PTPRJ_HUMAN
ID PTPRJ_HUMAN Reviewed; 1337 AA.
AC Q12913; Q15255; Q6P4H4; Q8NHM2; Q9UDA9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 215.
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=Density-enhanced phosphatase 1;
DE Short=DEP-1;
DE AltName: Full=HPTP eta;
DE AltName: Full=Protein-tyrosine phosphatase receptor type J;
DE Short=R-PTP-J;
DE AltName: CD_antigen=CD148;
DE Flags: Precursor;
GN Name=PTPRJ; Synonyms=DEP1;
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), AND VARIANT ASP-872.
RX PubMed=7937872; DOI=10.1073/pnas.91.21.9680;
RA Oestman A., Yang Q., Tonks N.K.;
RT "Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is
RT enhanced with increasing cell density.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-872.
RX PubMed=7994032;
RA Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.;
RT "Molecular cloning, characterization, and chromosomal localization of a
RT novel protein-tyrosine phosphatase, HPTP eta.";
RL Blood 84:4186-4194(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, AND VARIANTS CYS-214; PRO-276
RP AND ASP-872.
RC TISSUE=Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Leukemia;
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 [7]
RP PROTEIN SEQUENCE OF 36-49; 485-502 AND 723-739, FUNCTION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9531590;
RA de la Fuente-Garcia M.A., Nicolas J.M., Freed J.H., Palou E., Thomas A.P.,
RA Vilella R., Vives J., Gaya A.;
RT "CD148 is a membrane protein tyrosine phosphatase present in all
RT hematopoietic lineages and is involved in signal transduction on
RT lymphocytes.";
RL Blood 91:2800-2809(1998).
RN [8]
RP FUNCTION.
RX PubMed=9780142;
RA Tangye S.G., Wu J., Aversa G., de Vries J.E., Lanier L.L., Phillips J.H.;
RT "Negative regulation of human T cell activation by the receptor-type
RT protein tyrosine phosphatase CD148.";
RL J. Immunol. 161:3803-3807(1998).
RN [9]
RP FUNCTION.
RX PubMed=10821867; DOI=10.1074/jbc.275.21.16219;
RA Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E.,
RA Vilella R., Bohmer F., Ostman A.;
RT "Site-selective dephosphorylation of the platelet-derived growth factor
RT beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1.";
RL J. Biol. Chem. 275:16219-16226(2000).
RN [10]
RP FUNCTION.
RX PubMed=11259588; DOI=10.1128/mcb.21.7.2393-2403.2001;
RA Baker J.E., Majeti R., Tangye S.G., Weiss A.;
RT "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor
RT signal transduction is associated with reduced LAT and phospholipase
RT Cgamma1 phosphorylation.";
RL Mol. Cell. Biol. 21:2393-2403(2001).
RN [11]
RP FUNCTION.
RX PubMed=12062403; DOI=10.1016/s0014-5793(02)02570-x;
RA Persson C., Engstrom U., Mowbray S.L., Ostman A.;
RT "Primary sequence determinants responsible for site-selective
RT dephosphorylation of the PDGF beta-receptor by the receptor-like protein
RT tyrosine phosphatase DEP-1.";
RL FEBS Lett. 517:27-31(2002).
RN [12]
RP FUNCTION, INTERACTION WITH CTNNB1 AND JUP, MUTAGENESIS OF ASP-1205 AND
RP CYS-1239, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12370829; DOI=10.1038/sj.onc.1205858;
RA Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.;
RT "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts
RT with p120(ctn).";
RL Oncogene 21:7067-7076(2002).
RN [13]
RP FUNCTION, INTERACTION WITH CTNNB1; GRB2; GAB1 AND JUP, AND MUTAGENESIS OF
RP ASP-1205 AND CYS-1239.
RX PubMed=12475979; DOI=10.1074/jbc.m210656200;
RA Palka H.L., Park M., Tonks N.K.;
RT "Hepatocyte growth factor receptor tyrosine kinase met is a substrate of
RT the receptor protein-tyrosine phosphatase DEP-1.";
RL J. Biol. Chem. 278:5728-5735(2003).
