VPS25

VPS25
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ZME, 3CUQ, 3HTU
Identifiers
Aliases	VPS25 , DERP9, EAP20, FAP20, vacuolar protein sorting 25 homolog
External IDs	OMIM: 610907 MGI: 106354 HomoloGene: 6303 GeneCards: VPS25
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q21.2 Start 42,773,449 bp [1] End 42,779,599 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 D|11 64.48 cM Start 101,144,533 bp [2] End 101,150,375 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in rectum islet of Langerhans right uterine tube body of stomach smooth muscle tissue stromal cell of endometrium monocyte right lobe of liver body of pancreas minor salivary gland Top expressed in yolk sac lip superior frontal gyrus morula mirror proximal tubule spermatocyte neural tube thymus aortic valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein N-terminus binding structural molecule activity protein binding Cellular component cytoplasm cytosol endosome membrane nucleoplasm endosome membrane extracellular exosome nucleus ESCRT II complex Biological process regulation of transcription, DNA-templated multivesicular body assembly transcription, DNA-templated endosomal transport protein transport protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway macroautophagy negative regulation of epidermal growth factor-activated receptor activity transport multivesicular body sorting pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 84313 28084 Ensembl ENSG00000131475 ENSMUSG00000078656 UniProt Q9BRG1 Q9CQ80 RefSeq (mRNA) NM_032353 NM_001284411 NM_001284412 NM_001284414 NM_026776 RefSeq (protein) NP_115729 NP_115729.1 NP_001271340 NP_001271341 NP_001271343 NP_081052 Location (UCSC) Chr 17: 42.77 – 42.78 Mb Chr 11: 101.14 – 101.15 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

ESCRT-II complex subunit
crystal structure of subunit vps25 of the endosomal trafficking complex escrt-ii
Identifiers
Symbol	ESCRT-II
Pfam	PF05871
InterPro	IPR008570
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Vacuolar protein-sorting-associated protein 25 is a protein that in humans is encoded by the VPS25 gene. ^{[5] [6]}

It is a component of the endosome-associated complex ESCRT-II (Endosomal Sorting Complexes Required for Transport protein II). ESCRT (ESCRT-I, -II, -III) complexes orchestrate efficient sorting of ubiquitinated transmembrane receptors to lysosomes via multivesicular bodies (MVBs). ^[7] ESCRT-II recruits the transport machinery for protein sorting at MVB. ^[8] In addition, the human ESCRT-II has been shown to form a complex with RNA polymerase II elongation factor ELL in order to exert transcriptional control activity. ESCRT-II transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo. ^[9]

ESCRT-II is a trilobal complex composed of two copies of vps25, one copy of vps22 and the C-terminal region of vps36. The crystal structure of vps25 revealed two winged-helix domains, the N-terminal domain of vps25 interacting with vps22 and vps36. ^[10]

References

1. GRCh38: Ensembl release 89: ENSG00000131475 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000078656 - 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. Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y, Maki M (Mar 2005). "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting". Biochem J. 387 (Pt 1): 17–26. doi:10.1042/BJ20041227. PMC   1134928 . PMID   15511219.
6. "Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)".
7. Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL (January 2007). "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking". EMBO J. 26 (2): 600–12. doi:10.1038/sj.emboj.7601501. PMC   1783442 . PMID   17215868.
8. Teo H, Perisic O, Gonzalez B, Williams RL (October 2004). "ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes". Dev. Cell. 7 (4): 559–69. doi: 10.1016/j.devcel.2004.09.003 . PMID   15469844.
9. Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD (August 2002). "Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body". Dev. Cell. 3 (2): 283–9. doi: 10.1016/S1534-5807(02)00219-8 . PMID   12194858.
10. Wernimont AK, Weissenhorn W (December 2004). "Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II". BMC Struct. Biol. 4 (1): 10. doi:10.1186/1472-6807-4-10. PMC   539351 . PMID   15579210.

Further reading

• Kamura T, Burian D, Khalili H, et al. (2001). "Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a role for yeast EAP-like proteins in regulation of gene expression by glucose". J. Biol. Chem. 276 (19): 16528–33. doi: 10.1074/jbc.M010142200 . PMID   11278625.
• 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.
• von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi: 10.1016/S0092-8674(03)00714-1 . PMID   14505570. S2CID   16894972.
• Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. Bibcode:2003PNAS..10012414M. doi: 10.1073/pnas.2133846100 . PMC   218772 . PMID   14519844.
• Sharma M, Pampinella F, Nemes C, et al. (2004). "Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes". J. Cell Biol. 164 (6): 923–33. doi:10.1083/jcb.200312018. PMC   2172283 . PMID   15007060.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Bowers K, Piper SC, Edeling MA, et al. (2006). "Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII". J. Biol. Chem. 281 (8): 5094–105. doi: 10.1074/jbc.M508632200 . PMID   16371348.

This article incorporates text from the public domain Pfam and InterPro: IPR008570