ID   PPAC_PONAB              Reviewed;         158 AA.
AC   Q5REM7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Low molecular weight phosphotyrosine protein phosphatase {ECO:0000305};
DE            Short=LMW-PTP;
DE            Short=LMW-PTPase;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:P24666};
DE   AltName: Full=Low molecular weight cytosolic acid phosphatase;
DE            EC=3.1.3.2 {ECO:0000250|UniProtKB:P24666};
GN   Name=ACP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates with differences
CC       in substrate specificity between isoform 1 and isoform 2.
CC       {ECO:0000250|UniProtKB:P24666}.
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:0000250|UniProtKB:P24666};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P24666};
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:0000250|UniProtKB:P24666};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC         Evidence={ECO:0000250|UniProtKB:P24666};
CC   -!- ACTIVITY REGULATION: Inhibited by sulfhydryl reagents.
CC       {ECO:0000250|UniProtKB:P24666}.
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 {ECO:0000250|UniProtKB:P24666}.
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; CR857496; CAH89780.1; -; mRNA.
DR   RefSeq; NP_001124815.1; NM_001131343.1.
DR   AlphaFoldDB; Q5REM7; -.
DR   BMRB; Q5REM7; -.
DR   SMR; Q5REM7; -.
DR   STRING; 9601.ENSPPYP00000014169; -.
DR   Ensembl; ENSPPYT00000058335; ENSPPYP00000035868; ENSPPYG00000012694.
DR   GeneID; 100171673; -.
DR   KEGG; pon:100171673; -.
DR   CTD; 52; -.
DR   eggNOG; KOG3217; Eukaryota.
DR   GeneTree; ENSGT00940000158351; -.
DR   HOGENOM; CLU_071415_2_0_1; -.
DR   InParanoid; Q5REM7; -.
DR   Proteomes; UP000001595; Chromosome 2A.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   CHAIN           2..158
FT                   /note="Low molecular weight phosphotyrosine protein
FT                   phosphatase"
FT                   /id="PRO_0000256845"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
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"
SQ   SEQUENCE   158 AA;  18086 MW;  5617782F280321DC CRC64;
     MAEQSTKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW RVDSAATSGY EIGNPPDYRG
     QSCMKRHGIP MSHVARQITR EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY
     DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH