ID   PTPRB_MOUSE             Reviewed;        1998 AA.
AC   B2RU80; Q3UGZ7; Q8CIW2;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase beta;
DE            Short=Protein-tyrosine phosphatase beta;
DE            Short=R-PTP-beta;
DE            EC=3.1.3.48;
DE   AltName: Full=Vascular endothelial protein tyrosine phosphatase;
DE            Short=VE-PTP;
DE   Flags: Precursor;
GN   Name=Ptprb;
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], FUNCTION, INTERACTION WITH CDH5, DOMAIN, AND
RP   MUTAGENESIS OF ARG-1911.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=12234928; DOI=10.1093/emboj/cdf497;
RA   Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G.,
RA   Golding M., Shima D.T., Deutsch U., Vestweber D.;
RT   "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of
RT   phosphorylation and cell contacts.";
RL   EMBO J. 21:4885-4895(2002).
RN   [2]
RP   ERRATUM OF PUBMED:12234928.
RX   DOI=10.1093/sj.emboj.cdf497;
RA   Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G.,
RA   Golding M., Shima D.T., Deutsch U., Vestweber D.;
RL   EMBO J. 24:3158-3158(2005).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH TEK, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=10557082; DOI=10.1038/sj.onc.1202992;
RA   Fachinger G., Deutsch U., Risau W.;
RT   "Functional interaction of vascular endothelial-protein-tyrosine
RT   phosphatase with the angiopoietin receptor Tie-2.";
RL   Oncogene 18:5948-5953(1999).
RN   [7]
RP   SUBUNIT.
RX   PubMed=11564762; DOI=10.1083/jcb.200104122;
RA   Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J.,
RA   Brown S.A., Brown L.Y., Mason C.A., Grumet M.;
RT   "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in
RT   cerebellar granule cell development.";
RL   J. Cell Biol. 154:1259-1273(2001).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16514057; DOI=10.1182/blood-2006-01-0141;
RA   Bauemer S., Keller L., Holtmann A., Funke R., August B., Gamp A.,
RA   Wolburg H., Wolburg-Buchholz K., Deutsch U., Vestweber D.;
RT   "Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP)
RT   activity is required for blood vessel development.";
RL   Blood 107:4754-4762(2006).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=17360632; DOI=10.1073/pnas.0611510104;
RA   Dominguez M.G., Hughes V.C., Pan L., Simmons M., Daly C., Anderson K.,
RA   Noguera-Troise I., Murphy A.J., Valenzuela D.M., Davis S., Thurston G.,
RA   Yancopoulos G.D., Gale N.W.;
RT   "Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo
RT   vasculogenesis but die embryonically because of defects in angiogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:3243-3248(2007).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH CDH5.
RX   PubMed=19015309; DOI=10.1084/jem.20080406;
RA   Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R.,
RA   Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O.,
RA   Bixel M.G., Butz S., Vestweber D.;
RT   "VE-PTP maintains the endothelial barrier via plakoglobin and becomes
RT   dissociated from VE-cadherin by leukocytes and by VEGF.";
RL   J. Exp. Med. 205:2929-2945(2008).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH TEK.
RX   PubMed=19451274; DOI=10.1083/jcb.200811159;
RA   Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F.,
RA   Deutsch U., Nottebaum A.F., Vestweber D.;
RT   "VE-PTP controls blood vessel development by balancing Tie-2 activity.";
RL   J. Cell Biol. 185:657-671(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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).
RN   [13]
RP   INTERACTION WITH FYN AND GRB2, PHOSPHORYLATION AT TYR-1982, AND MUTAGENESIS
RP   OF TYR-1982.
RX   PubMed=20398064; DOI=10.1111/j.1365-2443.2010.01398.x;
RA   Murata Y., Mori M., Kotani T., Supriatna Y., Okazawa H., Kusakari S.,
RA   Saito Y., Ohnishi H., Matozaki T.;
RT   "Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine
RT   phosphatases and their complex formations with Grb2 or Fyn.";
RL   Genes Cells 15:513-524(2010).
