PTPRE_MOUSE
ID PTPRE_MOUSE Reviewed; 699 AA.
AC P49446; Q3U369; Q60986; Q61042; Q62134; Q62444; Q64496;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase epsilon;
DE Short=Protein-tyrosine phosphatase epsilon;
DE Short=R-PTP-epsilon;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptpre; Synonyms=Ptpe;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=FVB/N;
RX PubMed=7592814; DOI=10.1074/jbc.270.44.26116;
RA Elson A., Leder P.;
RT "Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in
RT mouse mammary tumors initiated by v-Ha-ras OR neu.";
RL J. Biol. Chem. 270:26116-26122(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=8618876; DOI=10.1073/pnas.92.26.12235;
RA Elson A., Leder P.;
RT "Identification of a cytoplasmic, phorbol ester-inducible isoform of
RT protein tyrosine phosphatase epsilon.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Osteoclast;
RX PubMed=8610169; DOI=10.1073/pnas.93.7.3068;
RA Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G.,
RA Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A.;
RT "Protein-tyrosine phosphatase activity regulates osteoclast formation and
RT function: inhibition by alendronate.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=DBA/2J;
RA Mukouyama Y.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Lung;
RA Hou E.W., Li S.L.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1454056; DOI=10.1007/bf00419663;
RA Schepens J., Zeeuwen P., Wieringa B., Hendriks W.;
RT "Identification and typing of members of the protein-tyrosine phosphatase
RT gene family expressed in mouse brain.";
RL Mol. Biol. Rep. 16:241-248(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-332, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Myeloid leukemia cell;
RX PubMed=1932742;
RA Yi T., Cleveland J.L., Ihle J.N.;
RT "Identification of novel protein tyrosine phosphatases of hematopoietic
RT cells by polymerase chain reaction amplification.";
RL Blood 78:2222-2228(1991).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7832766; DOI=10.1042/bj3050499;
RA Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT "A novel receptor-type protein tyrosine phosphatase with a single catalytic
RT domain is specifically expressed in mouse brain.";
RL Biochem. J. 305:499-504(1995).
RN [11]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=9914474; DOI=10.1046/j.1432-1327.1999.00004.x;
RA Tanuma N., Nakamura K., Kikuchi K.;
RT "Distinct promoters control transmembrane and cytosolic protein tyrosine
RT phosphatase epsilon expression during macrophage differentiation.";
RL Eur. J. Biochem. 259:46-54(1999).
RN [12]
RP IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION,
RP AND PROTEOLYTIC PROCESSING.
RX PubMed=10980613; DOI=10.1038/sj.onc.1203790;
RA Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A.;
RT "Generation of novel cytoplasmic forms of protein tyrosine phosphatase
RT epsilon by proteolytic processing and translational control.";
RL Oncogene 19:4375-4384(2000).
RN [13]
RP SUBUNIT, AND DOMAIN.
RX PubMed=12861030; DOI=10.1128/mcb.23.15.5460-5471.2003;
RA Toledano-Katchalski H., Tiran Z., Sines T., Shani G., Granot-Attas S.,
RA den Hertog J., Elson A.;
RT "Dimerization in vivo and inhibition of the nonreceptor form of protein
RT tyrosine phosphatase epsilon.";
RL Mol. Cell. Biol. 23:5460-5471(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [15]
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=18006633; DOI=10.1210/en.2007-0908;
RA Aga-Mizrachi S., Brutman-Barazani T., Jacob A.I., Bak A., Elson A.,
RA Sampson S.R.;
RT "Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of
RT insulin signaling in skeletal muscle.";
RL Endocrinology 149:605-614(2008).