RN [14]
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 [15]
RP FUNCTION.
RX PubMed=14709717; DOI=10.1242/jcs.00879;
RA Kellie S., Craggs G., Bird I.N., Jones G.E.;
RT "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements,
RT aberrant cell-substratum interactions and a reduction in cell
RT proliferation.";
RL J. Cell Sci. 117:609-618(2004).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND
RP ASN-396.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ASP-1205.
RX PubMed=16778204; DOI=10.1158/0008-5472.can-06-0228;
RA Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M.,
RA Carlomagno F., Santoro M., Fusco A.;
RT "The receptor-type protein tyrosine phosphatase J antagonizes the
RT biochemical and biological effects of RET-derived oncoproteins.";
RL Cancer Res. 66:6280-6287(2006).
RN [18]
RP FUNCTION.
RX PubMed=16682945; DOI=10.1038/sj.onc.1209647;
RA Balavenkatraman K.K., Jandt E., Friedrich K., Kautenburger T.,
RA Pool-Zobel B.L., Ostman A., Bohmer F.D.;
RT "DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of
RT colon carcinoma cells and is upregulated by protective nutrients.";
RL Oncogene 25:6319-6324(2006).
RN [19]
RP FUNCTION, MUTAGENESIS OF ASP-1205, AND SUBCELLULAR LOCATION.
RX PubMed=18348712; DOI=10.1042/bj20071317;
RA Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M.,
RA Takahashi T.;
RT "The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit
RT of phosphoinositide 3-kinase.";
RL Biochem. J. 413:193-200(2008).
RN [20]
RP ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=18603590; DOI=10.1093/nar/gkn391;
RA Karagyozov L., Godfrey R., Boehmer S.A., Petermann A., Hoelters S.,
RA Ostman A., Boehmer F.D.;
RT "The structure of the 5'-end of the protein-tyrosine phosphatase PTPRJ mRNA
RT reveals a novel mechanism for translation attenuation.";
RL Nucleic Acids Res. 36:4443-4453(2008).
RN [21]
RP SUBUNIT.
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 [22]
RP FUNCTION IN EGFR REGULATION, MUTAGENESIS OF ASP-1205 AND CYS-1239, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
RA Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
RA Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
RT "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
RT controlling EGFR endocytosis.";
RL Curr. Biol. 19:1788-1798(2009).
RN [23]
RP FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239, AND SUBCELLULAR LOCATION.
RX PubMed=19332538; DOI=10.1074/jbc.m901901200;
RA Sallee J.L., Burridge K.;
RT "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction
RT proteins and enhances barrier function of epithelial cells.";
RL J. Biol. Chem. 284:14997-15006(2009).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF LYS-1016 AND ASP-1205.
RX PubMed=19494114; DOI=10.1074/jbc.m109.002758;
RA Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P.,
RA Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.;
RT "Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS
RT pathway by direct dephosphorylation of ERK1/2 kinases.";
RL J. Biol. Chem. 284:22048-22058(2009).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [26]
RP FUNCTION, AND MUTAGENESIS OF ASP-1205 AND CYS-1239.
RX PubMed=18936167; DOI=10.1128/mcb.01374-08;
RA Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
RT "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and
RT endothelial cell survival.";
RL Mol. Cell. Biol. 29:241-253(2009).
RN [27]
RP FUNCTION.
RX PubMed=21091576; DOI=10.1111/j.1750-3639.2010.00464.x;
RA Petermann A., Haase D., Wetzel A., Balavenkatraman K.K., Tenev T.,
RA Guhrs K.H., Friedrich S., Nakamura M., Mawrin C., Bohmer F.D.;
RT "Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma
RT cell motility.";
RL Brain Pathol. 21:405-418(2011).
RN [28]
RP FUNCTION.
