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Vacuolar protein sorting-associated protein 20 (Amino acid sensor-independent protein 10) (Charged multivesicular body protein 6) (ESCRT-III complex subunit VPS20) (Vacuolar protein-targeting protein 20)

 VPS20_YEAST             Reviewed;         221 AA.
Q04272; D6VZQ1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 146.
RecName: Full=Vacuolar protein sorting-associated protein 20;
AltName: Full=Amino acid sensor-independent protein 10;
AltName: Full=Charged multivesicular body protein 6;
AltName: Full=ESCRT-III complex subunit VPS20;
AltName: Full=Vacuolar protein-targeting protein 20;
Name=VPS20; Synonyms=ASI10, CHM6, VPT20; OrderedLocusNames=YMR077C;
ORFNames=YM9582.02C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
MYRISTOYLATION AT GLY-2.
PubMed=9748261; DOI=10.1074/jbc.273.40.25864;
Ashrafi K., Farazi T.A., Gordon J.I.;
"A role for Saccharomyces cerevisiae fatty acid activation protein 4
in regulating protein N-myristoylation during entry into stationary
phase.";
J. Biol. Chem. 273:25864-25874(1998).
[4]
FUNCTION.
PubMed=11559748;
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
"CHMP1 functions as a member of a newly defined family of vesicle
trafficking proteins.";
J. Cell Sci. 114:2395-2404(2001).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11251082; DOI=10.1091/mbc.12.3.711;
Kranz A., Kinner A., Koelling R.;
"A family of small coiled-coil-forming proteins functioning at the
late endosome in yeast.";
Mol. Biol. Cell 12:711-723(2001).
[6]
FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH
VPS2; VPS24 AND SNF7, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
PubMed=12194857; DOI=10.1016/S1534-5807(02)00220-4;
Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.;
"Escrt-III: an endosome-associated heterooligomeric protein complex
required for mvb sorting.";
Dev. Cell 3:271-282(2002).
[7]
FUNCTION, AND INTERACTION WITH VPS4.
PubMed=12953057; DOI=10.1242/jcs.00751;
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.;
"Vps20p and Vta1p interact with Vps4p and function in multivesicular
body sorting and endosomal transport in Saccharomyces cerevisiae.";
J. Cell Sci. 116:3957-3970(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
INTERACTION WITH VPS25.
PubMed=15469844; DOI=10.1016/j.devcel.2004.09.003;
Teo H., Perisic O., Gonzalez B., Williams R.L.;
"ESCRT-II, an endosome-associated complex required for protein
sorting: crystal structure and interactions with ESCRT-III and
membranes.";
Dev. Cell 7:559-569(2004).
[11]
FUNCTION.
PubMed=15371534; DOI=10.1091/mbc.E04-08-0666;
Xu W., Smith F.J. Jr., Subaran R., Mitchell A.P.;
"Multivesicular body-ESCRT components function in pH response
regulation in Saccharomyces cerevisiae and Candida albicans.";
Mol. Biol. Cell 15:5528-5537(2004).
[12]
INTERACTION WITH VPS4.
PubMed=17949747; DOI=10.1016/j.jmb.2007.09.067;
Xiao J., Xia H., Yoshino-Koh K., Zhou J., Xu Z.;
"Structural characterization of the ATPase reaction cycle of endosomal
AAA protein Vps4.";
J. Mol. Biol. 374:655-670(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- 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. {ECO:0000269|PubMed:11251082,
ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:12194857,
ECO:0000269|PubMed:12953057, ECO:0000269|PubMed:15371534}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:12194857,
ECO:0000269|PubMed:12953057, ECO:0000269|PubMed:15469844,
ECO:0000269|PubMed:17949747}.
-!- INTERACTION:
P39929:SNF7; NbExp=5; IntAct=EBI-28157, EBI-17554;
Q96H20:SNF8 (xeno); NbExp=3; IntAct=EBI-28157, EBI-747719;
P47142:VPS25; NbExp=2; IntAct=EBI-28157, EBI-25595;
P52917:VPS4; NbExp=6; IntAct=EBI-28157, EBI-20475;
-!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane
protein. Vacuole membrane; Peripheral membrane protein.
-!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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EMBL; Z49259; CAA89223.1; -; Genomic_DNA.
EMBL; BK006946; DAA09975.1; -; Genomic_DNA.
PIR; S54452; S54452.
RefSeq; NP_013794.1; NM_001182576.1.
PDB; 5FVL; X-ray; 1.97 A; C/D=170-195.
PDBsum; 5FVL; -.
ProteinModelPortal; Q04272; -.
SMR; Q04272; -.
BioGrid; 35253; 164.
DIP; DIP-1961N; -.
IntAct; Q04272; 9.
MINT; Q04272; -.
STRING; 4932.YMR077C; -.
iPTMnet; Q04272; -.
MaxQB; Q04272; -.
PaxDb; Q04272; -.
PRIDE; Q04272; -.
EnsemblFungi; YMR077C; YMR077C; YMR077C.
GeneID; 855101; -.
KEGG; sce:YMR077C; -.
EuPathDB; FungiDB:YMR077C; -.
SGD; S000004682; VPS20.
GeneTree; ENSGT00720000108863; -.
HOGENOM; HOG000208642; -.
InParanoid; Q04272; -.
KO; K12195; -.
OMA; YQKRITQ; -.
OrthoDB; EOG092C4MFS; -.
BioCyc; YEAST:G3O-32779-MONOMER; -.
Reactome; R-SCE-1632852; Macroautophagy.
PRO; PR:Q04272; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000815; C:ESCRT III complex; IDA:SGD.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:1904669; P:ATP export; IMP:SGD.
GO; GO:0070676; P:intralumenal vesicle formation; IMP:SGD.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:SGD.
InterPro; IPR005024; Snf7_fam.
Pfam; PF03357; Snf7; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Endosome; Lipoprotein;
Membrane; Myristate; Protein transport; Reference proteome; Transport;
Vacuole.
INIT_MET 1 1 Removed.
CHAIN 2 221 Vacuolar protein sorting-associated
protein 20.
/FTId=PRO_0000211515.
COILED 72 178 {ECO:0000255}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:9748261}.
MUTAGEN 2 2 G->A: Loss of membrane association.
{ECO:0000269|PubMed:12194857}.
HELIX 171 180 {ECO:0000244|PDB:5FVL}.
SEQUENCE 221 AA; 25638 MW; CDC88BC4ADA3D602 CRC64;
MGQKSSKVHI TKTDRAILEV KRSKDEIHKF TRRTDNLILV EKSQLKDLIR KNPENYKSNM
KVRFLLKRIH YQEHLLQQAS DQLINLENMV STLEFKMVEK QFINGLKNGN EILKKLNKEF
SNVDELMDDV QDQIAYQNEI NETLSRSLVG TSNYEDDLDK ELDALESELN PEKMNNAKVA
NMPSTEGLPS LPQGEQTEQK EREEFATEER SDTKEPLALL S


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