ID   PPAC_BOVIN              Reviewed;         158 AA.
AC   P11064;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Low molecular weight phosphotyrosine protein phosphatase;
DE            Short=LMW-PTP;
DE            Short=LMW-PTPase;
DE            EC=3.1.3.48 {ECO:0000305|PubMed:8319676};
DE   AltName: Full=Low molecular weight cytosolic acid phosphatase;
DE            EC=3.1.3.2 {ECO:0000305|PubMed:8319676};
GN   Name=ACP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=1339287; DOI=10.1021/bi00121a019;
RA   Wo Y.Y.P., Zhou M.M., Stevis P.E., Davis J.P., Zhang Z.Y., van Etten R.L.;
RT   "Cloning, expression, and catalytic mechanism of the low molecular weight
RT   phosphotyrosyl protein phosphatase from bovine heart.";
RL   Biochemistry 31:1712-1721(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-158, AND ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=2644264; DOI=10.1016/s0021-9258(19)81649-6;
RA   Camici G., Manao G., Cappugi G., Modesti A., Stefani M., Ramponi G.;
RT   "The complete amino acid sequence of the low molecular weight cytosolic
RT   acid phosphatase.";
RL   J. Biol. Chem. 264:2560-2567(1989).
RN   [3]
RP   ACTIVE SITES, AND MUTAGENESIS OF ARG-19.
RX   PubMed=8319676; DOI=10.1111/j.1432-1033.1993.tb17965.x;
RA   Cirri P., Chiarugi P., Camici G., Manao G., Raugei G., Cappugi G.,
RA   Ramponi G.;
RT   "The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-M(r)
RT   cytosolic phosphotyrosine protein phosphatase.";
RL   Eur. J. Biochem. 214:647-657(1993).
RN   [4]
RP   ACTIVE SITES, AND MUTAGENESIS.
RX   PubMed=8132604; DOI=10.1016/s0021-9258(17)37030-8;
RA   Davis J.P., Zhou M.M., van Etten R.L.;
RT   "Kinetic and site-directed mutagenesis studies of the cysteine residues of
RT   bovine low molecular weight phosphotyrosyl protein phosphatase.";
RL   J. Biol. Chem. 269:8734-8740(1994).
RN   [5]
RP   MUTAGENESIS OF CYS-13; CYS-18; CYS-63 AND CYS-146.
RX   PubMed=1526287; DOI=10.1016/0014-5793(92)81134-8;
RA   Chiarugi P., Marzocchini R., Raugei G., Pazzagli C., Berti A., Camici G.,
RA   Manao G., Cappugi G., Ramponi G.;
RT   "Differential role of four cysteines on the activity of a low M(r)
RT   phosphotyrosine protein phosphatase.";
RL   FEBS Lett. 310:9-12(1992).
RN   [6]
RP   MUTAGENESIS OF HIS-67 AND HIS-73.
RX   PubMed=8135752; DOI=10.1042/bj2980427;
RA   Chiarugi P., Cirri P., Camici G., Manao G., Fiaschi T., Raugei G.,
RA   Cappugi G., Ramponi G.;
RT   "The role of His66 and His72 in the reaction mechanism of bovine liver low-
RT   M(r) phosphotyrosine protein phosphatase.";
RL   Biochem. J. 298:427-433(1994).
RN   [7]
RP   MUTAGENESIS OF HIS-67 AND HIS-73.
RX   PubMed=8110762; DOI=10.1021/bi00171a031;
RA   Davis J.P., Zhou M.M., van Etten R.L.;
RT   "Spectroscopic and kinetic studies of the histidine residues of bovine low-
RT   molecular-weight phosphotyrosyl protein phosphatase.";
RL   Biochemistry 33:1278-1286(1994).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=8052313; DOI=10.1038/370575a0;
RA   Su X.-D., Taddei N., Stefani M., Ramponi G., Nordlund P.;
RT   "The crystal structure of a low-molecular-weight phosphotyrosine protein
RT   phosphatase.";
RL   Nature 370:575-578(1994).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8993313; DOI=10.1021/bi961804n;
RA   Zhang M., van Etten R.L., Stauffacher C.V.;
RT   "Crystal structure of bovine low molecular weight phosphotyrosyl
RT   phosphatase complexed with the transition state analog vanadate.";
RL   Biochemistry 36:15-23(1997).
RN   [10]
RP   STRUCTURE BY NMR.
RX   PubMed=8172896; DOI=10.1021/bi00183a027;
RA   Zhou M.-M., Logan T.M., Theriault Y., van Etten R.L., Fesik S.W.;
RT   "Backbone 1H, 13C, and 15N assignments and secondary structure of bovine
RT   low molecular weight phosphotyrosyl protein phosphatase.";
RL   Biochemistry 33:5221-5229(1994).
CC   -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates.
CC       {ECO:0000269|PubMed:8319676}.
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:0000305|PubMed:8319676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000305|PubMed:8319676};
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:0000305|PubMed:8319676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC         Evidence={ECO:0000305|PubMed:8319676};
CC   -!- ACTIVITY REGULATION: Inhibited by sulfhydryl reagents.
