PTPRU_HUMAN
ID PTPRU_HUMAN Reviewed; 1446 AA.
AC Q92729; A6H8L1; O00197; P78399; Q59HA4; Q5SYU4; Q5SYU5; Q92735; Q92850;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase U;
DE Short=R-PTP-U;
DE EC=3.1.3.48;
DE AltName: Full=Pancreatic carcinoma phosphatase 2;
DE Short=PCP-2;
DE AltName: Full=Protein-tyrosine phosphatase J;
DE Short=PTP-J;
DE Short=hPTP-J;
DE AltName: Full=Protein-tyrosine phosphatase pi;
DE Short=PTP pi;
DE AltName: Full=Protein-tyrosine phosphatase receptor omicron;
DE Short=PTP-RO;
DE AltName: Full=Receptor-type protein-tyrosine phosphatase psi;
DE Short=R-PTP-psi;
DE Flags: Precursor;
GN Name=PTPRU; Synonyms=FMI, PCP2, PTPRO;
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 TISSUE SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=8870675; DOI=10.1042/bj3190249;
RA Crossland S., Smith P.D., Crompton M.R.;
RT "Molecular cloning and characterization of PTP pi, a novel receptor-like
RT protein-tyrosine phosphatase.";
RL Biochem. J. 319:249-254(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=8700514;
RA Wang H.-Y., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A.;
RT "Characterization of PCP-2, a novel receptor protein tyrosine phosphatase
RT of the MAM domain family.";
RL Oncogene 12:2555-2562(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Skeletal muscle;
RX PubMed=9070223; DOI=10.1006/bbrc.1997.6004;
RA Wang B., Kishihara K., Zhang D., Hara H., Nomoto K.;
RT "Molecular cloning and characterization of a novel human receptor protein
RT tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by
RT PMA and calcium ionophore in Jurkat T lymphoma cells.";
RL Biochem. Biophys. Res. Commun. 231:77-81(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9434160; DOI=10.1016/s0378-1119(97)00420-4;
RA Avraham S., London R., Tulloch G.A., Ellis M., Fu Y., Jiang S., White R.A.,
RA Painter C., Steinberger A.A., Avraham H.;
RT "Characterization and chromosomal localization of PTPRO, a novel receptor
RT protein tyrosine phosphatase, expressed in hematopoietic stem cells.";
RL Gene 204:5-16(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RA Banville D., Masson S., L'Abbe D., Stocco R., Shen S.-H.;
RT "Cloning and expression of R-PTP-psi, a novel receptor protein tyrosine
RT phosphatase related to the homophilic binding R-PTP-kappa and -mu.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1446 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP INDUCTION.
RX PubMed=10395944; DOI=10.1016/s0167-4889(99)00064-6;
RA Wang B., Kishihara K., Zhang D., Sakamoto T., Nomoto K.;
RT "Transcriptional regulation of a receptor protein tyrosine phosphatase gene
RT hPTP-J by PKC-mediated signaling pathways in Jurkat and Molt-4 T lymphoma
RT cells.";
RL Biochim. Biophys. Acta 1450:331-340(1999).
RN [11]
RP FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, PROTEOLYTIC PROCESSING,
RP AND INDUCTION BY PHORBOL ESTER.
RX PubMed=10397721;
RA Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.;
RT "The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during
RT megakaryocyte differentiation and is associated with the c-Kit receptor.";
RL Blood 94:539-549(1999).
RN [12]
RP FUNCTION, INTERACTION WITH CTNNB1, INDUCTION, AND MUTAGENESIS OF CYS-1085
RP AND CYS-1380.
RX PubMed=12501215; DOI=10.1021/bi026095u;
RA Yan H.-X., He Y.-Q., Dong H., Zhang P., Zeng J.-Z., Cao H.-F., Wu M.-C.,
RA Wang H.-Y.;
RT "Physical and functional interaction between receptor-like protein tyrosine
RT phosphatase PCP-2 and beta-catenin.";
RL Biochemistry 41:15854-15860(2002).
RN [13]
RP FUNCTION, INTERACTION WITH CTNNB1, AND MUTAGENESIS OF CYS-1085 AND
RP CYS-1380.