RX PubMed=19922411; DOI=10.1042/bj20091413;
RA Omerovic J., Clague M.J., Prior I.A.;
RT "Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative
RT regulators of PKB/Akt activation in Ras-mutated cancer cells.";
RL Biochem. J. 426:65-72(2010).
RN [29]
RP FUNCTION, INTERACTION WITH FLT3, AND MUTAGENESIS OF ASP-1205 AND CYS-1239.
RX PubMed=21262971; DOI=10.1074/jbc.m110.205021;
RA Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
RA Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
RA Muller J.P.;
RT "Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3
RT signaling.";
RL J. Biol. Chem. 286:10918-10929(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
RP ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=33296397; DOI=10.1371/journal.pone.0240498;
RA Karagyozov L., Grozdanov P.N., Boehmer F.D.;
RT "The translation attenuating arginine-rich sequence in the extended signal
RT peptide of the protein-tyrosine phosphatase PTPRJ/DEP1 is conserved in
RT mammals.";
RL PLoS ONE 15:e0240498-e0240498(2020).
RN [32]
RP STRUCTURE BY NMR OF 366-456.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fourth FN3 domain of human receptor-type
RT tyrosine-protein phosphatase eta.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [33]
RP VARIANTS PRO-276; GLN-326 AND ASP-872.
RX PubMed=15378013; DOI=10.1038/sj.onc.1207766;
RA Iuliano R., Le Pera I., Cristofaro C., Baudi F., Arturi F., Pallante P.,
RA Martelli M.L., Trapasso F., Chiariotti L., Fusco A.;
RT "The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid
RT carcinogenesis.";
RL Oncogene 23:8432-8438(2004).
CC -!- FUNCTION: Tyrosine phosphatase which dephosphorylates or contributes to
CC the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant
CC MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and
CC PIK3R2. Plays a role in cell adhesion, migration, proliferation and
CC differentiation. Involved in vascular development. Regulator of
CC macrophage adhesion and spreading. Positively affects cell-matrix
CC adhesion. Positive regulator of platelet activation and thrombosis.
CC Negative regulator of cell proliferation. Negative regulator of PDGF-
CC stimulated cell migration; through dephosphorylation of PDGFR. Positive
CC regulator of endothelial cell survival, as well as of VEGF-induced SRC
CC and AKT activation; through KDR dephosphorylation. Negative regulator
CC of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the
CC barrier function of epithelial junctions during reassembly. Negatively
CC regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation,
CC it is up-regulated and excluded from the immunological synapses, while
CC upon T-cell-antigen presenting cells (APC) disengagement, it is no
CC longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate
CC prolongation of signaling. {ECO:0000269|PubMed:10821867,
CC ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403,
CC ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979,
CC ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717,
CC ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:16778204,
CC ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167,
CC ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114,
CC ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411,
CC ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971,
CC ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.
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. {ECO:0000269|PubMed:12370829,
CC ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:19246339,
CC ECO:0000269|PubMed:21262971}.
CC -!- INTERACTION:
CC Q12913; P35222: CTNNB1; NbExp=2; IntAct=EBI-2264500, EBI-491549;
CC Q12913; O60716: CTNND1; NbExp=5; IntAct=EBI-2264500, EBI-701927;
CC Q12913; P04626: ERBB2; NbExp=2; IntAct=EBI-2264500, EBI-641062;
CC Q12913; P17948: FLT1; NbExp=2; IntAct=EBI-2264500, EBI-1026718;
CC Q12913; Q13480: GAB1; NbExp=2; IntAct=EBI-2264500, EBI-517684;
CC Q12913; P10912: GHR; NbExp=2; IntAct=EBI-2264500, EBI-286316;
CC Q12913; P35968: KDR; NbExp=4; IntAct=EBI-2264500, EBI-1005487;
CC Q12913; P28482: MAPK1; NbExp=7; IntAct=EBI-2264500, EBI-959949;
CC Q12913; P27361: MAPK3; NbExp=5; IntAct=EBI-2264500, EBI-73995;
CC Q12913; P08581: MET; NbExp=5; IntAct=EBI-2264500, EBI-1039152;
CC Q12913; P09619: PDGFRB; NbExp=4; IntAct=EBI-2264500, EBI-641237;
CC Q12913; Q02763: TEK; NbExp=2; IntAct=EBI-2264500, EBI-2257090;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell projection, ruffle membrane {ECO:0000250}. Cell junction.
