DET1_YEAST
ID DET1_YEAST Reviewed; 334 AA.
AC Q99288; D6VS38; P87337; Q05314; Q7LHX4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Broad-range acid phosphatase DET1;
DE EC=3.1.3.-;
DE AltName: Full=Decreased ergosterol transport protein 1;
GN Name=DET1; OrderedLocusNames=YDR051C; ORFNames=D4202;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
RX PubMed=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP 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).
RN [7]
RP FUNCTION.
RX PubMed=19060182; DOI=10.1128/ec.00135-08;
RA Sullivan D.P., Georgiev A., Menon A.K.;
RT "Tritium suicide selection identifies proteins involved in the uptake and
RT intracellular transport of sterols in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 8:161-169(2009).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=19753119; DOI=10.1371/journal.pone.0006993;
RA Ho C.K., Lam A.F., Symington L.S.;
RT "Identification of nucleases and phosphatases by direct biochemical screen
RT of the Saccharomyces cerevisiae proteome.";
RL PLoS ONE 4:E6993-E6993(2009).
CC -!- FUNCTION: Metal-independent, broad-range acid phosphatase. Involved,
CC either directly or indirectly, in the bidirectional transport of
CC sterols between the endoplasmic reticulum and the plasma membrane.
CC {ECO:0000269|PubMed:19060182, ECO:0000269|PubMed:19753119}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. Active from pH 4 to pH 5.5.
CC {ECO:0000269|PubMed:19753119};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
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DR EMBL; Z49209; CAA89081.1; -; Genomic_DNA.
DR EMBL; Z74347; CAA98868.1; -; Genomic_DNA.
DR EMBL; Z74348; CAA98870.1; -; Genomic_DNA.
DR EMBL; X84162; CAA58968.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11898.1; -; Genomic_DNA.
DR PIR; S54036; S54036.
DR RefSeq; NP_010336.3; NM_001180359.3.
DR AlphaFoldDB; Q99288; -.
DR BioGRID; 32105; 53.
DR DIP; DIP-1816N; -.
DR IntAct; Q99288; 9.
DR MINT; Q99288; -.
DR STRING; 4932.YDR051C; -.
DR iPTMnet; Q99288; -.
DR MaxQB; Q99288; -.
DR PaxDb; Q99288; -.
DR PRIDE; Q99288; -.
DR EnsemblFungi; YDR051C_mRNA; YDR051C; YDR051C.
DR GeneID; 851621; -.
DR KEGG; sce:YDR051C; -.
DR SGD; S000002458; DET1.
DR VEuPathDB; FungiDB:YDR051C; -.
DR eggNOG; ENOG502QQ8J; Eukaryota.
DR HOGENOM; CLU_033323_3_3_1; -.
DR InParanoid; Q99288; -.
DR OMA; RLFCMRW; -.
DR BioCyc; YEAST:G3O-29661-MON; -.
DR PRO; PR:Q99288; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q99288; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid transport; Nucleus; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..334
FT /note="Broad-range acid phosphatase DET1"
FT /id="PRO_0000244436"
FT ACT_SITE 32
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 334 AA; 39172 MW; D1F68EA851DBEDD0 CRC64;
MCEENVHVSE DVAGSHGSFT NARPRLIVLI RHGESESNKN KEVNGYIPNH LISLTKTGQI
QARQAGIDLL RVLNVDDHNL VEDLAKKYIK DESSRRTLPL KDYTRLSREK DTNIVFYTSP
YRRARETLKG ILDVIDEYNE LNSGVRICED MRYDPHGKQK HAFWPRGLNN TGGVYENNED
NICEGKPGKC YLQYRVKDEP RIREQDFGNF QKINSMQDVM KKRSTYGHFF FRFPHGESAA
DVYDRVASFQ ETLFRHFHDR QERRPRDVVV LVTHGIYSRV FLMKWFRWTY EEFESFTNVP
NGSVMVMELD ESINRYVLRT VLPKWTDCEG DLTT
