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Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2)

 PPAC_MOUSE              Reviewed;         158 AA.
Q9D358; O88739; O88740; Q9QWF5;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 140.
RecName: Full=Low molecular weight phosphotyrosine protein phosphatase;
Short=LMW-PTP;
Short=LMW-PTPase;
EC=3.1.3.48;
AltName: Full=Low molecular weight cytosolic acid phosphatase;
EC=3.1.3.2;
Name=Acp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:CAA76753.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
VARIANTS PRO-14 AND PRO-157.
TISSUE=Liver {ECO:0000312|EMBL:CAA76753.1};
PubMed=9824304; DOI=10.1016/S0014-5793(98)01241-1;
Magherini F., Giannoni E., Raugei G., Cirri P., Paoli P., Modesti A.,
Camici G., Ramponi G.;
"Cloning of murine low molecular weight phosphotyrosine protein
phosphatase cDNA: identification of a new isoform.";
FEBS Lett. 437:263-266(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Skin, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N {ECO:0000312|EMBL:AAH39744.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-158.
PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
"Structural genomics of protein phosphatases.";
J. Struct. Funct. Genomics 8:121-140(2007).
-!- FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl
phosphates and natural and synthetic acyl phosphates.
{ECO:0000250|UniProtKB:P11064}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000250|UniProtKB:P11064}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate.
-!- SUBUNIT: Interacts with the SH3 domain of SPTAN1. Interacts with
EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:9824304}; Synonyms=m-IF1
{ECO:0000303|PubMed:9824304};
IsoId=Q9D358-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:9824304}; Synonyms=m-IF2
{ECO:0000303|PubMed:9824304};
IsoId=Q9D358-2; Sequence=VSP_050726;
Note=Variant in position: 67:R->H.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain
and liver and lowest levels in muscle.
{ECO:0000269|PubMed:9824304}.
-!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
protein phosphatase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y17343; CAA76753.1; -; mRNA.
EMBL; Y17344; CAA76754.1; -; mRNA.
EMBL; Y17345; CAA76755.1; -; mRNA.
EMBL; AK014603; BAB29458.1; -; mRNA.
EMBL; AK018329; BAB31164.1; -; mRNA.
EMBL; AK019186; BAB31593.1; -; mRNA.
EMBL; AK082955; BAC38707.1; -; mRNA.
EMBL; BC039744; AAH39744.1; -; mRNA.
CCDS; CCDS36427.1; -. [Q9D358-1]
CCDS; CCDS49045.1; -. [Q9D358-2]
RefSeq; NP_001103709.1; NM_001110239.1.
RefSeq; NP_067305.2; NM_021330.4. [Q9D358-1]
UniGene; Mm.359831; -.
PDB; 2P4U; X-ray; 1.90 A; A/B/C/D=2-158.
PDB; 5JNU; X-ray; 2.54 A; A/B=1-158.
PDBsum; 2P4U; -.
PDBsum; 5JNU; -.
ProteinModelPortal; Q9D358; -.
SMR; Q9D358; -.
BioGrid; 197927; 3.
IntAct; Q9D358; 4.
MINT; Q9D358; -.
BindingDB; Q9D358; -.
ChEMBL; CHEMBL3593153; -.
iPTMnet; Q9D358; -.
PhosphoSitePlus; Q9D358; -.
REPRODUCTION-2DPAGE; Q9D358; -.
EPD; Q9D358; -.
PeptideAtlas; Q9D358; -.
PRIDE; Q9D358; -.
DNASU; 11431; -.
Ensembl; ENSMUST00000062740; ENSMUSP00000106509; ENSMUSG00000044573. [Q9D358-1]
GeneID; 11431; -.
KEGG; mmu:11431; -.
UCSC; uc007ngw.2; mouse. [Q9D358-1]
CTD; 52; -.
MGI; MGI:87881; Acp1.
GeneTree; ENSGT00500000044891; -.
HOGENOM; HOG000273094; -.
HOVERGEN; HBG007540; -.
InParanoid; Q9D358; -.
KO; K14394; -.
PhylomeDB; Q9D358; -.
TreeFam; TF353727; -.
PRO; PR:Q9D358; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000044573; -.
CleanEx; MM_ACP1; -.
ExpressionAtlas; Q9D358; baseline and differential.
Genevisible; Q9D358; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0003993; F:acid phosphatase activity; IDA:MGI.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0016791; F:phosphatase activity; IDA:MGI.
InterPro; IPR023485; Ptyr_pPase.
InterPro; IPR036196; Ptyr_pPase_sf.
InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
Pfam; PF01451; LMWPc; 1.
PRINTS; PR00719; LMWPTPASE.
PRINTS; PR00720; MAMMALPTPASE.
SMART; SM00226; LMWPc; 1.
SUPFAM; SSF52788; SSF52788; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Hydrolase; Phosphoprotein; Polymorphism;
Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11064}.
CHAIN 2 158 Low molecular weight phosphotyrosine
protein phosphatase.
/FTId=PRO_0000046559.
ACT_SITE 13 13 Nucleophile. {ECO:0000250}.
ACT_SITE 19 19 {ECO:0000250}.
ACT_SITE 130 130 Proton donor. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P11064}.
MOD_RES 132 132 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24666}.
MOD_RES 133 133 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24666}.
VAR_SEQ 41 74 RIDSAATSTYEVGNPPDYRGQNCMRKHGIHMQHI -> AID
SSAVSDWNVGRPPDPRAVSCLRNRGISTAHK (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9824304}.
/FTId=VSP_050726.
VARIANT 14 14 L -> P. {ECO:0000269|PubMed:9824304}.
VARIANT 157 157 T -> P. {ECO:0000269|PubMed:9824304}.
STRAND 7 18 {ECO:0000244|PDB:2P4U}.
HELIX 19 33 {ECO:0000244|PDB:2P4U}.
HELIX 37 39 {ECO:0000244|PDB:2P4U}.
STRAND 40 49 {ECO:0000244|PDB:2P4U}.
TURN 50 53 {ECO:0000244|PDB:2P4U}.
HELIX 58 66 {ECO:0000244|PDB:2P4U}.
HELIX 80 85 {ECO:0000244|PDB:2P4U}.
STRAND 87 93 {ECO:0000244|PDB:2P4U}.
HELIX 94 105 {ECO:0000244|PDB:2P4U}.
STRAND 113 116 {ECO:0000244|PDB:2P4U}.
HELIX 117 120 {ECO:0000244|PDB:2P4U}.
HELIX 131 133 {ECO:0000244|PDB:5JNU}.
HELIX 136 157 {ECO:0000244|PDB:2P4U}.
SEQUENCE 158 AA; 18192 MW; A374BE5C183226AE CRC64;
MAEVGSKSVL FVCLGNICRS PIAEAVFRKL VTDEKVSDNW RIDSAATSTY EVGNPPDYRG
QNCMRKHGIH MQHIARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKNC KAKIELLGSY
DPQKQLIIED PYYGNDSDFE VVYQQCLRCC KAFLEKTY


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