RN [16]
RP FUNCTION (ISOFORM 1), DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18924107; DOI=10.1002/pmic.200700596;
RA De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C., Deana R.,
RA Brunati A.M., Turretta L., Iolascon A., Perrotta S., Elson A., Bulato C.,
RA Brugnara C.;
RT "PTPepsilon has a critical role in signaling transduction pathways and
RT phosphoprotein network topology in red cells.";
RL Proteomics 8:4695-4708(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19508371; DOI=10.1111/j.1365-3083.2009.02235.x;
RA Akimoto M., Mishra K., Lim K.-T., Tani N., Hisanaga S.-I., Katagiri T.,
RA Elson A., Mizuno K., Yakura H.;
RT "Protein tyrosine phosphatase epsilon is a negative regulator of
RT FcepsilonRI-mediated mast cell responses.";
RL Scand. J. Immunol. 69:401-411(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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).
CC -!- FUNCTION: [Isoform 1]: Acts as a negative regulator of insulin receptor
CC (IR) signaling and is involved in insulin-induced glucose metabolism
CC mainly through direct dephosphorylation and inactivation of IR in
CC hepatocytes and liver (By similarity). Plays a critical role in
CC signaling transduction pathways and phosphoprotein network topology in
CC red blood cells. May play a role in osteoclast formation and function.
CC {ECO:0000250, ECO:0000269|PubMed:19508371, ECO:0000269|PubMed:8610169}.
CC -!- FUNCTION: [Isoform 2]: Acts as a negative regulator of insulin receptor
CC (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine
CC phosphorylation of insulin receptor (IR) and insulin receptor substrate
CC 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase
CC kinase-3 and insulin induced stimulation of glucose uptake.
CC -!- FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of FceRI-
CC mediated signal transduction leading to cytokine production and
CC degranulation, most likely by acting at the level of SYK to affect
CC downstream events such as phosphorylation of SLP76 and LAT and
CC mobilization of Ca(2+).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- ACTIVITY REGULATION: [Isoform 1]: Inhibited by alendronate (ALN),
CC orthovanadate, and phenylarsine oxide (PAO).
CC {ECO:0000269|PubMed:8610169}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for fluorescein diphosphate (isoform 1)
CC {ECO:0000269|PubMed:8610169};
CC Vmax=6 umol/min/mg enzyme for fluorescein diphosphate (isoform 1)
CC {ECO:0000269|PubMed:8610169};
CC -!- SUBUNIT: Monomer (By similarity). Isoform 2: Homodimer. Can form
CC oligomers. Dimerization is increased by oxidative stress and decreased
CC by EGFR. Isoform 2 interacts with GRB2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Predominantly
CC cytoplasmic. A small fraction is also associated with nucleus and
CC membrane. Insulin can induce translocation to the membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=PTPeM, RPTPe, tm-PTPe;
CC IsoId=P49446-1; Sequence=Displayed;
CC Name=2; Synonyms=PTPeC, cyt-PTPe;
CC IsoId=P49446-2; Sequence=VSP_038492;
CC Name=3; Synonyms=p67;
CC IsoId=P49446-3; Sequence=VSP_038491;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in the spleen and thymus (at
CC protein level). Detected in fibroblasts, myeloid cells, macrophages,
CC and T-cells but not in B-cell lines. Isoform 1 and isoform 2 are
CC expressed predominantly in the brain, testes, and lungs, with lower
CC levels present in lymph nodes, thymus, spleen, heart and mammary
CC glands. Isoform 1 is expressed in osteoclasts and not in osteoblasts
CC and its expression is related to osteoclast differentiation. It is also
CC expressed in the erythrocytes. Isoform 2 is strongly expressed in
CC skeletal muscle and L6 skeletal muscle cell line.
CC {ECO:0000269|PubMed:18006633, ECO:0000269|PubMed:18924107,
CC ECO:0000269|PubMed:1932742, ECO:0000269|PubMed:8610169,
CC ECO:0000269|PubMed:8618876}.
CC -!- INDUCTION: [Isoform 2]: Induced by 12-O-tetradecanoylphorbol-13-acetate
CC (TPA) and its induction is dependent upon PKC activity.
CC {ECO:0000269|PubMed:8618876}.