CC   -!- FUNCTION: Plays an important role in blood vessel remodeling and
CC       angiogenesis. Not necessary for the initial formation of blood vessels,
CC       but is essential for their maintenance and remodeling. Can induce
CC       dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2.
CC       Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a
CC       negative regulator of TIE2, and controls TIE2 driven endothelial cell
CC       proliferation, which in turn affects blood vessel remodeling during
CC       embryonic development and determines blood vessel size during perinatal
CC       growth. Essential for the maintenance of endothelial cell contact
CC       integrity and for the adhesive function of VE-cadherin in endothelial
CC       cells and this requires the presence of plakoglobin.
CC       {ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:12234928,
CC       ECO:0000269|PubMed:16514057, ECO:0000269|PubMed:17360632,
CC       ECO:0000269|PubMed:19015309, ECO:0000269|PubMed:19451274}.
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 (By similarity). Interacts with TEK (PubMed:10557082,
CC       PubMed:19451274). Interacts via fibronectin type-III 17 domain with
CC       CDH5 (PubMed:19015309). Detected in a complex with CNTN1 and NRCAM
CC       (PubMed:11564762). Interacts (phosphorylated form) with FYN and GRB2
CC       (PubMed:20398064). {ECO:0000250|UniProtKB:P23467,
CC       ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:11564762,
CC       ECO:0000269|PubMed:12234928, ECO:0000269|PubMed:19015309,
CC       ECO:0000269|PubMed:19451274, ECO:0000269|PubMed:20398064}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expression is very high in the vasculature of lung,
CC       spleen, and kidney, as well as in the heart valves, and is also present
CC       in the endothelium of arterioles and venules. Also expressed in tumor
CC       vasculature. {ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:16514057,
CC       ECO:0000269|PubMed:17360632}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in both arterial and venous vascular
CC       endothelium in embryos, although more strongly in arterial vessels.
CC       Highly expressed in the developing outflow tract of the heart and later
CC       is expressed in developing heart valves. {ECO:0000269|PubMed:10557082,
CC       ECO:0000269|PubMed:16514057, ECO:0000269|PubMed:17360632}.
CC   -!- DISRUPTION PHENOTYPE: Mice show severe cardiovascular defects and
CC       embryonic lethality by 10 dpc. Vasculogenesis occurs normally however,
CC       angiogenesis is abnormal. Angiogenic defects are most pronounced in the
CC       yolk sac and include a complete failure to elaborate the primitive
CC       vascular scaffold into higher-order branched arteries, veins, and
CC       capillaries. {ECO:0000269|PubMed:17360632}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY077755; AAL75813.1; -; mRNA.
DR   EMBL; AK147439; BAE27912.1; -; mRNA.
DR   EMBL; AK147668; BAE28060.1; -; mRNA.
DR   EMBL; CH466539; EDL21786.1; -; Genomic_DNA.
DR   EMBL; BC141006; AAI41007.1; -; mRNA.
DR   EMBL; BC145111; AAI45112.1; -; mRNA.
DR   CCDS; CCDS36063.1; -.
DR   RefSeq; NP_084204.2; NM_029928.2.
DR   AlphaFoldDB; B2RU80; -.
DR   SMR; B2RU80; -.
DR   BioGRID; 202492; 15.
DR   IntAct; B2RU80; 2.
DR   MINT; B2RU80; -.
DR   STRING; 10090.ENSMUSP00000089805; -.
DR   GlyCosmos; B2RU80; 23 sites, No reported glycans.
DR   GlyGen; B2RU80; 23 sites.
DR   iPTMnet; B2RU80; -.
DR   PhosphoSitePlus; B2RU80; -.
DR   MaxQB; B2RU80; -.
DR   PaxDb; 10090-ENSMUSP00000089805; -.
DR   PeptideAtlas; B2RU80; -.
DR   ProteomicsDB; 301917; -.
DR   Antibodypedia; 29475; 119 antibodies from 24 providers.
DR   DNASU; 19263; -.
DR   Ensembl; ENSMUST00000092167.7; ENSMUSP00000089805.6; ENSMUSG00000020154.11.
DR   GeneID; 19263; -.