CC   -!- SUBUNIT: Interacts with EPHA2; dephosphorylates EPHA2. Interacts with
CC       EPHB1. Interacts with the SH3 domain of SPTAN1.
CC       {ECO:0000250|UniProtKB:P24666}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylated by LCK. Phosphorylation at Tyr-132 increases its
CC       phosphatase activity. {ECO:0000250|UniProtKB:P24666}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; M83656; AAC37328.1; -; mRNA.
DR   PIR; A42082; A42082.
DR   RefSeq; NP_776403.1; NM_173978.2.
DR   PDB; 1BVH; NMR; -; A=2-158.
DR   PDB; 1C0E; X-ray; 2.20 A; A/B=2-158.
DR   PDB; 1DG9; X-ray; 1.90 A; A=2-158.
DR   PDB; 1PHR; X-ray; 2.10 A; A=2-158.
DR   PDB; 1PNT; X-ray; 2.20 A; A=2-158.
DR   PDB; 1Z12; X-ray; 2.20 A; A=2-158.
DR   PDB; 1Z13; X-ray; 2.20 A; A=2-158.
DR   PDB; 5JNV; X-ray; 1.60 A; A=2-158.
DR   PDB; 5JNW; X-ray; 1.86 A; A=2-158.
DR   PDBsum; 1BVH; -.
DR   PDBsum; 1C0E; -.
DR   PDBsum; 1DG9; -.
DR   PDBsum; 1PHR; -.
DR   PDBsum; 1PNT; -.
DR   PDBsum; 1Z12; -.
DR   PDBsum; 1Z13; -.
DR   PDBsum; 5JNV; -.
DR   PDBsum; 5JNW; -.
DR   AlphaFoldDB; P11064; -.
DR   BMRB; P11064; -.
DR   SMR; P11064; -.
DR   STRING; 9913.ENSBTAP00000056837; -.
DR   BindingDB; P11064; -.
DR   ChEMBL; CHEMBL1075054; -.
DR   iPTMnet; P11064; -.
DR   Ensembl; ENSBTAT00000027314.5; ENSBTAP00000027314.4; ENSBTAG00000020498.6.
DR   GeneID; 280977; -.
DR   KEGG; bta:280977; -.
DR   CTD; 52; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020498; -.
DR   VGNC; VGNC:59193; ACP1.
DR   GeneTree; ENSGT00940000158351; -.
DR   InParanoid; P11064; -.
DR   OMA; QGEWHVE; -.
DR   OrthoDB; 5470890at2759; -.
DR   SABIO-RK; P11064; -.
DR   EvolutionaryTrace; P11064; -.
DR   PRO; PR:P11064; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000020498; Expressed in spermatid and 103 other cell types or tissues.
DR   ExpressionAtlas; P11064; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   CDD; cd16343; LMWPTP; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   PANTHER; PTHR11717:SF35; 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   PRINTS; PR00720; MAMMALPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2644264"
FT   CHAIN           2..158
FT                   /note="Low molecular weight phosphotyrosine protein
FT                   phosphatase"
FT                   /id="PRO_0000046557"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:8052313,
FT                   ECO:0000269|PubMed:8132604, ECO:0000269|PubMed:8319676"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000269|PubMed:8052313,
FT                   ECO:0000269|PubMed:8319676"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:8052313"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:2644264"
FT   MOD_RES         132
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P24666"
FT   MOD_RES         133
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P24666"
FT   MUTAGEN         13
FT                   /note="C->A,S: Inactive."
FT                   /evidence="ECO:0000269|PubMed:1526287"
FT   MUTAGEN         18
FT                   /note="C->S: Greatly decreases activity."
FT                   /evidence="ECO:0000269|PubMed:1526287"
FT   MUTAGEN         19
FT                   /note="R->K,M: Almost inactive and not able to bind the
FT                   substrate."
FT                   /evidence="ECO:0000269|PubMed:8319676"
FT   MUTAGEN         63
FT                   /note="C->S: 2.5-fold increase in activity."
FT                   /evidence="ECO:0000269|PubMed:1526287"
FT   MUTAGEN         67
FT                   /note="H->E: Decreased activity."
FT                   /evidence="ECO:0000269|PubMed:8110762,
FT                   ECO:0000269|PubMed:8135752"
FT   MUTAGEN         73
FT                   /note="H->E: Decreased activity."
FT                   /evidence="ECO:0000269|PubMed:8110762,
FT                   ECO:0000269|PubMed:8135752"
FT   MUTAGEN         146
FT                   /note="C->S: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:1526287"
FT   CONFLICT        57
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..18
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           19..33
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   STRAND          40..49
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   TURN            50..53
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           58..66
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:5JNV"
FT   HELIX           136..157
FT                   /evidence="ECO:0007829|PDB:5JNV"
SQ   SEQUENCE   158 AA;  18055 MW;  5925D5048C42BE02 CRC64;
     MAEQVTKSVL FVCLGNICRS PIAEAVFRKL VTDQNISDNW VIDSGAVSDW NVGRSPDPRA
     VSCLRNHGIN TAHKARQVTK EDFVTFDYIL CMDESNLRDL NRKSNQVKNC RAKIELLGSY
     DPQKQLIIED PYYGNDADFE TVYQQCVRCC RAFLEKVR
//