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   27-MAR-2024, entry version 186.
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, KDR, LYN, SRC,
CC       MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (By similarity).
CC       Plays a role in cell adhesion, migration, proliferation and
CC       differentiation (PubMed:18249142). Involved in vascular development
CC       (PubMed:12588999). May be involved in the mechanism of contact
CC       inhibition of cell growth (PubMed:12771128). Regulator of macrophage
CC       adhesion and spreading (PubMed:19268662). Positively affects cell-
CC       matrix adhesion (PubMed:12833140). Positive regulator of platelet
CC       activation and thrombosis (PubMed:19246339). Negative regulator of cell
CC       proliferation (By similarity). Negative regulator of PDGF-stimulated
CC       cell migration; through dephosphorylation of PDGFR (PubMed:12833140).
CC       Positive regulator of endothelial cell survival, as well as of VEGF-
CC       induced SRC and AKT activation; through KDR dephosphorylation (By
CC       similarity). Negative regulator of EGFR signaling pathway; through EGFR
CC       dephosphorylation (By similarity). Enhances the barrier function of
CC       epithelial junctions during reassembly (By similarity). Negatively
CC       regulates T-cell receptor (TCR) signaling (By similarity). Upon T-cell
CC       TCR activation, it is up-regulated and excluded from the immunological
CC       synapses, while upon T-cell-antigen presenting cells (APC)
CC       disengagement, it is no longer excluded and can dephosphorylate PLCG1
CC       and LAT to down-regulate prolongation of signaling (PubMed:12913111).
CC       {ECO:0000250|UniProtKB:Q12913, 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.ENSMUSP00000129592; -.
DR   GlyConnect; 2668; 5 N-Linked glycans (4 sites).
DR   GlyCosmos; Q64455; 37 sites, 5 glycans.
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; 10090-ENSMUSP00000107121; -.
DR   ProteomicsDB; 302014; -.
DR   DNASU; 19271; -.
DR   Ensembl; ENSMUST00000168621.4; ENSMUSP00000129592.4; ENSMUSG00000025314.18.
DR   GeneID; 19271; -.
DR   KEGG; mmu:19271; -.
DR   AGR; MGI:104574; -.
DR   CTD; 5795; -.
DR   MGI; MGI:104574; Ptprj.
DR   eggNOG; KOG0791; Eukaryota.
DR   GeneTree; ENSGT00940000156870; -.
DR   InParanoid; Q64455; -.
DR   OrthoDB; 5399547at2759; -.
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 81 CRISPR screens.
DR   ChiTaRS; Ptprj; mouse.
DR   PRO; PR:Q64455; -.
DR   Proteomes; UP000000589; Chromosome 2.
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: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:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA: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: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:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; 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:0050766; P:positive regulation of phagocytosis; IGI:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0010572; P:positive regulation of platelet activation; IMP:UniProtKB.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
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   CDD; cd14615; R-PTPc-J; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF5; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, H; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 4.
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;
FT                   AAK96030/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
//