DR   KEGG; mmu:19263; -.
DR   UCSC; uc007hbv.2; mouse.
DR   AGR; MGI:97809; -.
DR   CTD; 5787; -.
DR   MGI; MGI:97809; Ptprb.
DR   VEuPathDB; HostDB:ENSMUSG00000020154; -.
DR   eggNOG; KOG0791; Eukaryota.
DR   GeneTree; ENSGT00940000156088; -.
DR   HOGENOM; CLU_000787_0_0_1; -.
DR   InParanoid; B2RU80; -.
DR   OMA; TRHQTNT; -.
DR   OrthoDB; 5402037at2759; -.
DR   PhylomeDB; B2RU80; -.
DR   TreeFam; TF351926; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 19263; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Ptprb; mouse.
DR   PRO; PR:B2RU80; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; B2RU80; Protein.
DR   Bgee; ENSMUSG00000020154; Expressed in right lung and 230 other cell types or tissues.
DR   ExpressionAtlas; B2RU80; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR   GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IDA:CACAO.
DR   CDD; cd00063; FN3; 12.
DR   CDD; cd14617; R-PTPc-B; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 15.
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:SF2; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE BETA; 1.
DR   Pfam; PF00041; fn3; 15.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 16.
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; 16.
DR   PROSITE; PS50853; FN3; 12.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   Genevisible; B2RU80; MM.
PE   1: Evidence at protein level;
KW   Angiogenesis; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1998
FT                   /note="Receptor-type tyrosine-protein phosphatase beta"
FT                   /id="PRO_0000390401"
FT   TOPO_DOM        23..1622
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1623..1643
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1644..1997
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..109
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          113..206
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          207..291
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          292..384
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          378..466
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          470..556
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          557..642
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          643..733
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          734..821
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          822..913
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          908..994
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          995..1088
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1086..1173
FT                   /note="Fibronectin type-III 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1176..1263
FT                   /note="Fibronectin type-III 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1264..1357
FT                   /note="Fibronectin type-III 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1358..1449
FT                   /note="Fibronectin type-III 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1449..1551
FT                   /note="Fibronectin type-III 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1704..1964
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        1905
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1871
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1905..1911
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1949
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1982
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:20398064"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
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        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        599
