ID   PPAC_RAT                Reviewed;         158 AA.
AC   P41498; Q9R138;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 167.
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 {ECO:0000312|RGD:2020};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SPTAN1.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=11971983; DOI=10.1128/mcb.22.10.3527-3536.2002;
RA   Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O.,
RA   Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B.,
RA   Lecomte M.-C.;
RT   "Tyrosine phosphorylation regulates alpha II spectrin cleavage by
RT   calpain.";
RL   Mol. Cell. Biol. 22:3527-3536(2002).
RN   [2]
RP   PROTEIN SEQUENCE (ISOFORMS 1 AND 2), CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=1388675; DOI=10.1007/bf01024871;
RA   Manao G., Pazzagli L., Cirri P., Caselli A., Camici G., Cappugi G.,
RA   Saeed A., Ramponi G.;
RT   "Rat liver low M(r) phosphotyrosine protein phosphatase isoenzymes:
RT   purification and amino acid sequences.";
RL   J. Protein Chem. 11:333-345(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 20-28; 42-59 AND 114-124, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
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. {ECO:0000250|UniProtKB:P24666}.
CC   -!- SUBUNIT: [Isoform 1]: Interacts with the SH3 domain of SPTAN1. There is
CC       no interaction observed for isoform 2. {ECO:0000250|UniProtKB:P24666}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=ACP1, A;
CC         IsoId=P41498-1; Sequence=Displayed;
CC       Name=2; Synonyms=ACP2, B;
CC         IsoId=P41498-2; Sequence=VSP_004705;
CC   -!- PTM: [Isoform 2]: Phosphorylated by LCK. Phosphorylation at Tyr-132
CC       increases its 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; AF171072; AAD50990.1; -; mRNA.
DR   EMBL; BC062229; AAH62229.1; -; mRNA.
DR   PIR; A53874; A53874.
DR   RefSeq; NP_067085.1; NM_021262.2. [P41498-1]
DR   AlphaFoldDB; P41498; -.
DR   SMR; P41498; -.
DR   BioGRID; 246352; 2.
DR   STRING; 10116.ENSRNOP00000072548; -.
DR   BindingDB; P41498; -.
DR   ChEMBL; CHEMBL5169132; -.
DR   iPTMnet; P41498; -.
DR   PhosphoSitePlus; P41498; -.
DR   SwissPalm; P41498; -.
DR   jPOST; P41498; -.
DR   PaxDb; 10116-ENSRNOP00000007287; -.
DR   DNASU; 24161; -.
DR   Ensembl; ENSRNOT00000007287.8; ENSRNOP00000007287.8; ENSRNOG00000005260.8. [P41498-1]
DR   Ensembl; ENSRNOT00055009490; ENSRNOP00055007304; ENSRNOG00055005874. [P41498-1]
DR   Ensembl; ENSRNOT00060013395; ENSRNOP00060010194; ENSRNOG00060008086. [P41498-1]
DR   Ensembl; ENSRNOT00065017323; ENSRNOP00065013267; ENSRNOG00065010681. [P41498-1]
DR   GeneID; 24161; -.
DR   KEGG; rno:24161; -.
DR   UCSC; RGD:2020; rat. [P41498-1]
DR   AGR; RGD:2020; -.
DR   CTD; 52; -.
DR   RGD; 2020; Acp1.
DR   eggNOG; KOG3217; Eukaryota.
DR   InParanoid; P41498; -.
DR   OrthoDB; 5470890at2759; -.
DR   PhylomeDB; P41498; -.
DR   TreeFam; TF353727; -.
DR   PRO; PR:P41498; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:RGD.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016791; F:phosphatase activity; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEP:RGD.
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:SF34; 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   Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1388675"
FT   CHAIN           2..158
FT                   /note="Low molecular weight phosphotyrosine protein
FT                   phosphatase"
FT                   /id="PRO_0000046561"
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:0000269|PubMed:1388675"
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   VAR_SEQ         41..74
FT                   /note="RIDSAATSTYEVGNPPDYRGQNCMKKHGIHMQHI -> AIDSSAVSDWNVGR
FT                   PPDPRAVNCLRNHGISTAHK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1388675"
FT                   /id="VSP_004705"
FT   CONFLICT        2
FT                   /note="A -> ACA (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   158 AA;  18152 MW;  5C454D4DA82FB094 CRC64;
     MAEVGSKSVL FVCLGNICRS PIAEAVFRKL VTDENVSDNW RIDSAATSTY EVGNPPDYRG
     QNCMKKHGIH MQHIARQITR EDFATFDYIL CMDESNLRDL NRKSNQVKNC KAKIELLGSY
     DPQKQLIIED PYYGNDSDFE VVYQQCLRCC KAFLEKTH
//