VPS20_YEAST
ID VPS20_YEAST Reviewed; 221 AA.
AC Q04272; D6VZQ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Vacuolar protein sorting-associated protein 20;
DE AltName: Full=Amino acid sensor-independent protein 10;
DE AltName: Full=Charged multivesicular body protein 6;
DE AltName: Full=ESCRT-III complex subunit VPS20;
DE AltName: Full=Vacuolar protein-targeting protein 20;
GN Name=VPS20; Synonyms=ASI10, CHM6, VPT20; OrderedLocusNames=YMR077C;
GN ORFNames=YM9582.02C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=9748261; DOI=10.1074/jbc.273.40.25864;
RA Ashrafi K., Farazi T.A., Gordon J.I.;
RT "A role for Saccharomyces cerevisiae fatty acid activation protein 4 in
RT regulating protein N-myristoylation during entry into stationary phase.";
RL J. Biol. Chem. 273:25864-25874(1998).
RN [4]
RP FUNCTION.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11251082; DOI=10.1091/mbc.12.3.711;
RA Kranz A., Kinner A., Koelling R.;
RT "A family of small coiled-coil-forming proteins functioning at the late
RT endosome in yeast.";
RL Mol. Biol. Cell 12:711-723(2001).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS2;
RP VPS24 AND SNF7, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX PubMed=12194857; DOI=10.1016/s1534-5807(02)00220-4;
RA Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.;
RT "Escrt-III: an endosome-associated heterooligomeric protein complex
RT required for mvb sorting.";
RL Dev. Cell 3:271-282(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH VPS4.
RX PubMed=12953057; DOI=10.1242/jcs.00751;
RA Yeo S.C.L., Xu L., Ren J., Boulton V.J., Wagle M.D., Liu C., Ren G.,
RA Wong P., Zahn R., Sasajala P., Yang H., Piper R.C., Munn A.L.;
RT "Vps20p and Vta1p interact with Vps4p and function in multivesicular body
RT sorting and endosomal transport in Saccharomyces cerevisiae.";
RL J. Cell Sci. 116:3957-3970(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP INTERACTION WITH VPS25.
RX PubMed=15469844; DOI=10.1016/j.devcel.2004.09.003;
RA Teo H., Perisic O., Gonzalez B., Williams R.L.;
RT "ESCRT-II, an endosome-associated complex required for protein sorting:
RT crystal structure and interactions with ESCRT-III and membranes.";
RL Dev. Cell 7:559-569(2004).
RN [11]
RP FUNCTION.
RX PubMed=15371534; DOI=10.1091/mbc.e04-08-0666;
RA Xu W., Smith F.J. Jr., Subaran R., Mitchell A.P.;
RT "Multivesicular body-ESCRT components function in pH response regulation in
RT Saccharomyces cerevisiae and Candida albicans.";
RL Mol. Biol. Cell 15:5528-5537(2004).
RN [12]
RP INTERACTION WITH VPS4.
RX PubMed=17949747; DOI=10.1016/j.jmb.2007.09.067;
RA Xiao J., Xia H., Yoshino-Koh K., Zhou J., Xu Z.;
RT "Structural characterization of the ATPase reaction cycle of endosomal AAA
RT protein Vps4.";
RL J. Mol. Biol. 374:655-670(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Class E VPS protein implicated in concentration and sorting
CC of cargo proteins of the multivesicular body (MVB) for incorporation
CC into intralumenal vesicles. The lumenal sequestrated membrane proteins
CC will be targeted into the vacuole after fusion of the endosome with the
CC vacuole. Acts a component of the ESCRT-III complex, which appears to be
CC critical for late steps in MVB sorting, such as membrane invagination
CC and final cargo sorting and recruitment of late-acting components of
CC the sorting machinery. The MVB pathway requires the sequential function
CC of ESCRT-O, -I,-II and -III complex assemblies. Required for the
CC oligomerization of SNF7 into a membrane-associated filament. The VPS20-
CC SNF7 subcomplex is responsible for the membrane association of the
CC ESCRT-III complex. Also required for the RIM101 repressor proteolytic
CC activation. {ECO:0000269|PubMed:11251082, ECO:0000269|PubMed:11559748,
CC ECO:0000269|PubMed:12194857, ECO:0000269|PubMed:12953057,
CC ECO:0000269|PubMed:15371534}.
CC -!- SUBUNIT: Core component of the ESCRT-III complex (endosomal sorting
CC required for transport complex III). ESCRT-III appears to be
CC sequentially assembled as a flat lattice on the endosome membrane and
CC forms a transient 450 kDa complex that contains DID4, oligomerized
CC SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated
CC filament is nucleated by association of SNF7 with VPS20; the process is
CC terminated through association of VPS24, possibly by capping the SNF7
CC filament. VPS24 subsequently associates with DID4/VPS2. Interacts with
CC the VPS4. Interacts with VPS25; the interaction mediates the
CC association with the ESCRT-II complex. {ECO:0000269|PubMed:12194857,
CC ECO:0000269|PubMed:12953057, ECO:0000269|PubMed:15469844,
CC ECO:0000269|PubMed:17949747}.
CC -!- INTERACTION:
CC Q04272; P39929: SNF7; NbExp=5; IntAct=EBI-28157, EBI-17554;
CC Q04272; P47142: VPS25; NbExp=2; IntAct=EBI-28157, EBI-25595;
CC Q04272; P52917: VPS4; NbExp=6; IntAct=EBI-28157, EBI-20475;
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC Vacuole membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; Z49259; CAA89223.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09975.1; -; Genomic_DNA.
DR PIR; S54452; S54452.
DR RefSeq; NP_013794.1; NM_001182576.1.
DR PDB; 5FVL; X-ray; 1.97 A; C/D=170-195.
DR PDBsum; 5FVL; -.
DR AlphaFoldDB; Q04272; -.
DR SMR; Q04272; -.
DR BioGRID; 35253; 170.
DR ComplexPortal; CPX-1624; ESCRT-III complex.
DR DIP; DIP-1961N; -.
DR IntAct; Q04272; 8.
DR MINT; Q04272; -.
DR STRING; 4932.YMR077C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q04272; -.
DR MaxQB; Q04272; -.
DR PaxDb; Q04272; -.
DR PRIDE; Q04272; -.
DR EnsemblFungi; YMR077C_mRNA; YMR077C; YMR077C.
DR GeneID; 855101; -.
DR KEGG; sce:YMR077C; -.
DR SGD; S000004682; VPS20.
DR VEuPathDB; FungiDB:YMR077C; -.
DR eggNOG; KOG2910; Eukaryota.
DR HOGENOM; CLU_086201_2_0_1; -.
DR InParanoid; Q04272; -.
DR OMA; GTIEFKL; -.
DR BioCyc; YEAST:G3O-32779-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q04272; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04272; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000815; C:ESCRT III complex; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP:SGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endosome; Lipoprotein; Membrane; Myristate;
KW Protein transport; Reference proteome; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..221
FT /note="Vacuolar protein sorting-associated protein 20"
FT /id="PRO_0000211515"
FT REGION 170..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..178
FT /evidence="ECO:0000255"
FT COMPBIAS 177..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:9748261"
FT MUTAGEN 2
FT /note="G->A: Loss of membrane association."
FT /evidence="ECO:0000269|PubMed:12194857"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5FVL"
SQ 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
