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   27-MAR-2024, entry version 190.
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; 78.
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; 4932-YPR073C; -.
DR   PeptideAtlas; P40347; -.
DR   EnsemblFungi; YPR073C_mRNA; YPR073C; YPR073C.
DR   GeneID; 856187; -.
DR   KEGG; sce:YPR073C; -.
DR   AGR; SGD:S000006277; -.
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; VCHGNIC; -.
DR   OrthoDB; 5470890at2759; -.
DR   BioCyc; YEAST:G3O-34220-MONOMER; -.
DR   BRENDA; 3.1.3.48; 984.
DR   BioGRID-ORCS; 856187; 5 hits in 10 CRISPR screens.
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   CDD; cd00115; LMWP; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   PANTHER; PTHR11717:SF7; LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11717; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 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
//