Q04272 (VPS20_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein sorting-associated protein 20

Alternative name(s):
Amino acid sensor-independent protein 10
Charged multivesicular body protein 6
ESCRT-III complex subunit VPS20
Vacuolar protein-targeting protein 20

Gene names

Name:	VPS20
Synonyms:	ASI10, CHM6, VPT20
Ordered Locus Names:	YMR077C
ORF Names:	YM9582.02C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Required for the oligomerization of SNF7 into a membrane-associated filament. The VPS20-SNF7 subcomplex is responsible for the membrane association of the ESCRT-III complex. Also required for the RIM101 repressor proteolytic activation. Ref.4 Ref.5 Ref.6 Ref.7 Ref.11
Subunit structure	Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with the VPS4. Interacts with VPS25; the interaction mediates the association with the ESCRT-II complex. Ref.6 Ref.7 Ref.10 Ref.13
Subcellular location	Endosome membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein Ref.5 Ref.6 Ref.8.
Miscellaneous	Present with 937 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the SNF7 family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Membrane Vacuole
Domain	Coiled coil
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intralumenal vesicle formation Inferred from mutant phenotype. Source: SGD late endosome to vacuole transport Inferred from mutant phenotype. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred by curator. Source: SGD
Cellular component	ESCRT III complex Inferred from direct assay Ref.6. Source: SGD vacuolar membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VPS25	P47142	3	EBI-28157,EBI-25595
VPS4	P52917	6	EBI-28157,EBI-20475

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 221	220	Vacuolar protein sorting-associated protein 20		PRO_0000211515
Regions
	Coiled coil	72 – 178	107	Potential
Amino acid modifications
	Modified residue	43	1	Phosphoserine Ref.12
	Modified residue	184	1	Phosphoserine Ref.14
	Lipidation	2	1	N-myristoyl glycine Ref.3
Experimental info
	Mutagenesis	2	1	G → A: Loss of membrane association. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q04272 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CDC88BC4ADA3D602	FASTA	221	25,638
	10 20 30 40 50 60 MGQKSSKVHI TKTDRAILEV KRSKDEIHKF TRRTDNLILV EKSQLKDLIR KNPENYKSNM 70 80 90 100 110 120 KVRFLLKRIH YQEHLLQQAS DQLINLENMV STLEFKMVEK QFINGLKNGN EILKKLNKEF 130 140 150 160 170 180 SNVDELMDDV QDQIAYQNEI NETLSRSLVG TSNYEDDLDK ELDALESELN PEKMNNAKVA 190 200 210 220 NMPSTEGLPS LPQGEQTEQK EREEFATEER SDTKEPLALL S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase." Ashrafi K., Farazi T.A., Gordon J.I. J. Biol. Chem. 273:25864-25874(1998) [PubMed: 9748261] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[4]	"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins." Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M. J. Cell Sci. 114:2395-2404(2001) [PubMed: 11559748] [Abstract] Cited for: FUNCTION.
[5]	"A family of small coiled-coil-forming proteins functioning at the late endosome in yeast." Kranz A., Kinner A., Koelling R. Mol. Biol. Cell 12:711-723(2001) [PubMed: 11251082] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting." Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D. Dev. Cell 3:271-282(2002) [PubMed: 12194857] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS2; VPS24 AND SNF7, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
[7]	"Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae." Yeo S.C.L., Xu L., Ren J., Boulton V.J., Wagle M.D., Liu C., Ren G., Wong P., Zahn R., Sasajala P., Yang H., Piper R.C., Munn A.L. J. Cell Sci. 116:3957-3970(2003) [PubMed: 12953057] [Abstract] Cited for: FUNCTION, INTERACTION WITH VPS4.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes." Teo H., Perisic O., Gonzalez B., Williams R.L. Dev. Cell 7:559-569(2004) [PubMed: 15469844] [Abstract] Cited for: INTERACTION WITH VPS25.
[11]	"Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans." Xu W., Smith F.J. Jr., Subaran R., Mitchell A.P. Mol. Biol. Cell 15:5528-5537(2004) [PubMed: 15371534] [Abstract] Cited for: FUNCTION.
[12]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, MASS SPECTROMETRY. Strain: YAL6B.
[13]	"Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4." Xiao J., Xia H., Yoshino-Koh K., Zhou J., Xu Z. J. Mol. Biol. 374:655-670(2007) [PubMed: 17949747] [Abstract] Cited for: INTERACTION WITH VPS4.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49259 Genomic DNA. Translation: CAA89223.1. BK006946 Genomic DNA. Translation: DAA09975.1.
PIR	S54452.
RefSeq	NP_013794.1. NM_001182576.1.
3D structure databases
ProteinModelPortal	Q04272.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1961N.
IntAct	Q04272. 9 interactions.
MINT	MINT-390066.
STRING	Q04272.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR077C; YMR077C; YMR077C.
GeneID	855101.
KEGG	sce:YMR077C.
NMPDR	fig|4932.3.peg.4841.
Organism-specific databases
SGD	S000004682. VPS20.
Phylogenomic databases
eggNOG	fuNOG10753.
GeneTree	EFGT00050000003227.
HOGENOM	HBG592869.
OMA	QKRITQQ.
OrthoDB	EOG46DQCG.
Gene expression databases
ArrayExpress	Q04272.
Genevestigator	Q04272.
GermOnline	YMR077C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005024. Snf7. [Graphical view]
KO	K12195.
Pfam	PF03357. Snf7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978422.

Entry information

Entry name

VPS20_YEAST

Accession

Primary (citable) accession number: Q04272
Secondary accession number(s): D6VZQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program