PPAC_BOVIN
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 03-AUG-2022, entry version 162.
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 BindingDB; P11064; -.
DR ChEMBL; CHEMBL1075054; -.
DR iPTMnet; P11064; -.
DR PRIDE; P11064; -.
DR Ensembl; ENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498.
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; YQQVTRF; -.
DR OrthoDB; 1362234at2759; -.
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 tissues.
DR ExpressionAtlas; P11064; baseline and differential.
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 GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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 Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR PRINTS; PR00720; MAMMALPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 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
