PTPRO_HUMAN
ID PTPRO_HUMAN Reviewed; 1216 AA.
AC Q16827; A0AV39; Q13101; Q8IYG3; Q9UBF0; Q9UBT5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase O;
DE Short=R-PTP-O;
DE EC=3.1.3.48;
DE AltName: Full=Glomerular epithelial protein 1;
DE AltName: Full=Protein tyrosine phosphatase U2;
DE Short=PTP-U2;
DE Short=PTPase U2;
DE Flags: Precursor;
GN Name=PTPRO; Synonyms=GLEPP1, PTPU2;
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).
RC TISSUE=Kidney;
RX PubMed=7753550;
RA Seimiya H., Sawabe T., Inazawa J., Tsuruo T.;
RT "Cloning, expression and chromosomal localization of a novel gene for
RT protein tyrosine phosphatase (PTP-U2) induced by various differentiation-
RT inducing agents.";
RL Oncogene 10:1731-1738(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=7665166; DOI=10.1006/geno.1995.1021;
RA Wiggins R.C., Wiggins J.E., Goyal M., Wharram B.L., Thomas P.E.;
RT "Molecular cloning of cDNAs encoding human GLEPP1, a membrane protein
RT tyrosine phosphatase: characterization of the GLEPP1 protein distribution
RT in human kidney and assignment of the GLEPP1 gene to human chromosome
RT 12p12-p13.";
RL Genomics 27:174-181(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
RX PubMed=10498613;
RA Aguiar R.C., Yakushijin Y., Kharbanda S., Tiwari S., Freeman G.J.,
RA Shipp M.A.;
RT "PTPROt: an alternatively spliced and developmentally regulated B-lymphoid
RT phosphatase that promotes G0/G1 arrest.";
RL Blood 94:2403-2413(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Kidney;
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 [8]
RP INVOLVEMENT IN NPHS6.
RX PubMed=21722858; DOI=10.1016/j.ajhg.2011.05.026;
RA Ozaltin F., Ibsirlioglu T., Taskiran E.Z., Baydar D.E., Kaymaz F.,
RA Buyukcelik M., Kilic B.D., Balat A., Iatropoulos P., Asan E., Akarsu N.A.,
RA Schaefer F., Yilmaz E., Bakkaloglu A.;
RT "Disruption of PTPRO causes childhood-onset nephrotic syndrome.";
RL Am. J. Hum. Genet. 89:139-147(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 916-1208, AND FUNCTION.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 914-1200.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
CC -!- FUNCTION: Possesses tyrosine phosphatase activity. Plays a role in
CC regulating the glomerular pressure/filtration rate relationship through
CC an effect on podocyte structure and function (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19167335}.
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: Interacts (phosphorylated form) with FYN and GRB2.
CC {ECO:0000250|UniProtKB:E9Q612}.
CC -!- INTERACTION:
CC Q16827; P04626: ERBB2; NbExp=2; IntAct=EBI-723739, EBI-641062;
CC Q16827; P08581: MET; NbExp=2; IntAct=EBI-723739, EBI-1039152;
CC Q16827; Q02763: TEK; NbExp=2; IntAct=EBI-723739, EBI-2257090;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q16827-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16827-2; Sequence=VSP_035586;
CC Name=3; Synonyms=PTPROt;
CC IsoId=Q16827-3; Sequence=VSP_043136;
CC Name=4;
CC IsoId=Q16827-4; Sequence=VSP_043136, VSP_035586;
CC Name=5;
CC IsoId=Q16827-5; Sequence=VSP_054481, VSP_054482;
CC -!- TISSUE SPECIFICITY: Glomerulus of kidney. Also detected in brain, lung
CC and placenta. {ECO:0000269|PubMed:10498613}.
CC -!- INDUCTION: By various differentiation-inducing agents.
CC -!- DISEASE: Nephrotic syndrome 6 (NPHS6) [MIM:614196]: A form of nephrotic
CC syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form and progress to end-stage renal failure.
CC {ECO:0000269|PubMed:21722858}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Predominantly expressed in B-lymphoid
CC tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; Z48541; CAA88425.1; -; mRNA.
DR EMBL; U20489; AAA82892.1; -; mRNA.
DR EMBL; AF187043; AAF04086.1; -; mRNA.
DR EMBL; AF187044; AAF04087.1; -; mRNA.
DR EMBL; AK290982; BAF83671.1; -; mRNA.
DR EMBL; AC007542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96349.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96350.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96351.1; -; Genomic_DNA.
DR EMBL; BC035960; AAH35960.1; -; mRNA.
