PTPRJ_MOUSE
ID PTPRJ_MOUSE Reviewed; 1238 AA.
AC Q64455; Q3UH64; Q3UHL5; Q541R5; Q8CIW9; Q8K3Q2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase eta;
DE Short=Protein-tyrosine phosphatase eta;
DE Short=R-PTP-eta;
DE EC=3.1.3.48;
DE AltName: Full=HPTP beta-like tyrosine phosphatase;
DE AltName: Full=Protein-tyrosine phosphatase receptor type J;
DE Short=R-PTP-J;
DE AltName: Full=Susceptibility to colon cancer 1;
DE AltName: CD_antigen=CD148;
DE Flags: Precursor;
GN Name=Ptprj; Synonyms=Byp, Scc1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=MRL-LPR/LPR; TISSUE=Lymph node;
RX PubMed=8549806; DOI=10.1016/0014-5793(95)01415-2;
RA Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M., Yamamoto T.;
RT "Molecular cloning and characterization of Byp, a murine receptor-type
RT tyrosine phosphatase similar to human DEP-1.";
RL FEBS Lett. 378:7-14(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvSl, and BALB/cJ;
RX PubMed=12089527; DOI=10.1038/ng903;
RA Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C.,
RA Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L., Groot P.C.,
RA Lindeman J., Mooi W.J., Meijjer G.A., Scholten G., Dauwerse H., Paces V.,
RA van Zandwijk N., van Ommen G.J.B., Demant P.;
RT "Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1
RT and is frequently deleted in human cancers.";
RL Nat. Genet. 31:295-300(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129P2;
RA Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P.,
RA van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C., Ostman A.,
RA Demant P., Berns A.;
RT "Phenotypic consequences of the germ-line loss of the putative tumor
RT suppressor Ptprj (Scc1).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=8483328;
RA Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
RT "Identification of novel protein-tyrosine phosphatases in a human leukemia
RT cell line, F-36P.";
RL Leukemia 7:742-746(1993).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9823776; DOI=10.1002/jlb.64.5.692;
RA Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T.,
RA Cassady A.I., Hume D.A.;
RT "Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in
RT macrophages and is regulated by CSF-1 and LPS.";
RL J. Leukoc. Biol. 64:692-701(1998).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-1106 AND CYS-1140.
RX PubMed=12771128; DOI=10.1083/jcb.200209019;
RA Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G.,
RA Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O., Dejana E.;
RT "Contact inhibition of VEGF-induced proliferation requires vascular
RT endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148.";
RL J. Cell Biol. 161:793-804(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12913111; DOI=10.1083/jcb.200303040;
RA Lin J., Weiss A.;
RT "The tyrosine phosphatase CD148 is excluded from the immunologic synapse
RT and down-regulates prolonged T cell signaling.";
RL J. Cell Biol. 162:673-682(2003).
RN [9]
RP FUNCTION.
RX PubMed=12588999; DOI=10.1128/mcb.23.5.1817-1831.2003;
RA Takahashi T., Takahashi K., St John P.L., Fleming P.A., Tomemori T.,
RA Watanabe T., Abrahamson D.R., Drake C.J., Shirasawa T., Daniel T.O.;
RT "A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular
RT development.";
RL Mol. Cell. Biol. 23:1817-1831(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF CYS-1140.
RX PubMed=12833140; DOI=10.1038/sj.onc.1206652;
RA Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.;
RT "The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated
RT cell migration and cell-matrix adhesion.";
RL Oncogene 22:4175-4185(2003).
RN [11]
RP FUNCTION.
RX PubMed=18249142; DOI=10.1016/j.immuni.2007.11.024;
RA Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.;
RT "Structurally distinct phosphatases CD45 and CD148 both regulate B cell and
RT macrophage immunoreceptor signaling.";
RL Immunity 28:183-196(2008).
RN [12]
RP FUNCTION.
