PPAC_MOUSE
ID PPAC_MOUSE Reviewed; 158 AA.
AC Q9D358; O88739; O88740; Q9QWF5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
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|MGI:MGI:87881};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:CAA76753.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANTS PRO-14 AND PRO-157.
RC TISSUE=Liver {ECO:0000312|EMBL:CAA76753.1};
RX PubMed=9824304; DOI=10.1016/s0014-5793(98)01241-1;
RA Magherini F., Giannoni E., Raugei G., Cirri P., Paoli P., Modesti A.,
RA Camici G., Ramponi G.;
RT "Cloning of murine low molecular weight phosphotyrosine protein phosphatase
RT cDNA: identification of a new isoform.";
RL FEBS Lett. 437:263-266(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Skin, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH39744.1};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-158.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
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 {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9824304}; Synonyms=m-IF1
CC {ECO:0000303|PubMed:9824304};
CC IsoId=Q9D358-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9824304}; Synonyms=m-IF2
CC {ECO:0000303|PubMed:9824304};
CC IsoId=Q9D358-2; Sequence=VSP_050726;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain and
CC liver and lowest levels in muscle. {ECO:0000269|PubMed:9824304}.
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; Y17343; CAA76753.1; -; mRNA.
DR EMBL; Y17344; CAA76754.1; -; mRNA.
DR EMBL; Y17345; CAA76755.1; -; mRNA.
DR EMBL; AK014603; BAB29458.1; -; mRNA.
DR EMBL; AK018329; BAB31164.1; -; mRNA.
DR EMBL; AK019186; BAB31593.1; -; mRNA.
DR EMBL; AK082955; BAC38707.1; -; mRNA.
DR EMBL; BC039744; AAH39744.1; -; mRNA.
DR CCDS; CCDS36427.1; -. [Q9D358-1]
DR CCDS; CCDS49045.1; -. [Q9D358-2]
DR RefSeq; NP_001103709.1; NM_001110239.1.
DR RefSeq; NP_067305.2; NM_021330.4. [Q9D358-1]
DR PDB; 2P4U; X-ray; 1.90 A; A/B/C/D=2-158.
DR PDB; 5JNU; X-ray; 2.54 A; A/B=1-158.
DR PDBsum; 2P4U; -.
DR PDBsum; 5JNU; -.
DR AlphaFoldDB; Q9D358; -.
DR SMR; Q9D358; -.
DR BioGRID; 197927; 8.
DR IntAct; Q9D358; 2.
DR STRING; 10090.ENSMUSP00000106509; -.
DR BindingDB; Q9D358; -.
DR ChEMBL; CHEMBL3593153; -.
DR iPTMnet; Q9D358; -.
DR PhosphoSitePlus; Q9D358; -.
DR REPRODUCTION-2DPAGE; Q9D358; -.
DR CPTAC; non-CPTAC-3861; -.
DR EPD; Q9D358; -.
DR jPOST; Q9D358; -.
DR MaxQB; Q9D358; -.
DR PeptideAtlas; Q9D358; -.
DR PRIDE; Q9D358; -.
DR ProteomicsDB; 291644; -. [Q9D358-1]
DR ProteomicsDB; 291645; -. [Q9D358-2]
DR DNASU; 11431; -.
DR Ensembl; ENSMUST00000062740; ENSMUSP00000106509; ENSMUSG00000044573. [Q9D358-1]
DR GeneID; 11431; -.
DR KEGG; mmu:11431; -.
DR UCSC; uc007ngw.2; mouse. [Q9D358-1]
DR CTD; 52; -.
DR MGI; MGI:87881; Acp1.
DR VEuPathDB; HostDB:ENSMUSG00000044573; -.
DR eggNOG; KOG3217; Eukaryota.
DR GeneTree; ENSGT00940000158351; -.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; Q9D358; -.
DR OrthoDB; 1362234at2759; -.
DR PhylomeDB; Q9D358; -.
DR TreeFam; TF353727; -.
DR BioGRID-ORCS; 11431; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Acp1; mouse.
DR PRO; PR:Q9D358; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D358; protein.
DR Bgee; ENSMUSG00000044573; Expressed in undifferentiated genital tubercle and 159 other tissues.
DR ExpressionAtlas; Q9D358; baseline and differential.
DR Genevisible; Q9D358; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:MGI.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016791; F:phosphatase activity; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
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; Alternative splicing; Cytoplasm; Hydrolase;
KW Phosphoprotein; Protein phosphatase; 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_0000046559"
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"
FT VAR_SEQ 41..74
FT /note="RIDSAATSTYEVGNPPDYRGQNCMRKHGIHMQHI -> AIDSSAVSDWNVGR
FT PPDPRAVSCLRNRGISTAHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9824304"
FT /id="VSP_050726"
FT VARIANT 14
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:9824304"
FT VARIANT 157
FT /note="T -> P"
FT /evidence="ECO:0000269|PubMed:9824304"
FT STRAND 7..18
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2P4U"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:2P4U"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:2P4U"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2P4U"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2P4U"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5JNU"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:2P4U"
FT VARIANT Q9D358-2:67
FT /note="R -> H"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18192 MW; A374BE5C183226AE CRC64;
MAEVGSKSVL FVCLGNICRS PIAEAVFRKL VTDEKVSDNW RIDSAATSTY EVGNPPDYRG
QNCMRKHGIH MQHIARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKNC KAKIELLGSY
DPQKQLIIED PYYGNDSDFE VVYQQCLRCC KAFLEKTY
