PPAL_YEAST
ID PPAL_YEAST Reviewed; 161 AA.
AC P40347; D6W477;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase {ECO:0000303|PubMed:7629177};
DE Short=PTPase {ECO:0000303|PubMed:7629177};
DE EC=3.1.3.48 {ECO:0000269|PubMed:7629177};
DE AltName: Full=Low molecular weight cytosolic acid phosphatase {ECO:0000303|PubMed:7629177};
DE EC=3.1.3.2 {ECO:0000269|PubMed:7629177};
GN Name=LTP1 {ECO:0000303|PubMed:7629177}; OrderedLocusNames=YPR073C;
GN ORFNames=YP9499.28C;
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 / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Y133;
RX PubMed=7629177; DOI=10.1074/jbc.270.31.18491;
RA Ostanin K., Pokalsky C., Wang S., van Etten R.L.;
RT "Cloning and characterization of a Saccharomyces cerevisiae gene encoding
RT the low molecular weight protein-tyrosine phosphatase.";
RL J. Biol. Chem. 270:18491-18499(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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-57, 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] {ECO:0007744|PDB:1D2A}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-161.
RX PubMed=10684601; DOI=10.1021/bi991515+;
RA Wang S., Stauffacher C.V., Van Etten R.L.;
RT "Structural and mechanistic basis for the activation of a low-molecular
RT weight protein tyrosine phosphatase by adenine.";
RL Biochemistry 39:1234-1242(2000).
RN [8] {ECO:0007744|PDB:1D1P, ECO:0007744|PDB:1D1Q}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=10684639; DOI=10.1021/bi991348d;
RA Wang S., Tabernero L., Zhang M., Harms E., Van Etten R.L.,
RA Stauffacher C.V.;
RT "Crystal structures of a low-molecular weight protein tyrosine phosphatase
RT from Saccharomyces cerevisiae and its complex with the substrate p-
RT nitrophenyl phosphate.";
RL Biochemistry 39:1903-1914(2000).
CC -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC phosphates and natural and synthetic acyl phosphates.
CC {ECO:0000269|PubMed:7629177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:7629177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000269|PubMed:7629177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7629177}.
CC -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; U11057; AAA99546.1; -; mRNA.
DR EMBL; L48604; AAA80146.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89190.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94981.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68124.1; -; Genomic_DNA.
DR EMBL; AY692891; AAT92910.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11493.1; -; Genomic_DNA.
DR PIR; A57390; A57390.
DR RefSeq; NP_015398.1; NM_001184170.1.
DR PDB; 1D1P; X-ray; 2.20 A; A/B=2-161.
DR PDB; 1D1Q; X-ray; 1.70 A; A/B=1-161.
DR PDB; 1D2A; X-ray; 1.90 A; A/B=2-161.
DR PDBsum; 1D1P; -.
DR PDBsum; 1D1Q; -.
DR PDBsum; 1D2A; -.
DR AlphaFoldDB; P40347; -.
DR SMR; P40347; -.
DR BioGRID; 36246; 77.
DR DIP; DIP-6559N; -.
DR IntAct; P40347; 1.
DR STRING; 4932.YPR073C; -.
DR BindingDB; P40347; -.
DR ChEMBL; CHEMBL5397; -.
DR iPTMnet; P40347; -.
DR MaxQB; P40347; -.
DR PaxDb; P40347; -.
DR PRIDE; P40347; -.
DR EnsemblFungi; YPR073C_mRNA; YPR073C; YPR073C.
DR GeneID; 856187; -.
DR KEGG; sce:YPR073C; -.
DR SGD; S000006277; LTP1.
DR VEuPathDB; FungiDB:YPR073C; -.
DR eggNOG; KOG3217; Eukaryota.
DR GeneTree; ENSGT00940000167505; -.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; P40347; -.
DR OMA; TGSWHVG; -.
DR BioCyc; YEAST:G3O-34220-MON; -.
DR BRENDA; 3.1.3.48; 984.
DR EvolutionaryTrace; P40347; -.
DR PRO; PR:P40347; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P40347; 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; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..161
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase"
FT /id="PRO_0000046565"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10684639,
FT ECO:0007744|PDB:1D1Q"
FT ACT_SITE 20
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:10684639,
FT ECO:0007744|PDB:1D1Q"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:10684639,
FT ECO:0007744|PDB:1D1Q"
FT SITE 21
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:10684639,
FT ECO:0007744|PDB:1D1Q"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 8..19
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1D1Q"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:1D1Q"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1D1P"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1D1Q"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1D1Q"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1D1Q"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1D1Q"
FT HELIX 139..160
FT /evidence="ECO:0007829|PDB:1D1Q"
SQ SEQUENCE 161 AA; 18675 MW; 0911F4B85C050AB3 CRC64;
MTIEKPKISV AFICLGNFCR SPMAEAIFKH EVEKANLENR FNKIDSFGTS NYHVGESPDH
RTVSICKQHG VKINHKGKQI KTKHFDEYDY IIGMDESNIN NLKKIQPEGS KAKVCLFGDW
NTNDGTVQTI IEDPWYGDIQ DFEYNFKQIT YFSKQFLKKE L