DR EMBL; BC126201; AAI26202.1; -; mRNA.
DR EMBL; BC126203; AAI26204.1; -; mRNA.
DR CCDS; CCDS44837.1; -. [Q16827-3]
DR CCDS; CCDS53754.1; -. [Q16827-4]
DR CCDS; CCDS8674.1; -. [Q16827-2]
DR CCDS; CCDS8675.1; -. [Q16827-1]
DR PIR; A57064; A57064.
DR PIR; S60613; S60613.
DR RefSeq; NP_002839.1; NM_002848.3. [Q16827-2]
DR RefSeq; NP_109592.1; NM_030667.2. [Q16827-1]
DR RefSeq; NP_109593.1; NM_030668.2. [Q16827-4]
DR RefSeq; NP_109594.1; NM_030669.2. [Q16827-3]
DR RefSeq; NP_109595.1; NM_030670.2. [Q16827-4]
DR RefSeq; NP_109596.1; NM_030671.2. [Q16827-3]
DR PDB; 2G59; X-ray; 2.19 A; A/B=914-1200.
DR PDB; 2GJT; X-ray; 2.15 A; A/B=916-1208.
DR PDBsum; 2G59; -.
DR PDBsum; 2GJT; -.
DR AlphaFoldDB; Q16827; -.
DR SMR; Q16827; -.
DR BioGRID; 111764; 138.
DR IntAct; Q16827; 36.
DR MINT; Q16827; -.
DR STRING; 9606.ENSP00000281171; -.
DR BindingDB; Q16827; -.
DR ChEMBL; CHEMBL4105749; -.
DR DEPOD; PTPRO; -.
DR GlyGen; Q16827; 16 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q16827; -.
DR PhosphoSitePlus; Q16827; -.
DR BioMuta; PTPRO; -.
DR DMDM; 209572663; -.
DR jPOST; Q16827; -.
DR MassIVE; Q16827; -.
DR MaxQB; Q16827; -.
DR PaxDb; Q16827; -.
DR PeptideAtlas; Q16827; -.
DR PRIDE; Q16827; -.
DR ProteomicsDB; 61085; -. [Q16827-1]
DR ProteomicsDB; 61086; -. [Q16827-2]
DR ProteomicsDB; 61087; -. [Q16827-3]
DR ProteomicsDB; 61088; -. [Q16827-4]
DR ProteomicsDB; 71169; -.
DR Antibodypedia; 23718; 91 antibodies from 22 providers.
DR DNASU; 5800; -.
DR Ensembl; ENST00000281171.9; ENSP00000281171.4; ENSG00000151490.15. [Q16827-1]
DR Ensembl; ENST00000348962.7; ENSP00000343434.2; ENSG00000151490.15. [Q16827-2]
DR Ensembl; ENST00000442921.7; ENSP00000404188.2; ENSG00000151490.15. [Q16827-3]
DR Ensembl; ENST00000445537.6; ENSP00000393449.2; ENSG00000151490.15. [Q16827-3]
DR Ensembl; ENST00000542557.5; ENSP00000437571.1; ENSG00000151490.15. [Q16827-4]
DR Ensembl; ENST00000543886.6; ENSP00000444173.1; ENSG00000151490.15. [Q16827-5]
DR Ensembl; ENST00000544244.5; ENSP00000439234.1; ENSG00000151490.15. [Q16827-4]
DR Ensembl; ENST00000674261.1; ENSP00000501538.1; ENSG00000151490.15. [Q16827-1]
DR Ensembl; ENST00000674316.1; ENSP00000501352.1; ENSG00000151490.15. [Q16827-1]
DR Ensembl; ENST00000674388.1; ENSP00000501494.1; ENSG00000151490.15. [Q16827-3]
DR GeneID; 5800; -.
DR KEGG; hsa:5800; -.
DR MANE-Select; ENST00000281171.9; ENSP00000281171.4; NM_030667.3; NP_109592.1.
DR UCSC; uc001rcu.3; human. [Q16827-1]
DR CTD; 5800; -.
DR DisGeNET; 5800; -.
DR GeneCards; PTPRO; -.
DR HGNC; HGNC:9678; PTPRO.
DR HPA; ENSG00000151490; Tissue enhanced (intestine, kidney).
DR MalaCards; PTPRO; -.
DR MIM; 600579; gene.
DR MIM; 614196; phenotype.
DR neXtProt; NX_Q16827; -.
DR OpenTargets; ENSG00000151490; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA34023; -.
DR VEuPathDB; HostDB:ENSG00000151490; -.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000154814; -.