CC Note=After T-cell stimulation, it is temporarily excluded from
CC immunological synapses.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Comment=Isoform 1 and isoform 3 result from alternative initiation of
CC translation within the same 5' exon but produce the same functional
CC protein following cleavage of their respective signal peptides
CC (PubMed:18603590). Alternative initiation is probably a conserved
CC mechanism in mammals to regulate the overall expression of that
CC functional protein (PubMed:18603590, PubMed:33296397).
CC {ECO:0000269|PubMed:18603590, ECO:0000305|PubMed:33296397};
CC Name=1;
CC IsoId=Q12913-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12913-2; Sequence=VSP_043652, VSP_043653;
CC Name=3;
CC IsoId=Q12913-3; Sequence=VSP_060928;
CC -!- TISSUE SPECIFICITY: Expressed in the promyelocytic cell line HL-60, the
CC granulocyte-macrophage colony-stimulating factor-dependent leukemic
CC cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell
CC line F-36E. Expressed predominantly in epithelial cells and
CC lymphocytes. Enhanced expression at high cell density.
CC {ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:8483328,
CC ECO:0000269|PubMed:9531590}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9531590}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPRJID41932ch11p11.html";
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DR EMBL; U10886; AAB36687.1; -; mRNA.
DR EMBL; D37781; BAA07035.1; -; mRNA.
DR EMBL; AC026975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063417; AAH63417.1; -; mRNA.
DR EMBL; AH011675; AAM69432.1; -; Genomic_DNA.
DR CCDS; CCDS44596.1; -. [Q12913-2]
DR CCDS; CCDS7945.1; -. [Q12913-1]
DR PIR; I38670; I38670.
DR RefSeq; NP_001091973.1; NM_001098503.1. [Q12913-2]
DR RefSeq; NP_002834.3; NM_002843.3. [Q12913-1]
DR PDB; 2CFV; X-ray; 2.50 A; A=1019-1311.
DR PDB; 2DLE; NMR; -; A=366-456.
DR PDB; 2NZ6; X-ray; 2.30 A; A=1019-1311.
DR PDBsum; 2CFV; -.
DR PDBsum; 2DLE; -.
DR PDBsum; 2NZ6; -.
DR AlphaFoldDB; Q12913; -.
DR SMR; Q12913; -.
DR BioGRID; 111759; 94.
DR IntAct; Q12913; 81.
DR MINT; Q12913; -.
DR STRING; 9606.ENSP00000400010; -.
DR BindingDB; Q12913; -.
DR ChEMBL; CHEMBL3692; -.
DR DEPOD; PTPRJ; -.
DR GlyConnect; 1707; 7 N-Linked glycans (4 sites).
DR GlyGen; Q12913; 40 sites, 7 N-linked glycans (4 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; Q12913; -.
DR PhosphoSitePlus; Q12913; -.
DR BioMuta; PTPRJ; -.
DR DMDM; 166899088; -.
DR EPD; Q12913; -.
DR jPOST; Q12913; -.
DR MassIVE; Q12913; -.
DR MaxQB; Q12913; -.
DR PaxDb; Q12913; -.
DR PeptideAtlas; Q12913; -.
DR PRIDE; Q12913; -.
DR ProteomicsDB; 59024; -. [Q12913-1]
DR ProteomicsDB; 59025; -. [Q12913-2]
DR Antibodypedia; 1162; 491 antibodies from 34 providers.
DR DNASU; 5795; -.
DR Ensembl; ENST00000418331.7; ENSP00000400010.2; ENSG00000149177.14. [Q12913-1]
DR Ensembl; ENST00000440289.6; ENSP00000409733.2; ENSG00000149177.14. [Q12913-2]
DR GeneID; 5795; -.