CC -!- DOMAIN: The tyrosine-protein phosphatase 2 domain (D2) mediates
CC dimerization. The extreme N- and C- termini of the D2 domain act to
CC inhibit dimerization and removal of these sequences increases
CC dimerization and inhibits enzyme activity.
CC {ECO:0000269|PubMed:12861030}.
CC -!- PTM: A catalytically active cytoplasmic form (p65) is produced by
CC proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.
CC {ECO:0000269|PubMed:10980613}.
CC -!- PTM: [Isoform 1]: Phosphorylated on tyrosine residues by tyrosine
CC kinase Neu. {ECO:0000250}.
CC -!- PTM: [Isoform 2]: Phosphorylated on tyrosine residues by tyrosine
CC kinase Neu. {ECO:0000250}.
CC -!- PTM: [Isoform 1]: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show greater insulin-induced tyrosine
CC phosphorylation of insulin receptor (IR) and insulin receptor substrate
CC 1 (IRS-1) in the skeletal muscle. Antigen- and IgE-mediated passive
CC systemic anaphylactic reactions are enhanced. Erythrocytes exhibit
CC abnormal morphology, increased Ca(2+)-activated-K(+) channel activity
CC and marked perturbation of the erythrocyte membrane tyrosine
CC phosphoproteome. {ECO:0000269|PubMed:18006633,
CC ECO:0000269|PubMed:18924107, ECO:0000269|PubMed:19508371}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met-
CC 85 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; U35368; AAC52281.1; -; mRNA.
DR EMBL; U36758; AAC52331.1; -; mRNA.
DR EMBL; U40280; AAB02190.1; -; mRNA.
DR EMBL; D83484; BAA11927.1; -; mRNA.
DR EMBL; U62387; AAB04553.1; -; mRNA.
DR EMBL; AK154910; BAE32920.1; -; mRNA.
DR EMBL; CH466531; EDL17805.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL17807.1; -; Genomic_DNA.
DR EMBL; Z23052; CAA80587.1; -; mRNA.
DR EMBL; Z23053; CAA80588.1; -; mRNA.
DR CCDS; CCDS21944.1; -. [P49446-1]
DR CCDS; CCDS85446.1; -. [P49446-2]
DR PIR; B61180; B61180.
DR PIR; JC6132; JC6132.
DR PIR; S40284; S40284.
DR RefSeq; NP_001303607.1; NM_001316678.1.
DR RefSeq; NP_001303608.1; NM_001316679.1. [P49446-1]
DR RefSeq; NP_001303609.1; NM_001316680.1.
DR RefSeq; NP_001303610.1; NM_001316681.1. [P49446-2]
DR RefSeq; NP_035342.3; NM_011212.3. [P49446-1]
DR AlphaFoldDB; P49446; -.
DR SMR; P49446; -.
DR BioGRID; 202496; 15.
DR IntAct; P49446; 4.
DR MINT; P49446; -.
DR STRING; 10090.ENSMUSP00000073616; -.
DR GlyGen; P49446; 2 sites.
DR iPTMnet; P49446; -.
DR PhosphoSitePlus; P49446; -.
DR EPD; P49446; -.
DR jPOST; P49446; -.
DR MaxQB; P49446; -.
DR PaxDb; P49446; -.
DR PeptideAtlas; P49446; -.
DR PRIDE; P49446; -.
DR ProteomicsDB; 301973; -. [P49446-1]
DR ProteomicsDB; 301974; -. [P49446-2]
DR ProteomicsDB; 301975; -. [P49446-3]
DR Antibodypedia; 3004; 535 antibodies from 31 providers.
DR DNASU; 19267; -.
DR Ensembl; ENSMUST00000073961; ENSMUSP00000073616; ENSMUSG00000041836. [P49446-1]
DR Ensembl; ENSMUST00000209979; ENSMUSP00000147613; ENSMUSG00000041836. [P49446-2]
DR Ensembl; ENSMUST00000210833; ENSMUSP00000147313; ENSMUSG00000041836. [P49446-1]
DR Ensembl; ENSMUST00000211140; ENSMUSP00000147957; ENSMUSG00000041836. [P49446-1]
DR GeneID; 19267; -.
