DID2_YEAST
ID DID2_YEAST Reviewed; 204 AA.
AC P69771; D6VX98;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Vacuolar protein-sorting-associated protein 46;
DE AltName: Full=Charged multivesicular body protein 1;
DE AltName: Full=DOA4-independent degradation protein 2;
DE AltName: Full=Fifty two inhibitor 1;
GN Name=DID2; Synonyms=CHM1, FTI1, VPS46; OrderedLocusNames=YKR035W-A;
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=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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11029042; DOI=10.1091/mbc.11.10.3365;
RA Amerik A.Y., Nowak J., Swaminathan S., Hochstrasser M.;
RT "The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar
RT protein-sorting and endocytic pathways.";
RL Mol. Biol. Cell 11:3365-3380(2000).
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 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 [6]
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 [7]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH VPS4 AND VTA1.
RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
RA Stevens T.H.;
RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Traffic 5:194-210(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH VPS4 AND VPS24.
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 [9]
RP ERRATUM OF PUBMED:17130288.
RA Nickerson D.P., West M., Odorizzi G.;
RL J. Cell Biol. 175:1043-1043(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH VSP4 AND VTA1.
RX PubMed=16601096; DOI=10.1073/pnas.0601712103;
RA Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.;
RT "Vta1p and Vps46p regulate the membrane association and ATPase activity of
RT Vps4p at the yeast multivesicular body.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006).
RN [11]
RP INTERACTION WITH VSP4, AND MUTAGENESIS OF ARG-198; LEU-199 AND LEU-202.
RX PubMed=17928861; DOI=10.1038/nature06171;
RA Obita T., Saksena S., Ghazi-Tabatabai S., Gill D.J., Perisic O., Emr S.D.,
RA Williams R.L.;
RT "Structural basis for selective recognition of ESCRT-III by the AAA ATPase
RT Vps4.";
RL Nature 449:735-739(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH VTA1.
RX PubMed=18194652; DOI=10.1016/j.devcel.2007.10.021;
RA Azmi I.F., Davies B.A., Xiao J., Babst M., Xu Z., Katzmann D.J.;
RT "ESCRT-III family members stimulate Vps4 ATPase activity directly or via
RT Vta1.";
RL Dev. Cell 14:50-61(2008).
RN [13]
RP FUNCTION, AND INTERACTION WITH IST1.
RX PubMed=18032584; DOI=10.1091/mbc.e07-07-0694;
RA Rue S.M., Mattei S., Saksena S., Emr S.D.;
RT "Novel Ist1-Did2 complex functions at a late step in multivesicular body
RT sorting.";
RL Mol. Biol. Cell 19:475-484(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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. Probably acts as a peripherally associated component of the
CC ESCRT-III complex, which appears to be critical for late steps in MVB
CC sorting, such as membrane invagination and final cargo sorting and
CC recruits late-acting components of the sorting machinery. The MVB
CC pathway requires the sequential function of ESCRT-O, -I,-II and -III
CC complex assemblies. Regulates the membrane association of VPS4. Can
CC stimulate VPS4 ATPase activity directly or via VTA1.
CC {ECO:0000269|PubMed:11029042, ECO:0000269|PubMed:11559748,
CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:16601096,
CC ECO:0000269|PubMed:17130288, ECO:0000269|PubMed:18032584,
CC ECO:0000269|PubMed:18194652}.
CC -!- SUBUNIT: Self-associates. Interacts with VPS4 and VTA1. Interacts with
CC IST1. {ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:16601096,
CC ECO:0000269|PubMed:17130288, ECO:0000269|PubMed:17928861,
CC ECO:0000269|PubMed:18032584, ECO:0000269|PubMed:18194652}.
CC -!- INTERACTION:
CC P69771; P53843: IST1; NbExp=3; IntAct=EBI-2053489, EBI-28245;
CC P69771; P52917: VPS4; NbExp=3; IntAct=EBI-2053489, EBI-20475;
CC P69771; Q06263: VTA1; NbExp=3; IntAct=EBI-2053489, EBI-37098;
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 2440 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; Z28260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006944; DAA09188.1; -; Genomic_DNA.
DR RefSeq; NP_012961.3; NM_001184309.3.
DR PDB; 3GGZ; X-ray; 3.80 A; E/F/G/H=176-204.
DR PDB; 5H7P; NMR; -; B=176-204.
DR PDBsum; 3GGZ; -.
DR PDBsum; 5H7P; -.
DR AlphaFoldDB; P69771; -.
DR SMR; P69771; -.
DR BioGRID; 34166; 271.
DR DIP; DIP-52223N; -.
DR IntAct; P69771; 6.
DR MINT; P69771; -.
DR STRING; 4932.YKR035W-A; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P69771; -.
DR MaxQB; P69771; -.
DR PaxDb; P69771; -.
DR PRIDE; P69771; -.
DR EnsemblFungi; YKR035W-A_mRNA; YKR035W-A; YKR035W-A.
DR GeneID; 853906; -.
DR KEGG; sce:YKR035W-A; -.
DR SGD; S000006435; DID2.
DR VEuPathDB; FungiDB:YKR035W-A; -.
DR eggNOG; KOG3232; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_080826_0_0_1; -.
DR InParanoid; P69771; -.
DR BioCyc; YEAST:G3O-32071-MON; -.
DR EvolutionaryTrace; P69771; -.
DR PRO; PR:P69771; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P69771; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:1904902; P:ESCRT III complex assembly; IDA: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; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Vacuolar protein-sorting-associated protein 46"
FT /id="PRO_0000211461"
FT REGION 1..103
FT /note="Interaction with VSP24"
FT REGION 104..204
FT /note="Interaction with VSP4"
FT REGION 176..204
FT /note="Interaction with VTA1"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..56
FT /evidence="ECO:0000255"
FT COILED 109..129
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 198
FT /note="R->D: Impairs sorting."
FT /evidence="ECO:0000269|PubMed:17928861"
FT MUTAGEN 199
FT /note="L->D: Impairs sorting; when associated with D-202."
FT /evidence="ECO:0000269|PubMed:17928861"
FT MUTAGEN 202
FT /note="L->D: Impairs sorting; when associated with D-199."
FT /evidence="ECO:0000269|PubMed:17928861"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:5H7P"
SQ SEQUENCE 204 AA; 23091 MW; 70D1CF4588A8C6E6 CRC64;
MSRNSAAGLE NTLFQLKFTS KQLQKQANKA SKEEKQETNK LKRALNENED ISRIYASNAI
RKKNERLQLL KLASRVDSVA SRVQTAVTMR QVSASMGQVC KGMDKALQNM NLQQITMIMD
KFEQQFEDLD TSVNVYEDMG VNSDAMLVDN DKVDELMSKV ADENGMELKQ SAKLDNVPEI
KAKEVNVDDE KEDKLAQRLR ALRG