RX PubMed=16574648; DOI=10.1074/jbc.m602607200;
RA Yan H.-X., Yang W., Zhang R., Chen L., Tang L., Zhai B., Liu S.-Q.,
RA Cao H.-F., Man X.-B., Wu H.-P., Wu M.-C., Wang H.-Y.;
RT "Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and
RT increases E-cadherin-dependent cell adhesion.";
RL J. Biol. Chem. 281:15423-15433(2006).
RN [14]
RP INTERACTION WITH AP3B1.
RX PubMed=17622474; DOI=10.1111/j.1745-7270.2007.00303.x;
RA Dong H., Yuan H., Jin W., Shen Y., Xu X., Wang H.-Y.;
RT "Involvement of beta3A subunit of adaptor protein-3 in intracellular
RT trafficking of receptor-like protein tyrosine phosphatase PCP-2.";
RL Acta Biochim. Biophys. Sin. 39:540-546(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-853, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853, 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 [17]
RP VARIANTS [LARGE SCALE ANALYSIS] TYR-830; TRP-835 AND CYS-856.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Tyrosine-protein phosphatase which dephosphorylates CTNNB1.
CC Regulates CTNNB1 function both in cell adhesion and signaling. May
CC function in cell proliferation and migration and play a role in the
CC maintenance of epithelial integrity. May play a role in
CC megakaryocytopoiesis. {ECO:0000269|PubMed:10397721,
CC ECO:0000269|PubMed:12501215, ECO:0000269|PubMed:16574648}.
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, ECO:0000269|PubMed:8700514};
CC -!- SUBUNIT: Forms homooligomeric complexes which mediate cell homotypic
CC adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane
CC domain) with CTNNB1; may mediate interaction with the cadherin/catenin
CC adhesion complex. Interacts with KIT. May interact with AP3B1.
CC {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12501215,
CC ECO:0000269|PubMed:16574648, ECO:0000269|PubMed:17622474, ECO:0000305}.
CC -!- INTERACTION:
CC Q92729; P10721: KIT; NbExp=2; IntAct=EBI-7052301, EBI-1379503;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:8700514}. Cell
CC membrane {ECO:0000269|PubMed:8700514}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:8700514}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q92729-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92729-2; Sequence=VSP_037082;
CC Name=3;
CC IsoId=Q92729-3; Sequence=VSP_037082, VSP_037084;
CC Name=4; Synonyms=PTPRO;
CC IsoId=Q92729-4; Sequence=VSP_037082, VSP_037083, VSP_037085;
CC -!- TISSUE SPECIFICITY: High levels in brain, pancreas, and skeletal
CC muscle; less in colon, kidney, liver, stomach, and uterus; not
CC expressed in placenta and spleen. Also detected in heart, prostate,
CC lung, thymus, testis and ovary. Ubiquitously expressed in brain.
CC Expressed by hematopoietic stem cells. {ECO:0000269|PubMed:8700514,
CC ECO:0000269|PubMed:8870675, ECO:0000269|PubMed:9070223,
CC ECO:0000269|PubMed:9434160}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung and kidney.
CC {ECO:0000269|PubMed:9434160}.
CC -!- INDUCTION: Up-regulated upon cell contact (at protein level). Down-
CC regulated by phorbol ester (at protein level) and calcium ionophore but
CC up-regulated by phorbol ester in megakaryocytic cells
CC (PubMed:10397721). {ECO:0000269|PubMed:10395944,
CC ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12501215,
CC ECO:0000269|PubMed:9070223}.
CC -!- PTM: The extracellular domain is proteolytically processed through
CC cleavage within the fibronectin type-III 4 domain (By similarity). In
CC addition to the 190 kDa full-length protein, proteolytic products of
CC 100 kDa, 80 kDa and 73 kDa are observed. {ECO:0000250,
CC ECO:0000269|PubMed:10397721}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8700514}.
CC -!- PTM: Phosphorylated on tyrosine residues upon activation of KIT with
CC stem cell factor (SCF). The 73 kDa proteolytic product is not
CC phosphorylated. {ECO:0000269|PubMed:10397721}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65016.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};
CC Sequence=CAA65832.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};
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DR EMBL; X95712; CAA65016.1; ALT_SEQ; mRNA.
