VPS24_YEAST
ID VPS24_YEAST Reviewed; 224 AA.
AC P36095; D6VXP5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Vacuolar protein-sorting-associated protein 24;
DE AltName: Full=DOA4-independent degradation protein 3;
DE AltName: Full=ESCRT-III complex subunit VPS24;
GN Name=VPS24; Synonyms=DID3; OrderedLocusNames=YKL041W; ORFNames=YKL254;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154189; DOI=10.1002/yea.320091212;
RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome
RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a
RT new gene encoding a putative histone and seven new open reading frames.";
RL Yeast 9:1379-1384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9606181; DOI=10.1093/emboj/17.11.2982;
RA Babst M., Wendland B., Estepa E.J., Emr S.D.;
RT "The Vps4p AAA ATPase regulates membrane association of a Vps protein
RT complex required for normal endosome function.";
RL EMBO J. 17:2982-2993(1998).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS2;
RP VPS20; SNF7 AND VPS4, AND SUBCELLULAR LOCATION.
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 [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 DID2.
RX PubMed=17130288; DOI=10.1083/jcb.200606113;
RA Nickerson D.P., West M., Odorizzi G.;
RT "Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes.";
RL J. Cell Biol. 175:715-720(2006).
RN [11]
RP ERRATUM OF PUBMED:17130288.
RA Nickerson D.P., West M., Odorizzi G.;
RL J. Cell Biol. 175:1043-1043(2006).
RN [12]
RP ASSEMBLY OF THE ESCRT-III COMPLEX.
RX PubMed=18854142; DOI=10.1016/j.devcel.2008.08.013;
RA Teis D., Saksena S., Emr S.D.;
RT "Ordered assembly of the ESCRT-III complex on endosomes is required to
RT sequester cargo during MVB formation.";
RL Dev. Cell 15:578-589(2008).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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 oflate-acting components of the
CC sorting machinery. The MVB pathway requires the sequential function of
CC ESCRT-O, -I,-II and -III complex assemblies. The DID4/VPS2-VPS24
CC subcomplex is required for the VPS4-dependent dissociation of ESCRT-
CC III. {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:12194857,
CC ECO:0000269|PubMed:9606181}.
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 DID2. {ECO:0000269|PubMed:12194857,
CC ECO:0000269|PubMed:17130288}.
CC -!- INTERACTION:
CC P36095; P36095: VPS24; NbExp=3; IntAct=EBI-26653, EBI-26653;
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein.
CC Endomembrane system; Peripheral membrane protein. Note=Endosomal and
CC other punctate structures.
CC -!- MISCELLANEOUS: Present with 1890 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; X71621; CAA50631.1; -; Genomic_DNA.
DR EMBL; Z28041; CAA81876.1; -; Genomic_DNA.
DR EMBL; AY557901; AAS56227.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09115.1; -; Genomic_DNA.
DR PIR; S37862; S37862.
DR RefSeq; NP_012883.1; NM_001179607.1.
DR PDB; 6ZH3; EM; 3.20 A; A/B/C/D=1-224.
DR PDBsum; 6ZH3; -.
DR AlphaFoldDB; P36095; -.
DR SMR; P36095; -.
DR BioGRID; 34091; 709.
DR ComplexPortal; CPX-1624; ESCRT-III complex.
DR DIP; DIP-7295N; -.
DR IntAct; P36095; 6.
DR MINT; P36095; -.
DR STRING; 4932.YKL041W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P36095; -.
DR MaxQB; P36095; -.
DR PaxDb; P36095; -.
DR PRIDE; P36095; -.
DR EnsemblFungi; YKL041W_mRNA; YKL041W; YKL041W.
DR GeneID; 853825; -.
DR KEGG; sce:YKL041W; -.
DR SGD; S000001524; VPS24.
DR VEuPathDB; FungiDB:YKL041W; -.
DR eggNOG; KOG3229; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_0_2_1; -.
DR InParanoid; P36095; -.
DR OMA; INEMMDD; -.
DR BioCyc; YEAST:G3O-31842-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:P36095; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36095; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000815; C:ESCRT III complex; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
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:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Isopeptide bond; Membrane; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..224
FT /note="Vacuolar protein-sorting-associated protein 24"
FT /id="PRO_0000211487"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 13..55
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 58..97
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6ZH3"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:6ZH3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6ZH3"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:6ZH3"
SQ SEQUENCE 224 AA; 26242 MW; 6073C1B680D58E98 CRC64;
MDYIKKAIWG PDPKEQQRRI RSVLRKNGRN IEKSLRELTV LQNKTQQLIK KSAKKNDVRT
VRLYAKELYQ INKQYDRMYT SRAQLDSVRM KIDEAIRMNT LSNQMADSAG LMREVNSLVR
LPQLRNTMIE LEKELMKSGI ISEMVDDTME SVGDVGEEMD EAVDEEVNKI VEQYTNEKFK
NVDQVPTVEL AANEEEQEIP DEKVDEEADR MVNEMRERLR ALQN