RX PubMed=19246339; DOI=10.1182/blood-2008-08-174318;
RA Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y.,
RA Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W.,
RA Weiss A., Watson S.P.;
RT "The tyrosine phosphatase CD148 is an essential positive regulator of
RT platelet activation and thrombosis.";
RL Blood 113:4942-4954(2009).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19268662; DOI=10.1016/j.yexcr.2009.02.023;
RA Dave R.K., Hume D.A., Elsegood C., Kellie S.;
RT "CD148/DEP-1 association with areas of cytoskeletal organisation in
RT macrophages.";
RL Exp. Cell Res. 315:1734-1744(2009).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-313; ASN-317 AND
RP ASN-538.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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: Tyrosine phosphatase which dephosphorylates or contributes to
CC the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET, KDR, LYN, SRC,
CC MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell
CC adhesion, migration, proliferation and differentiation. Involved in
CC vascular development. May be involved in the mechanism of contact
CC inhibition of cell growth. Regulator of macrophage adhesion and
CC spreading. Positively affects cell-matrix adhesion. Positive regulator
CC of platelet activation and thrombosis. Negative regulator of cell
CC proliferation. Negative regulator of PDGF-stimulated cell migration;
CC through dephosphorylation of PDGFR. Positive regulator of endothelial
CC cell survival, as well as of VEGF-induced SRC and AKT activation;
CC through KDR dephosphorylation. Negative regulator of EGFR signaling
CC pathway; through EGFR dephosphorylation. Enhances the barrier function
CC of epithelial junctions during reassembly. Negatively regulates T-cell
CC receptor (TCR) signaling. Upon T-cell TCR activation, it is up-
CC regulated and excluded from the immunological synapses, while upon T-
CC cell-antigen presenting cells (APC) disengagement, it is no longer
CC excluded and can dephosphorylate PLCG1 and LAT to down-regulate
CC prolongation of signaling. {ECO:0000269|PubMed:12588999,
CC ECO:0000269|PubMed:12771128, ECO:0000269|PubMed:12833140,
CC ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:18249142,
CC ECO:0000269|PubMed:19246339, ECO:0000269|PubMed:19268662}.
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. Interacts with CTNNB1 (phosphorylated) and JUP
CC (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with
CC GAB1 and GRB2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell projection, ruffle membrane. Cell junction. Note=After T-
CC cell stimulation, it is temporarily excluded from immunological
CC synapses. Found at cell borders.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, kidney, spleen
CC and intestine, and at lower levels in liver, lung, thymus and heart.
CC Expressed at a high level in the myeloid cell line FDC-P2, and at a
CC lower level in the pre-B lymphoid cell line WEHI-231 and the T
CC hybridoma cell line HB21.7.31. Not expressed in the fibroblast cell
CC line NIH3T3 or the erythroid cell line F5-5. Expressed in macrophages.
CC {ECO:0000269|PubMed:8483328, ECO:0000269|PubMed:8549806,
CC ECO:0000269|PubMed:9823776}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 11.5 dpc in presumptive macrophages
CC concentrated in the liver and scattered throughout the embryonic
CC mesenchyme. Expressed at 11.5 and 12.5 dpc in the developing eye and in
CC the ganglia and processes of cranial and spinal nerves constituting the
CC PNS. {ECO:0000269|PubMed:9823776}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; D45212; BAA08146.1; -; mRNA.
DR EMBL; AY038877; AAN11409.1; -; Genomic_DNA.
DR EMBL; AY038861; AAN11409.1; JOINED; Genomic_DNA.
DR EMBL; AY038891; AAK96030.1; -; mRNA.
DR EMBL; AY039232; AAK98640.1; -; mRNA.
DR EMBL; DQ133576; ABA07808.1; -; mRNA.
DR EMBL; AK147318; BAE27842.1; -; mRNA.
DR EMBL; AK147556; BAE27993.1; -; mRNA.
DR CCDS; CCDS50630.1; -.
DR PIR; S68700; S68700.
DR RefSeq; NP_033008.3; NM_008982.5.
DR AlphaFoldDB; Q64455; -.
DR SMR; Q64455; -.
DR BioGRID; 202499; 8.