DR EMBL; X97198; CAA65832.1; ALT_SEQ; mRNA.
DR EMBL; U73727; AAB51343.1; -; mRNA.
DR EMBL; U71075; AAC51938.1; -; mRNA.
DR EMBL; U60289; AAB07074.1; -; Genomic_DNA.
DR EMBL; AL645859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07651.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07652.1; -; Genomic_DNA.
DR EMBL; BC146655; AAI46656.1; -; mRNA.
DR EMBL; AB208855; BAD92092.1; -; mRNA.
DR CCDS; CCDS334.1; -. [Q92729-1]
DR CCDS; CCDS335.1; -. [Q92729-2]
DR CCDS; CCDS44098.2; -. [Q92729-4]
DR CCDS; CCDS53290.1; -. [Q92729-3]
DR PIR; JC5290; JC5290.
DR PIR; S72441; S72441.
DR RefSeq; NP_001181930.1; NM_001195001.1. [Q92729-3]
DR RefSeq; NP_005695.3; NM_005704.4. [Q92729-1]
DR RefSeq; NP_573438.3; NM_133177.3. [Q92729-4]
DR RefSeq; NP_573439.2; NM_133178.3. [Q92729-2]
DR PDB; 6SUB; X-ray; 1.72 A; A=871-1153.
DR PDB; 6SUC; X-ray; 1.97 A; A=871-1153.
DR PDBsum; 6SUB; -.
DR PDBsum; 6SUC; -.
DR AlphaFoldDB; Q92729; -.
DR SMR; Q92729; -.
DR BioGRID; 115386; 154.
DR IntAct; Q92729; 22.
DR MINT; Q92729; -.
DR STRING; 9606.ENSP00000334941; -.
DR ChEMBL; CHEMBL1961785; -.
DR DEPOD; PTPRU; -.
DR GlyGen; Q92729; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q92729; -.
DR PhosphoSitePlus; Q92729; -.
DR BioMuta; PTPRU; -.
DR DMDM; 229462800; -.
DR EPD; Q92729; -.
DR jPOST; Q92729; -.
DR MassIVE; Q92729; -.
DR MaxQB; Q92729; -.
DR PaxDb; Q92729; -.
DR PeptideAtlas; Q92729; -.
DR PRIDE; Q92729; -.
DR ProteomicsDB; 75416; -. [Q92729-1]
DR ProteomicsDB; 75417; -. [Q92729-2]
DR ProteomicsDB; 75418; -. [Q92729-3]
DR ProteomicsDB; 75419; -. [Q92729-4]
DR Antibodypedia; 31032; 42 antibodies from 17 providers.
DR DNASU; 10076; -.
DR Ensembl; ENST00000345512.7; ENSP00000334941.5; ENSG00000060656.20. [Q92729-1]
DR Ensembl; ENST00000373779.8; ENSP00000362884.3; ENSG00000060656.20. [Q92729-2]
DR Ensembl; ENST00000428026.6; ENSP00000392332.2; ENSG00000060656.20. [Q92729-3]
DR Ensembl; ENST00000460170.2; ENSP00000432906.1; ENSG00000060656.20. [Q92729-4]
DR GeneID; 10076; -.
DR KEGG; hsa:10076; -.
DR MANE-Select; ENST00000373779.8; ENSP00000362884.3; NM_133178.4; NP_573439.2. [Q92729-2]
DR UCSC; uc001bru.4; human. [Q92729-1]
DR CTD; 10076; -.
DR DisGeNET; 10076; -.
DR GeneCards; PTPRU; -.
DR HGNC; HGNC:9683; PTPRU.
DR HPA; ENSG00000060656; Low tissue specificity.
DR MIM; 602454; gene.
DR neXtProt; NX_Q92729; -.
DR OpenTargets; ENSG00000060656; -.
DR PharmGKB; PA34028; -.
DR VEuPathDB; HostDB:ENSG00000060656; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000157151; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR InParanoid; Q92729; -.
DR OMA; WEQVRSH; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q92729; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q92729; -.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR SignaLink; Q92729; -.
DR BioGRID-ORCS; 10076; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; PTPRU; human.
DR GeneWiki; PTPRU; -.
DR GenomeRNAi; 10076; -.
DR Pharos; Q92729; Tbio.
