Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Broad-range acid phosphatase DET1

Gene

DET1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Metal-independent, broad-range acid phosphatase. Involved, either directly or indirectly, in the bidirectional transport of sterols between the endoplasmic reticulum and the plasma membrane.2 Publications

pH dependencei

Optimum pH is 4.5. Active from pH 4 to pH 5.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321Tele-phosphohistidine intermediateBy similarity
Binding sitei38 – 381SubstrateBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Active sitei126 – 1261Proton donor/acceptorBy similarity

GO - Molecular functioni

  • acid phosphatase activity Source: SGD

GO - Biological processi

  • dephosphorylation Source: SGD
  • intracellular sterol transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29661-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Broad-range acid phosphatase DET1 (EC:3.1.3.-)
Alternative name(s):
Decreased ergosterol transport protein 1
Gene namesi
Name:DET1
Ordered Locus Names:YDR051C
ORF Names:D4202
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR051C.
SGDiS000002458. DET1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Broad-range acid phosphatase DET1PRO_0000244436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99288.
PeptideAtlasiQ99288.

PTM databases

iPTMnetiQ99288.

Interactioni

Protein-protein interaction databases

BioGridi32105. 14 interactions.
DIPiDIP-1816N.
IntActiQ99288. 9 interactions.
MINTiMINT-395648.

Structurei

3D structure databases

ProteinModelPortaliQ99288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 452Substrate bindingBy similarity
Regioni168 – 1714Substrate bindingBy similarity
Regioni195 – 20511Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

HOGENOMiHOG000221683.
InParanoidiQ99288.
OMAiEFESFTN.
OrthoDBiEOG7S7SPZ.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCEENVHVSE DVAGSHGSFT NARPRLIVLI RHGESESNKN KEVNGYIPNH
60 70 80 90 100
LISLTKTGQI QARQAGIDLL RVLNVDDHNL VEDLAKKYIK DESSRRTLPL
110 120 130 140 150
KDYTRLSREK DTNIVFYTSP YRRARETLKG ILDVIDEYNE LNSGVRICED
160 170 180 190 200
MRYDPHGKQK HAFWPRGLNN TGGVYENNED NICEGKPGKC YLQYRVKDEP
210 220 230 240 250
RIREQDFGNF QKINSMQDVM KKRSTYGHFF FRFPHGESAA DVYDRVASFQ
260 270 280 290 300
ETLFRHFHDR QERRPRDVVV LVTHGIYSRV FLMKWFRWTY EEFESFTNVP
310 320 330
NGSVMVMELD ESINRYVLRT VLPKWTDCEG DLTT
Length:334
Mass (Da):39,172
Last modified:November 1, 1996 - v1
Checksum:iD1F68EA851DBEDD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49209 Genomic DNA. Translation: CAA89081.1.
Z74347 Genomic DNA. Translation: CAA98868.1.
Z74348 Genomic DNA. Translation: CAA98870.1.
X84162 Genomic DNA. Translation: CAA58968.1.
BK006938 Genomic DNA. Translation: DAA11898.1.
PIRiS54036.
RefSeqiNP_010336.3. NM_001180359.3.

Genome annotation databases

EnsemblFungiiYDR051C; YDR051C; YDR051C.
GeneIDi851621.
KEGGisce:YDR051C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49209 Genomic DNA. Translation: CAA89081.1.
Z74347 Genomic DNA. Translation: CAA98868.1.
Z74348 Genomic DNA. Translation: CAA98870.1.
X84162 Genomic DNA. Translation: CAA58968.1.
BK006938 Genomic DNA. Translation: DAA11898.1.
PIRiS54036.
RefSeqiNP_010336.3. NM_001180359.3.

3D structure databases

ProteinModelPortaliQ99288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32105. 14 interactions.
DIPiDIP-1816N.
IntActiQ99288. 9 interactions.
MINTiMINT-395648.

PTM databases

iPTMnetiQ99288.

Proteomic databases

MaxQBiQ99288.
PeptideAtlasiQ99288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR051C; YDR051C; YDR051C.
GeneIDi851621.
KEGGisce:YDR051C.

Organism-specific databases

EuPathDBiFungiDB:YDR051C.
SGDiS000002458. DET1.

Phylogenomic databases

HOGENOMiHOG000221683.
InParanoidiQ99288.
OMAiEFESFTN.
OrthoDBiEOG7S7SPZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29661-MONOMER.

Miscellaneous databases

NextBioi969154.
PROiQ99288.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV."
    Brandt P., Ramlow S., Otto B., Bloecker H.
    Yeast 12:85-90(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Tritium suicide selection identifies proteins involved in the uptake and intracellular transport of sterols in Saccharomyces cerevisiae."
    Sullivan D.P., Georgiev A., Menon A.K.
    Eukaryot. Cell 8:161-169(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Identification of nucleases and phosphatases by direct biochemical screen of the Saccharomyces cerevisiae proteome."
    Ho C.K., Lam A.F., Symington L.S.
    PLoS ONE 4:E6993-E6993(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiDET1_YEAST
AccessioniPrimary (citable) accession number: Q99288
Secondary accession number(s): D6VS38
, P87337, Q05314, Q7LHX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3170 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.