DR KEGG; hsa:5795; -.
DR MANE-Select; ENST00000418331.7; ENSP00000400010.2; NM_002843.4; NP_002834.3.
DR UCSC; uc001ngo.5; human. [Q12913-1]
DR CTD; 5795; -.
DR DisGeNET; 5795; -.
DR GeneCards; PTPRJ; -.
DR HGNC; HGNC:9673; PTPRJ.
DR HPA; ENSG00000149177; Low tissue specificity.
DR MalaCards; PTPRJ; -.
DR MIM; 600925; gene.
DR neXtProt; NX_Q12913; -.
DR OpenTargets; ENSG00000149177; -.
DR PharmGKB; PA34018; -.
DR VEuPathDB; HostDB:ENSG00000149177; -.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000156870; -.
DR HOGENOM; CLU_001541_2_0_1; -.
DR InParanoid; Q12913; -.
DR OMA; WKNNDTA; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q12913; -.
DR TreeFam; TF351926; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q12913; -.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR SignaLink; Q12913; -.
DR SIGNOR; Q12913; -.
DR BioGRID-ORCS; 5795; 15 hits in 1082 CRISPR screens.
DR ChiTaRS; PTPRJ; human.
DR EvolutionaryTrace; Q12913; -.
DR GeneWiki; PTPRJ; -.
DR GenomeRNAi; 5795; -.
DR Pharos; Q12913; Tbio.
DR PRO; PR:Q12913; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q12913; protein.
DR Bgee; ENSG00000149177; Expressed in ileal mucosa and 180 other tissues.
DR ExpressionAtlas; Q12913; baseline and differential.
DR Genevisible; Q12913; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
DR GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:ARUK-UCL.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:ARUK-UCL.
DR GO; GO:0060242; P:contact inhibition; NAS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
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; 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; IDA:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; ISS:ARUK-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:ARUK-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 7.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00665; -.
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; 2.
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 3D-structure; Alternative initiation; Alternative splicing; Cell junction;
KW Cell membrane; Cell projection; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1337
FT /note="Receptor-type tyrosine-protein phosphatase eta"
FT /id="PRO_0000025444"
FT TOPO_DOM 36..975
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 997..1337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 121..209
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 207..291
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 271..364
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 368..456
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 457..541
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 542..623
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 625..720
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 721..817
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 816..902
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1041..1298
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 66..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1239
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1239..1245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
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 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1
FT /note="M -> MSPGKPGAGGAGTRRTGWRRRRRRRRQEAATTVPGLGRTAGPDSRVR
FT GTFQGARGM (in isoform 3)"
FT /id="VSP_060928"
FT VAR_SEQ 539
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043652"
FT VAR_SEQ 540..1337
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043653"
FT VARIANT 214
FT /note="R -> C (in a colon cancer sample; somatic mutation;
FT dbSNP:rs121434507)"
FT /evidence="ECO:0000269|PubMed:12089527"
FT /id="VAR_015905"
FT VARIANT 276
FT /note="Q -> P (in a colon cancer sample; somatic mutation;
FT dbSNP:rs1566734)"
FT /evidence="ECO:0000269|PubMed:12089527,
FT ECO:0000269|PubMed:15378013"
FT /id="VAR_015906"
FT VARIANT 293
FT /note="A -> T (in dbSNP:rs2229701)"
FT /id="VAR_038414"
FT VARIANT 326
FT /note="R -> Q (in dbSNP:rs1503185)"
FT /evidence="ECO:0000269|PubMed:15378013"
FT /id="VAR_024582"
FT VARIANT 372
FT /note="V -> I (in dbSNP:rs2229703)"
FT /id="VAR_038415"
FT VARIANT 872
FT /note="E -> D (in dbSNP:rs4752904)"
FT /evidence="ECO:0000269|PubMed:12089527,
FT ECO:0000269|PubMed:15378013, ECO:0000269|PubMed:7937872,
FT ECO:0000269|PubMed:7994032"
FT /id="VAR_038416"
FT VARIANT 1235
FT /note="I -> T (in dbSNP:rs11039554)"
FT /id="VAR_038417"
FT MUTAGEN 1016
FT /note="K->A: 80% decrease in interaction with MAPK1 and
FT MAPK3."
