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 24-JAN-2024, entry version 181. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000147656; -. DR GlyCosmos; P49446; 2 sites, No reported glycans. DR GlyGen; P49446; 2 sites. DR iPTMnet; P49446; -. DR PhosphoSitePlus; P49446; -. DR EPD; P49446; -. DR jPOST; P49446; -. DR MaxQB; P49446; -. DR PaxDb; 10090-ENSMUSP00000073616; -. DR PeptideAtlas; P49446; -. DR ProteomicsDB; 301973; -. [P49446-1] DR ProteomicsDB; 301974; -. [P49446-2] DR ProteomicsDB; 301975; -. [P49446-3] DR Antibodypedia; 3004; 594 antibodies from 31 providers. DR DNASU; 19267; -. DR Ensembl; ENSMUST00000073961.8; ENSMUSP00000073616.7; ENSMUSG00000041836.11. [P49446-1] DR Ensembl; ENSMUST00000209979.2; ENSMUSP00000147613.2; ENSMUSG00000041836.11. [P49446-2] DR Ensembl; ENSMUST00000210833.2; ENSMUSP00000147313.2; ENSMUSG00000041836.11. [P49446-1] DR Ensembl; ENSMUST00000211140.2; ENSMUSP00000147957.2; ENSMUSG00000041836.11. [P49446-1] DR GeneID; 19267; -. DR KEGG; mmu:19267; -. DR UCSC; uc009kee.1; mouse. [P49446-1] DR UCSC; uc009kek.1; mouse. [P49446-2] DR AGR; MGI:97813; -. 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; QEGCKAP; -. DR OrthoDB; 2875525at2759; -. DR PhylomeDB; P49446; -. DR TreeFam; TF351829; -. DR SABIO-RK; P49446; -. DR BioGRID-ORCS; 19267; 1 hit in 80 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 201 other cell types or tissues. DR ExpressionAtlas; P49446; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB. 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 CDD; cd14620; R-PTPc-E-1; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR19134:SF499; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON; 1. 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; (Phosphotyrosine protein) phosphatases II; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. DR Genevisible; P49446; MM. 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 //