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Reviewed, UniProtKB/Swiss-Prot P69771 (DID2_YEAST)

Last modified December 15, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vacuolar protein-sorting-associated protein 46
Alternative name(s):
    Charged multivesicular body protein 1
    DOA4-independent degradation protein 2
    Fifty two inhibitor 1
Gene names
Name: DID2
Synonyms: CHM1, FTI1, VPS46
Ordered Locus Names: YKR035W-A
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. Probably acts as a peripherally asocciated 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 recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1. Ref.2 Ref.3 Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Subunit structure

Self-associates. Interacts with VPS4 and VTA1. Interacts with IST1. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12 Ref.10

Subcellular location

Endosome membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Note: Endosomal and other punctate structures. Ref.2 Ref.4

Miscellaneous

Present with 2440 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the SNF7 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Vacuolar protein-sorting-associated protein 46
PRO_0000211461

Regions

Region1 – 103103Interaction with VSP24
Region104 – 204101Interaction with VSP4
Region176 – 20429Interaction with VTA1
Coiled coil9 – 5648 Potential
Coiled coil109 – 12921 Potential

Experimental info

Mutagenesis1981R → D: Impairs sorting. Ref.10
Mutagenesis1991L → D: Impairs sorting; when associated with D-202. Ref.10
Mutagenesis2021L → D: Impairs sorting; when associated with D-199. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P69771-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 70D1CF4588A8C6E6

FASTA20423,091
        10         20         30         40         50         60 
MSRNSAAGLE NTLFQLKFTS KQLQKQANKA SKEEKQETNK LKRALNENED ISRIYASNAI 

        70         80         90        100        110        120 
RKKNERLQLL KLASRVDSVA SRVQTAVTMR QVSASMGQVC KGMDKALQNM NLQQITMIMD 

       130        140        150        160        170        180 
KFEQQFEDLD TSVNVYEDMG VNSDAMLVDN DKVDELMSKV ADENGMELKQ SAKLDNVPEI 

       190        200 
KAKEVNVDDE KEDKLAQRLR ALRG 

« Hide

References

« Hide 'large scale' references
[1]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways."
Amerik A.Y., Nowak J., Swaminathan S., Hochstrasser M.
Mol. Biol. Cell 11:3365-3380(2000) [PubMed: 11029042] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[3]"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.
[4]"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].
[5]"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].
[6]"Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
Traffic 5:194-210(2004) [PubMed: 15086794] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH VPS4 AND VTA1.
[7]"Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes."
Nickerson D.P., West M., Odorizzi G.
J. Cell Biol. 175:715-720(2006) [PubMed: 17130288] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS4 AND VPS24.
[8]Erratum
Nickerson D.P., West M., Odorizzi G.
J. Cell Biol. 175:1043-1043(2006)
[9]"Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body."
Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.
Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006) [PubMed: 16601096] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VSP4 AND VTA1.
[10]"Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4."
Obita T., Saksena S., Ghazi-Tabatabai S., Gill D.J., Perisic O., Emr S.D., Williams R.L.
Nature 449:735-739(2007) [PubMed: 17928861] [Abstract]
Cited for: INTERACTION WITH VSP4, MUTAGENESIS OF ARG-198; LEU-199 AND LEU-202.
[11]"ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1."
Azmi I.F., Davies B.A., Xiao J., Babst M., Xu Z., Katzmann D.J.
Dev. Cell 14:50-61(2008) [PubMed: 18194652] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VTA1.
[12]"Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting."
Rue S.M., Mattei S., Saksena S., Emr S.D.
Mol. Biol. Cell 19:475-484(2008) [PubMed: 18032584] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IST1.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z28260 Genomic DNA. No translation available.
RefSeqNP_012961.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3GGZX-ray3.80E/F/G/H176-204[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP69771. 5 interactions.
STRINGP69771.

Genome annotation databases

EnsemblYKR035W-A; YKR035W-A; YKR035W-A; Saccharomyces cerevisiae. [Genome view]
GeneID853906.
KEGGsce:YKR035W-A.
NMPDRfig|4932.3.peg.3947.

Organism-specific databases

CYGDYKR035w-a.
SGDS000006435. DID2.

Phylogenomic databases

HOGENOMHBG379179.
OMAMDLQKVS.
OrthoDBEOG91ZGT6.

Gene expression databases

ArrayExpressP69771.
GenevestigatorP69771.
GermOnlineYKR035W-A. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio975236.

Entry information

Entry nameDID2_YEAST
AccessionPrimary (citable) accession number: P69771
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: December 15, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents