007 |pmid= 17101778 |doi= 10.1128/MCB.00156-06  | pmc=1800681 }}
*{{cite journal  | author=Hierro A, Rojas AL, Rojas R, ''et al.'' |title=Functional architecture of the retromer cargo-recognition complex. |journal=Nature |volume=449 |issue= 7165 |pages= 1063-7 |year= 2007 |pmid= 17891154 |doi= 10.1038/nature06216 }}
*{{cite journal  | author=Hierro A |title=Functional architecture of the retromer cargo-recognition complex |journal=Nature |volume=449 |issue= 7165 |pages= 1063–7 |year= 2007 |pmid= 17891154 |doi= 10.1038/nature06216 | pmc=2377034  |name-list-format=vanc| author2=Rojas AL  | author3=Rojas R  | display-authors=3  | last4=Murthy  | first4=Namita  | last5=Effantin  | first5=Grégory  | last6=Kajava  | first6=Andrey V.  | last7=Steven  | first7=Alasdair C.  | last8=Bonifacino  | first8=Juan S.  | last9=Hurley  | first9=James H. }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=51699}}
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Latest revision as of 15:39, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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. ↑ 2.0 2.1 "Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)".
  3. ↑ 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.
  4. ↑ 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



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