FT /evidence="ECO:0000269|PubMed:19494114"
FT MUTAGEN 1205
FT /note="D->A: Substrate trapping with much higher affinity
FT for substrate."
FT /evidence="ECO:0000269|PubMed:12370829,
FT ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:16778204,
FT ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167,
FT ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114,
FT ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21262971"
FT MUTAGEN 1239
FT /note="C->S: Catalytically inactive and substrate trapping
FT with higher affinity for substrate."
FT /evidence="ECO:0000269|PubMed:12370829,
FT ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:18936167,
FT ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19836242,
FT ECO:0000269|PubMed:21262971"
FT CONFLICT 261
FT /note="G -> D (in Ref. 1; AAB36687)"
FT /evidence="ECO:0000305"
FT CONFLICT 918..929
FT /note="YNGKLEPLGSYR -> LQWEAGTSGLLP (in Ref. 2; BAA07035)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="K -> Q (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="P -> E (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="V -> I (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:2DLE"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:2DLE"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:2DLE"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:2DLE"
FT STRAND 429..440
FT /evidence="ECO:0007829|PDB:2DLE"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:2DLE"
FT HELIX 1023..1047
FT /evidence="ECO:0007829|PDB:2NZ6"
FT TURN 1048..1054
FT /evidence="ECO:0007829|PDB:2NZ6"
FT TURN 1058..1061
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1063..1068
FT /evidence="ECO:0007829|PDB:2NZ6"
FT TURN 1078..1080
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1087..1089
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1090..1093
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1096..1100
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1108..1113
FT /evidence="ECO:0007829|PDB:2NZ6"
FT TURN 1117..1119
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1120..1129
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1134..1138
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1159..1161
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1164..1173
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1175..1186
FT /evidence="ECO:0007829|PDB:2NZ6"
FT TURN 1187..1189
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1192..1200
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1212..1225
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1235..1243
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1244..1261
FT /evidence="ECO:0007829|PDB:2NZ6"
FT STRAND 1262..1265
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1267..1275
FT /evidence="ECO:0007829|PDB:2NZ6"
FT HELIX 1285..1302
FT /evidence="ECO:0007829|PDB:2NZ6"
SQ SEQUENCE 1337 AA; 145941 MW; B44F4343FC8FD1B4 CRC64;
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT VATGENGITQ
ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE QGSNGTDGAS QKTPSSTGPS
PVFDIKAVSI SPTNVILTWK SNDTAASEYK YVVKHKMENE KTITVVHQPW CNITGLRPAT
SYVFSITPGI GNETWGDPRV IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL
ESIGSHEELT QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA NGTEGQPQAI
EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK IHVAGETDSS NLNVSEPRAV
IPGLRSSTFY NITVCPVLGD IEGTPGFLQV HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE
SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP
SAVFDIHVVY VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD ASPTYSYCLL
IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ VGDGIKSLEP GRKSFCTDPA
SMASFDCEVV PKEPALVLKW TCPPGANAGF ELEVSSGAWN NATHLESCSS ENGTEYRTEV
TYLNFSTSYN ISITTVSCGK MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF
EASHGPIKAY AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG AESYVSFSRY
SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR KDAKNNEVSF SQIKPKKSKL
IRVENFEAYF KKQQADSNCG FAEEYEDLKL VGISQPKYAA ELAENRGKNR YNNVLPYDIS
RVKLSVQTHS TDDYINANYM PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK
CVEQGRTKCE EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI AIDRLIYQIE
NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR SQKDSKVDLI YQNTTAMTIY
ENLAPVTTFG KTNGYIA
