PTPRE_HUMAN
ID PTPRE_HUMAN Reviewed; 700 AA.
AC P23469; Q13345; Q5VWH3; Q5VWH4; Q96KQ6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 201.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2170109; DOI=10.1002/j.1460-2075.1990.tb07523.x;
RA Krueger N.X., Streuli M., Saito H.;
RT "Structural diversity and evolution of human receptor-like protein tyrosine
RT phosphatases.";
RL EMBO J. 9:3241-3252(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12121439; DOI=10.1046/j.1365-3083.2002.01126.x;
RA Wabakken T.K., Hauge H., Finne E.F., Wiedlocha A., Aasheim H.-C.;
RT "Expression of human protein tyrosine phosphatase epsilon in leucocytes: a
RT potential ERK pathway-regulating phosphatase.";
RL Scand. J. Immunol. 56:195-203(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP INDUCTION.
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 [8]
RP TISSUE SPECIFICITY.
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 [9]
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 [10]
RP IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC PROCESSING, PHOSPHORYLATION, GLYCOSYLATION, AND INTERACTION
RP WITH GRB2.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-696, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 107-697, AND SUBUNIT.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
CC -!- FUNCTION: Isoform 1 plays a critical role in signaling transduction
CC pathways and phosphoprotein network topology in red blood cells. May
CC play a role in osteoclast formation and function (By similarity).
CC {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
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+). {ECO:0000250}.
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 -!- SUBUNIT: Monomer. Isoform 2: Homodimer. Can form oligomers.
CC Dimerization is increased by oxidative stress and decreased by EGFR.
CC 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 induces translocation to the membrane (By
CC similarity). {ECO:0000250}.
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=P23469-1; Sequence=Displayed;
CC Name=2; Synonyms=PTPeC, cyt-PTPe;
CC IsoId=P23469-2; Sequence=VSP_007778;
CC Name=3; Synonyms=p67;
CC IsoId=P23469-3; Sequence=VSP_038490;
CC -!- TISSUE SPECIFICITY: Expressed in giant cell tumor (osteoclastoma rich
CC in multinucleated osteoclastic cells). {ECO:0000269|PubMed:8610169}.
CC -!- INDUCTION: Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA)
CC in HL-60 cells. {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 (By similarity).
CC {ECO:0000250}.
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 and isoform 2 are phosphorylated on tyrosine residues by
CC tyrosine kinase Neu. {ECO:0000269|PubMed:10980613}.
CC -!- PTM: Isoform 1 is glycosylated. {ECO:0000269|PubMed:10980613}.
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 86 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50324.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; X54134; CAA38069.1; -; mRNA.
DR EMBL; AJ315969; CAC86583.1; -; mRNA.
DR EMBL; AK291828; BAF84517.1; -; mRNA.
DR EMBL; AL390236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49180.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49181.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49182.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49184.1; -; Genomic_DNA.
DR EMBL; BC050062; AAH50062.1; -; mRNA.
DR EMBL; U36623; AAC50324.1; ALT_SEQ; mRNA.
DR CCDS; CCDS7657.1; -. [P23469-1]
DR CCDS; CCDS7658.1; -. [P23469-2]
DR PIR; S12053; S12053.
DR RefSeq; NP_001303605.1; NM_001316676.1.
DR RefSeq; NP_001303606.1; NM_001316677.1. [P23469-1]
DR RefSeq; NP_001310283.1; NM_001323354.1. [P23469-1]
DR RefSeq; NP_006495.1; NM_006504.5. [P23469-1]
DR RefSeq; NP_569119.1; NM_130435.4. [P23469-2]
DR RefSeq; XP_005252748.1; XM_005252691.2. [P23469-1]
DR RefSeq; XP_016871957.1; XM_017016468.1. [P23469-1]
DR PDB; 2JJD; X-ray; 3.20 A; A/B/C/D/E/F=107-697.
DR PDB; 6D3F; X-ray; 2.27 A; A/B=425-700.
DR PDB; 6D4D; X-ray; 1.76 A; A/B=107-398.
DR PDB; 6D4F; X-ray; 1.91 A; A=425-700.
DR PDBsum; 2JJD; -.
DR PDBsum; 6D3F; -.
DR PDBsum; 6D4D; -.
DR PDBsum; 6D4F; -.
DR AlphaFoldDB; P23469; -.
DR SASBDB; P23469; -.
DR SMR; P23469; -.
DR BioGRID; 111755; 55.
DR IntAct; P23469; 25.
DR MINT; P23469; -.
DR STRING; 9606.ENSP00000254667; -.
DR BindingDB; P23469; -.
DR ChEMBL; CHEMBL4850; -.
DR DrugBank; DB00630; Alendronic acid.
DR DrugBank; DB01133; Tiludronic acid.
DR DEPOD; PTPRE; -.
DR GlyGen; P23469; 2 sites.
DR iPTMnet; P23469; -.
DR PhosphoSitePlus; P23469; -.
DR BioMuta; PTPRE; -.
DR DMDM; 126471; -.
DR CPTAC; CPTAC-1569; -.
DR EPD; P23469; -.
DR jPOST; P23469; -.
DR MassIVE; P23469; -.
DR MaxQB; P23469; -.
DR PaxDb; P23469; -.
DR PeptideAtlas; P23469; -.
DR PRIDE; P23469; -.