DR KEGG; mmu:19267; -.
DR UCSC; uc009kee.1; mouse. [P49446-1]
DR UCSC; uc009kek.1; mouse. [P49446-2]
DR CTD; 5791; -.
DR MGI; MGI:97813; Ptpre.
DR VEuPathDB; HostDB:ENSMUSG00000041836; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000156570; -.
DR HOGENOM; CLU_001645_8_2_1; -.
DR InParanoid; P49446; -.
DR OMA; RKFCVHS; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P49446; -.
DR TreeFam; TF351829; -.
DR BioGRID-ORCS; 19267; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ptpre; mouse.
DR PRO; PR:P49446; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P49446; protein.
DR Bgee; ENSMUSG00000041836; Expressed in granulocyte and 199 other tissues.
DR ExpressionAtlas; P49446; baseline and differential.
DR Genevisible; P49446; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0033003; P:regulation of mast cell activation; IMP:UniProtKB.
DR GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; IDA:MGI.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative promoter usage; Cell membrane;
KW Cytoplasm; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..699
FT /note="Receptor-type tyrosine-protein phosphatase epsilon"
FT /id="PRO_0000025440"
FT TOPO_DOM 20..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..393
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 425..688
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 629
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334..340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 695
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19144319"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038491"
FT VAR_SEQ 1..69
FT /note="MEPFCPLLLASFSLSLARAGQGNDTTPTESNWTSTTAGPPDPGASQPLLTWL
FT LLPLLLLLFLLAAYFFR -> MSSRKNFSRLTW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8618876"
FT /id="VSP_038492"
FT CONFLICT 137
FT /note="E -> K (in Ref. 6; BAE32920)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> A (in Ref. 4; BAA11927)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="V -> G (in Ref. 1; AAC52281, 2; AAC52331 and 5;
FT AAB04553)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..522
FT /note="IV -> ML (in Ref. 4; BAA11927)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="M -> I (in Ref. 1; AAC52281 and 2; AAC52331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 80688 MW; 581EF9CB881BC05B CRC64;
MEPFCPLLLA SFSLSLARAG QGNDTTPTES NWTSTTAGPP DPGASQPLLT WLLLPLLLLL
FLLAAYFFRF RKQRKAVVSS NDKKMPNGIL EEQEQQRVML LSRSPSGPKK FFPIPVEHLE
EEIRVRSADD CKRFREEFNS LPSGHIQGTF ELANKEENRE KNRYPNILPN DHCRVILSQV
DGIPCSDYIN ASYIDGYKEK NKFIAAQGPK QETVNDFWRM VWEQRSATIV MLTNLKERKE
EKCYQYWPDQ GCWTYGNIRV CVEDCVVLVD YTIRKFCIHP QLPDSCKAPR LVSQLHFTSW
PDFGVPFTPI GMLKFLKKVK TLNPSHAGPI VVHCSAGVGR TGTFIVIDAM MDMIHSEQKV
DVFEFVSRIR NQRPQMVQTD VQYTFIYQAL LEYYLYGDTE LDVSSLERHL QTLHSTATHF
DKIGLEEEFR KLTNVRIMKE NMRTGNLPAN MKKARVIQII PYDFNRVILS MKRGQEFTDY
INASFIDGYR QKDYFMATQG PLAHTVEDFW RMVWEWKSHT IVMLTEVQER EQDKCYQYWP
TEGSVTHGDI TIEIKSDTLS EAISVRDFLV TFKQPLARQE EQVRMVRQFH FHGWPEVGIP
AEGKGMIDLI AAVQKQQQQT GNHPITVHCS AGAGRTGTFI ALSNILERVK AEGLLDVFQA
VKSLRLQRPH MVQTLEQYEF CYKVVQDFID IFSDYANFK