DR PRO; PR:Q92729; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92729; protein.
DR Bgee; ENSG00000060656; Expressed in endocervix and 165 other tissues.
DR Genevisible; Q92729; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; NAS:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; 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:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; NAS:UniProtKB.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Differentiation; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1446
FT /note="Receptor-type tyrosine-protein phosphatase U"
FT /id="PRO_0000371658"
FT TOPO_DOM 19..749
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..1446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..188
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 190..275
FT /note="Ig-like C2-type"
FT DOMAIN 288..383
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 386..484
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 485..591
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 592..674
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 888..1144
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1176..1439
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 771..887
FT /note="Mediates interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 833..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1085
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1380
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1053
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 1085..1091
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AUH1"
FT MOD_RES 865
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:B1AUH1"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 210..264
FT /evidence="ECO:0000255"
FT VAR_SEQ 774..783
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8700514, ECO:0000303|PubMed:9070223,
FT ECO:0000303|PubMed:9434160, ECO:0000303|Ref.9"
FT /id="VSP_037082"
FT VAR_SEQ 950
FT /note="D -> DIRINRE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9434160"
FT /id="VSP_037083"
FT VAR_SEQ 993..995
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037084"
FT VAR_SEQ 1329..1330
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9434160"
FT /id="VSP_037085"
FT VARIANT 60
FT /note="T -> N (in dbSNP:rs35332573)"
FT /id="VAR_055075"
FT VARIANT 471
FT /note="R -> L (in dbSNP:rs35745442)"
FT /id="VAR_055076"
FT VARIANT 830
FT /note="H -> Y (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035650"
FT VARIANT 835
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs558954146)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035651"
FT VARIANT 856
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs763868325)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035652"
FT VARIANT 940
FT /note="N -> S (in dbSNP:rs2235937)"
FT /id="VAR_055077"
FT MUTAGEN 1085
FT /note="C->S: Loss of phosphatase activity toward CTNNB1.
FT Loss of the inhibitory effect on CTNNB1 transcriptional
FT activity without effect on interaction with CTNNB1; when
FT associated with S-1380."
FT /evidence="ECO:0000269|PubMed:12501215,
FT ECO:0000269|PubMed:16574648"
FT MUTAGEN 1380
FT /note="C->S: No effect on phosphatase activity toward
FT CTNNB1. Loss of the inhibitory effect on CTNNB1
FT transcriptional activity without effect on interaction with
FT CTNNB1; when associated with S-1085."
FT /evidence="ECO:0000269|PubMed:12501215,
FT ECO:0000269|PubMed:16574648"
FT CONFLICT 359..360
FT /note="LT -> S (in Ref. 4; AAC51938)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="T -> A (in Ref. 4; AAC51938)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="E -> D (in Ref. 3; AAB51343)"
FT /evidence="ECO:0000305"
FT CONFLICT 840..841
FT /note="SG -> GW (in Ref. 4; AAC51938)"
FT /evidence="ECO:0000305"
FT CONFLICT 1215
FT /note="P -> A (in Ref. 5; AAB07074)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="A -> R (in Ref. 4; AAC51938)"
FT /evidence="ECO:0000305"
FT CONFLICT 1399
FT /note="M -> I (in Ref. 4; AAC51938)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436
FT /note="A -> V (in Ref. 5; AAB07074)"
FT /evidence="ECO:0000305"
FT HELIX 876..878
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 879..900
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 952..954
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 958..961
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 966..968
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 969..978
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 983..986
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1004..1009
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1012..1021
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1023..1034
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1041..1048
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1053..1056
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 1061..1073
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1081..1084
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 1091..1108
FT /evidence="ECO:0007829|PDB:6SUB"
FT STRAND 1109..1111
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 1113..1123
FT /evidence="ECO:0007829|PDB:6SUB"
FT HELIX 1131..1144
FT /evidence="ECO:0007829|PDB:6SUB"
SQ SEQUENCE 1446 AA; 162423 MW; 76F9BD6EFABE8663 CRC64;
MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT
RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL
LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI
SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT
RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS
LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ
TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP
LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG
LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDHYAYS
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES
FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA
TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA
ILEACLCGET TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL
PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV
FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC
LNGGGRSGTF CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL
EGLESR