DR ProteomicsDB; 54107; -. [P23469-1]
DR ProteomicsDB; 54108; -. [P23469-2]
DR ProteomicsDB; 54109; -. [P23469-3]
DR Antibodypedia; 3004; 535 antibodies from 31 providers.
DR DNASU; 5791; -.
DR Ensembl; ENST00000254667.8; ENSP00000254667.3; ENSG00000132334.17. [P23469-1]
DR Ensembl; ENST00000306042.9; ENSP00000303350.5; ENSG00000132334.17. [P23469-2]
DR GeneID; 5791; -.
DR KEGG; hsa:5791; -.
DR MANE-Select; ENST00000254667.8; ENSP00000254667.3; NM_006504.6; NP_006495.1.
DR UCSC; uc001lkb.4; human. [P23469-1]
DR CTD; 5791; -.
DR DisGeNET; 5791; -.
DR GeneCards; PTPRE; -.
DR HGNC; HGNC:9669; PTPRE.
DR HPA; ENSG00000132334; Tissue enhanced (bone).
DR MIM; 600926; gene.
DR neXtProt; NX_P23469; -.
DR OpenTargets; ENSG00000132334; -.
DR PharmGKB; PA34014; -.
DR VEuPathDB; HostDB:ENSG00000132334; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000156570; -.
DR HOGENOM; CLU_001645_8_2_1; -.
DR InParanoid; P23469; -.
DR OMA; RKFCVHS; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P23469; -.
DR TreeFam; TF351829; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P23469; -.
DR SignaLink; P23469; -.
DR SIGNOR; P23469; -.
DR BioGRID-ORCS; 5791; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; PTPRE; human.
DR EvolutionaryTrace; P23469; -.
DR GeneWiki; PTPRE; -.
DR GenomeRNAi; 5791; -.
DR Pharos; P23469; Tbio.
DR PRO; PR:P23469; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P23469; protein.
DR Bgee; ENSG00000132334; Expressed in monocyte and 181 other tissues.
DR ExpressionAtlas; P23469; baseline and differential.
DR Genevisible; P23469; HS.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 3D-structure; Alternative initiation; Alternative promoter usage;
KW Cell membrane; Cytoplasm; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..700
FT /note="Receptor-type tyrosine-protein phosphatase epsilon"
FT /id="PRO_0000025439"
FT TOPO_DOM 20..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..394
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 426..689
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 335
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 630
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335..341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 696
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038490"
FT VAR_SEQ 1..70
FT /note="MEPLCPLLLVGFSLPLARALRGNETTADSNETTTTSGPPDPGASQPLLAWLL
FT LPLLLLLLVLLLAAYFFR -> MSNRSSFSRLTW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12121439,
FT ECO:0000303|PubMed:8618876"
FT /id="VSP_007778"
FT CONFLICT 516
FT /note="E -> D (in Ref. 2; CAC86583)"
FT /evidence="ECO:0000305"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 120..140
FT /evidence="ECO:0007829|PDB:6D4D"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:6D4D"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6D4D"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 270..281
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:6D4D"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 381..397
FT /evidence="ECO:0007829|PDB:6D4D"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:6D4F"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6D3F"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:6D4F"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 507..516
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 551..561
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 564..573
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6D4F"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 584..592
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 605..621
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 626..634
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 635..653
FT /evidence="ECO:0007829|PDB:6D4F"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:2JJD"
FT HELIX 659..666
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 676..693
FT /evidence="ECO:0007829|PDB:6D4F"
FT HELIX 694..696
FT /evidence="ECO:0007829|PDB:6D3F"
SQ SEQUENCE 700 AA; 80642 MW; D096BCADCEA65708 CRC64;
MEPLCPLLLV GFSLPLARAL RGNETTADSN ETTTTSGPPD PGASQPLLAW LLLPLLLLLL
VLLLAAYFFR FRKQRKAVVS TSDKKMPNGI LEEQEQQRVM LLSRSPSGPK KYFPIPVEHL
EEEIRIRSAD DCKQFREEFN SLPSGHIQGT FELANKEENR EKNRYPNILP NDHSRVILSQ
LDGIPCSDYI NASYIDGYKE KNKFIAAQGP KQETVNDFWR MVWEQKSATI VMLTNLKERK
EEKCHQYWPD QGCWTYGNIR VCVEDCVVLV DYTIRKFCIQ PQLPDGCKAP RLVSQLHFTS
WPDFGVPFTP IGMLKFLKKV KTLNPVHAGP IVVHCSAGVG RTGTFIVIDA MMAMMHAEQK
VDVFEFVSRI RNQRPQMVQT DMQYTFIYQA LLEYYLYGDT ELDVSSLEKH LQTMHGTTTH
FDKIGLEEEF RKLTNVRIMK ENMRTGNLPA NMKKARVIQI IPYDFNRVIL SMKRGQEYTD
YINASFIDGY RQKDYFIATQ GPLAHTVEDF WRMIWEWKSH TIVMLTEVQE REQDKCYQYW
PTEGSVTHGE ITIEIKNDTL SEAISIRDFL VTLNQPQARQ EEQVRVVRQF HFHGWPEIGI
PAEGKGMIDL IAAVQKQQQQ TGNHPITVHC SAGAGRTGTF IALSNILERV KAEGLLDVFQ
AVKSLRLQRP HMVQTLEQYE FCYKVVQDFI DIFSDYANFK