DR IntAct; Q64455; 1.
DR STRING; 10090.ENSMUSP00000107121; -.
DR GlyConnect; 2668; 5 N-Linked glycans (4 sites).
DR GlyGen; Q64455; 37 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q64455; -.
DR PhosphoSitePlus; Q64455; -.
DR EPD; Q64455; -.
DR MaxQB; Q64455; -.
DR PaxDb; Q64455; -.
DR PRIDE; Q64455; -.
DR ProteomicsDB; 302014; -.
DR DNASU; 19271; -.
DR GeneID; 19271; -.
DR KEGG; mmu:19271; -.
DR CTD; 5795; -.
DR MGI; MGI:104574; Ptprj.
DR eggNOG; KOG0791; Eukaryota.
DR InParanoid; Q64455; -.
DR OrthoDB; 411281at2759; -.
DR BRENDA; 3.1.3.48; 3474.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR Reactome; R-MMU-9706369; Negative regulation of FLT3.
DR BioGRID-ORCS; 19271; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Ptprj; mouse.
DR PRO; PR:Q64455; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64455; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0070097; F:delta-catenin binding; ISO:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0007596; P:blood coagulation; IMP:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:ARUK-UCL.
DR GO; GO:0042593; P:glucose homeostasis; IMP:CACAO.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:CACAO.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; IMP:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IMP:CACAO.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IGI:ARUK-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:ARUK-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0010572; P:positive regulation of platelet activation; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 6.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041201; PTPRJ_TM.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 4.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1238
FT /note="Receptor-type tyrosine-protein phosphatase eta"
FT /id="PRO_0000025445"
FT TOPO_DOM 29..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..1238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..122
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 170..266
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 270..358
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 359..443
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 444..527
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 528..621
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..718
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 717..803
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 942..1199
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1140
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1140..1146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12913"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1106
FT /note="D->A: Substrate trapping with much higher affinity
FT for substrate."
FT /evidence="ECO:0000269|PubMed:12771128"
FT MUTAGEN 1140
FT /note="C->S: Catalytically inactive and substrate trapping
FT with higher affinity for substrate."
FT /evidence="ECO:0000269|PubMed:12771128,
FT ECO:0000269|PubMed:12833140"
FT CONFLICT 175
FT /note="S -> T (in Ref. 1; BAA08146 and 2; AAK96030/
FT AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> P (in Ref. 2; AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="V -> A (in Ref. 2; AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="Q -> H (in Ref. 4; BAE27842)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="A -> T (in Ref. 2; AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="P -> S (in Ref. 2; AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="D -> E (in Ref. 2; AAK98640)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="Y -> D (in Ref. 2; AAN11409)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="E -> K (in Ref. 2; AAN11409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1238 AA; 136769 MW; E525D346A2C60335 CRC64;
MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV SPTSVLLTWK
HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY TFSIISVTTN ETLNKTITTE
PWPVSDLHVT SVGVTQARLT WSNANGTASY RMLIEELTTH SSVNISGLKP GTNNSFAFPE
SNETQADFAV AEEVPDANGT KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD
TQYNATIYSQ AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV
YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL QVYTSPDQVS
DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS TGNQSYMVED LKPGTSYHFE
IIPRGPDGTE GLSSTVNGST DPSAVTDIRV VNISTTEMQL EWQNTDDASG YTYHLVLESK
SGSIIRTNSS QKWITVGSLT PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT
TTTAAIRWKN EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT
QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG FELGVRSDSW
DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG KMALPAQNIC TTGITDPPTP
DGSPNITSVS HNSVKVKFSG FEASHGPIKA YAVILTTGEA AQPSADVLKY TYEDFKRGAS
DTYVTYLIRI EEKGQSQGLS EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT
YNLQNDGLIN GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK
RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK LIGISLPKYT
AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY MPGYHSKKDF IATQGPLPNT
LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI
RDFVVKNMQN SESHPLRQFH FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC
SAGVGRTGTF IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII
RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA
