PPAC_PIG
ID PPAC_PIG Reviewed; 158 AA.
AC P81693;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
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;
GN Name=ACP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 2-158.
RC TISSUE=Liver;
RX PubMed=8011064; DOI=10.1007/bf01891998;
RA Caselli A., Pazzagli L., Paoli P., Manao G., Camici G., Cappugi G.,
RA Ramponi G.;
RT "Porcine liver low M(r) phosphotyrosine protein phosphatase: the amino acid
RT sequence.";
RL J. Protein Chem. 13:107-115(1994).
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 RefSeq; XP_003481358.1; XM_003481310.2.
DR AlphaFoldDB; P81693; -.
DR SMR; P81693; -.
DR STRING; 9823.ENSSSCP00000009231; -.
DR PaxDb; P81693; -.
DR PeptideAtlas; P81693; -.
DR PRIDE; P81693; -.
DR Ensembl; ENSSSCT00005031744; ENSSSCP00005019328; ENSSSCG00005019704.
DR Ensembl; ENSSSCT00005031836; ENSSSCP00005019403; ENSSSCG00005019704.
DR Ensembl; ENSSSCT00015098433; ENSSSCP00015040539; ENSSSCG00015073160.
DR Ensembl; ENSSSCT00040084873; ENSSSCP00040037061; ENSSSCG00040062216.
DR Ensembl; ENSSSCT00050051325; ENSSSCP00050021527; ENSSSCG00050038047.
DR Ensembl; ENSSSCT00070035716; ENSSSCP00070029841; ENSSSCG00070018094.
DR GeneID; 100737301; -.
DR KEGG; ssc:100737301; -.
DR CTD; 52; -.
DR eggNOG; KOG3217; Eukaryota.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; P81693; -.
DR OMA; YQQVTRF; -.
DR OrthoDB; 1362234at2759; -.
DR TreeFam; TF353727; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 3.
DR Genevisible; P81693; SS.
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 Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11064,
FT ECO:0000269|PubMed:8011064"
FT CHAIN 2..158
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase"
FT /id="PRO_0000046560"
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; 18035 MW; 526AF176D24F86D2 CRC64;
MAEQVTKSVL FVCLGNICRS PIAEAVFRKL VTDQNVSDNW VIDSSAVSDW NVGRSPDPRA
VSCLRHHGIN TAHKARQITK EDFATFDYIL CMDESNLRDL NRKGNQVKNC RAKIELLGSY
DPQKQLIIED PYYGNDSDFE AVYQQCVRCC RAFLEKVR
