PPAC_RAT
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 03-AUG-2022, entry version 160.
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.ENSRNOP00000007287; -.
DR iPTMnet; P41498; -.
DR PhosphoSitePlus; P41498; -.
DR SwissPalm; P41498; -.
DR jPOST; P41498; -.
DR PaxDb; P41498; -.
DR PRIDE; P41498; -.
DR DNASU; 24161; -.
DR Ensembl; ENSRNOT00000007287; ENSRNOP00000007287; ENSRNOG00000005260. [P41498-1]
DR GeneID; 24161; -.
DR KEGG; rno:24161; -.
DR UCSC; RGD:2020; rat. [P41498-1]
DR CTD; 52; -.
DR RGD; 2020; Acp1.
DR eggNOG; KOG3217; Eukaryota.
DR InParanoid; P41498; -.
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:0043005; C:neuron projection; IDA: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 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; 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