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        653
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        830
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1041
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1097
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         1911
FT                   /note="R->A: Loss of activity and dephosphorylation of
FT                   CDH5."
FT                   /evidence="ECO:0000269|PubMed:12234928"
FT   MUTAGEN         1982
FT                   /note="Y->F: Loss of tyrosine phosphorylation. Abolishes
FT                   interaction with FYN and GRB2."
FT                   /evidence="ECO:0000269|PubMed:20398064"
FT   CONFLICT        647
FT                   /note="V -> A (in Ref. 3; BAE28060/BAE27912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="T -> P (in Ref. 1; AAL75813)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1037
FT                   /note="L -> F (in Ref. 3; BAE28060/BAE27912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1168
FT                   /note="I -> V (in Ref. 3; BAE28060/BAE27912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1748
FT                   /note="C -> S (in Ref. 1; AAL75813)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1998 AA;  224495 MW;  066EE7141F942887 CRC64;
     MLRHGALTAL WITLSVVQTG VAEQVKCNFT LLESRVSSLS ASIQWRTFAS PCNFSLIYSS
     DTSGPMWCHP IRIDNFTYGC NPKDLQAGTV YNFRIVSLDG EESTLVLQTD PLPPARFEVN
     REKTASTTLQ VRWTPSSGKV SWYEVQLFDH NNQKIQEVQV QESTTWSQYT FLNLTEGNSY
     KVAITAVSGE KRSFPVYING STVPSPVKDL GISPNPNSLL ISWSRGSGNV EQYRLVLMDK
     GAIVQDTNVD RRDTSYAFHE LTPGHLYNLT IVTMASGLQN SRWKLVRTAP MEVSNLKVTN
     DGRLTSLNVK WQKPPGDVDS YSITLSHQGT IKESKTLAPP VTETQFKDLV PGRLYQVTIS
     CISGELSAEK SAAGRTVPEK VRNLVSYNEI WMKSFTVNWT PPAGDWEHYR IVLFNESLVL
     LNTTVGKEET HYALDGLELI PGRQYEIEVI VESGNLRNSE RCQGRTVPLA VLQLRVKHAN
     ETSLGITWRA PLGEWEKYII SLMDRELLVI HKSLSKDAKE FTFTDLMPGR NYKATVTSMS
     GDLKQSSSIK GRTVPAQVTD LHVNNQGMTS SLFTNWTKAL GDVEFYQVLL IHENVVVKNE
     SVSSDTSRYS FRALKPGSLY SVVVTTVSGG ISSRQVVAEG RTVPSSVSGV TVNNSGRNDY
     LSVSWLPAPG EVDHYVVSLS HEGKVDQFLI IAKSVSECSF SSLTPGRLYN VTVTTKSGNY
     ASHSFTEERT VPDKVQGISV SNSARSDYLK VSWVHATGDF DHYEVTIKNR ESFIQTKTIP
     KSENECEFIE LVPGRLYSVT VSTKSGQYEA SEQGTGRTIP EPVKDLTLLN RSTEDLHVTW
     SRANGDVDQY EVQLLFNDMK VFPHIHLVNT ATEYKFTALT PGRHYKILVL TISGDVQQSA
     FIEGLTVPST VKNIHISANG ATDRLMVTWS PGGGDVDSYV VSAFRQDEKV DSQTIPKHAS
     EHTFHRLEAG AKYRIAIVSV SGSLRNQIDA LGQTVPASVQ GVVAANAYSS NSLTVSWQKA
     LGVAERYDIL LLNENGLLLS NVSEPATARQ HKFEDLTPGK KYKMQILTVS GGLFSKESQA
     EGRTVPAAVT NLRITENSSR YLSFGWTASE GELSWYNIFL YNPDRTLQER AQVDPLVQSF
     SFQNLLQGRM YKMVIVTHSG ELSNESFIFG RTVPAAVNHL KGSHRNTTDS LWFSWSPASG
     DFDFYELILY NPNGTKKENW KEKDVTEWRF QGLVPGRKYT LYVVTHSGDL SNKVTGEGRT
     APSPPSLLSF ADVANTSLAI TWKGPPDWTD YNDFELQWFP GDALTIFNPY SSRKSEGRIV
     YGLHPGRSYQ FSVKTVSGDS WKTYSKPISG SVRTKPDKIQ NLHCRPQNST AIACSWIPPD
     SDFDGYSIEC RKMDTQEIEF SRKLEKEKSL LNIMMLVPHK RYLVSIKVQS AGMTSEVVED
     STITMIDRPP QPPPHIRVNE KDVLISKSSI NFTVNCSWFS DTNGAVKYFA VVVREADSMD
     ELKPEQQHPL PSYLEYRHNA SIRVYQTNYF ASKCAESPDS SSKSFNIKLG AEMDSLGGKC
     DPSQQKFCDG PLKPHTAYRI SIRAFTQLFD EDLKEFTKPL YSDTFFSMPI TTESEPLFGV
     IEGVSAGLFL IGMLVALVAF FICRQKASHS RERPSARLSI RRDRPLSVHL NLGQKGNRKT
     SCPIKINQFE GHFMKLQADS NYLLSKEYED LKDVGRSQSC DIALLPENRG KNRYNNILPY
     DASRVKLCNV DDDPCSDYIN ASYIPGNNFR REYIATQGPL PGTKDDFWKM AWEQNVHNIV
     MVTQCVEKGR VKCDHYWPAD QDPLYYGDLI LQMVSESVLP EWTIREFKIC SEEQLDAHRL
     IRHFHYTVWP DHGVPETTQS LIQFVRTVRD YINRSPGAGP TVVHCSAGVG RTGTFVALDR
     ILQQLDSKDS VDIYGAVHDL RLHRVHMVQT ECQYVYLHQC VRDVLRAKKL RNEQENPLFP
     IYENVNPEYH RDAIYSRH
//