PTPRB_MOUSE
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 03-AUG-2022, entry version 108.
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}.
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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 GlyGen; B2RU80; 23 sites.
DR iPTMnet; B2RU80; -.
DR PhosphoSitePlus; B2RU80; -.
DR MaxQB; B2RU80; -.
DR PaxDb; B2RU80; -.
DR PeptideAtlas; B2RU80; -.
DR PRIDE; B2RU80; -.
DR ProteomicsDB; 301917; -.
DR Antibodypedia; 29475; 104 antibodies from 24 providers.
DR DNASU; 19263; -.
DR Ensembl; ENSMUST00000092167; ENSMUSP00000089805; ENSMUSG00000020154.
DR GeneID; 19263; -.
DR KEGG; mmu:19263; -.
DR UCSC; uc007hbv.2; mouse.
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; SATWEFP; -.
DR PhylomeDB; B2RU80; -.
DR TreeFam; TF351926; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19263; 2 hits in 74 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 229 other tissues.
DR ExpressionAtlas; B2RU80; baseline and differential.
DR Genevisible; B2RU80; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus 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 Gene3D; 2.60.40.10; -; 15.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041201; PTPRJ_TM.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 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; SSF49265; SSF49265; 16.
DR SUPFAM; SSF52799; SSF52799; 1.
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.
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