DR HOGENOM; CLU_007724_0_0_1; -.
DR InParanoid; Q16827; -.
DR OMA; KNATTFH; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q16827; -.
DR TreeFam; TF351926; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q16827; -.
DR Reactome; R-HSA-9034015; Signaling by NTRK3 (TRKC).
DR SignaLink; Q16827; -.
DR BioGRID-ORCS; 5800; 5 hits in 1067 CRISPR screens.
DR ChiTaRS; PTPRO; human.
DR EvolutionaryTrace; Q16827; -.
DR GeneWiki; PTPRO; -.
DR GenomeRNAi; 5800; -.
DR Pharos; Q16827; Tbio.
DR PRO; PR:Q16827; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16827; protein.
DR Bgee; ENSG00000151490; Expressed in renal glomerulus and 139 other tissues.
DR ExpressionAtlas; Q16827; baseline and differential.
DR Genevisible; Q16827; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0032835; P:glomerulus development; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0003105; P:negative regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0090260; P:negative regulation of retinal ganglion cell axon guidance; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0072112; P:podocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0003093; P:regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0036060; P:slit diaphragm assembly; ISS:UniProtKB.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR042996; PTPRO.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR47028; PTHR47028; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 5.
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 splicing; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1216
FT /note="Receptor-type tyrosine-protein phosphatase O"
FT /id="PRO_0000025458"
FT TOPO_DOM 30..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..1216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..124
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 142..211
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 246..306
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 329..425
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 435..531
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 532..628
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 631..724
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 725..817
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 938..1195
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1136
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1136..1142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q612"
FT MOD_RES 1210
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q612"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
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 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..811
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10498613,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_043136"
FT VAR_SEQ 594..597
FT /note="RIAN -> VIFP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054481"
FT VAR_SEQ 598..1216
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054482"
FT VAR_SEQ 876..903
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10498613,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:7665166"
FT /id="VSP_035586"
FT CONFLICT 159
FT /note="E -> G (in Ref. 1; CAA88425 and 2; AAA82892)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> C (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> V (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="V -> F (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="V -> F (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="A -> T (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="I -> T (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="A -> T (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="E -> K (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..758
FT /note="CQQ -> FQH (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="S -> P (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="N -> S (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 861..863
FT /note="VNF -> ANC (in Ref. 1; CAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="W -> C (in Ref. 1; CAA88425 and 2; AAA82892)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="L -> P (in Ref. 1; CAA88425 and 2; AAA82892)"
FT /evidence="ECO:0000305"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 923..946
FT /evidence="ECO:0007829|PDB:2GJT"
FT TURN 947..951
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 960..965
FT /evidence="ECO:0007829|PDB:2GJT"
FT TURN 975..977
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:2GJT"
FT TURN 988..991
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 992..998
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1007..1010
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1015..1017
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1018..1027
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1032..1035
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1053..1056
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1058..1060
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1063..1072
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1074..1085
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1088..1097
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1103..1105
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1108..1127
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1132..1140
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1141..1158
FT /evidence="ECO:0007829|PDB:2GJT"
FT STRAND 1160..1162
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1164..1172
FT /evidence="ECO:0007829|PDB:2GJT"
FT HELIX 1182..1202
FT /evidence="ECO:0007829|PDB:2GJT"
SQ SEQUENCE 1216 AA; 138344 MW; C902B48D1A73BFE1 CRC64;
MGHLPTGIHG ARRLLPLLWL FVLFKNATAF HVTVQDDNNI VVSLEASDVI SPASVYVVKI
TGESKNYFFE FEEFNSTLPP PVIFKASYHG LYYIITLVVV NGNVVTKPSR SITVLTKPLP
VTSVSIYDYK PSPETGVLFE IHYPEKYNVF TRVNISYWEG KDFRTMLYKD FFKGKTVFNH
WLPGMCYSNI TFQLVSEATF NKSTLVEYSG VSHEPKQHRT APYPPQNISV RIVNLNKNNW
EEQSGNFPEE SFMRSQDTIG KEKLFHFTEE TPEIPSGNIS SGWPDFNSSD YETTSQPYWW
DSASAAPESE DEFVSVLPME YENNSTLSET EKSTSGSFSF FPVQMILTWL PPKPPTAFDG
FHIHIEREEN FTEYLMVDEE AHEFVAELKE PGKYKLSVTT FSSSGSCETR KSQSAKSLSF
YISPSGEWIE ELTEKPQHVS VHVLSSTTAL MSWTSSQENY NSTIVSVVSL TCQKQKESQR
LEKQYCTQVN SSKPIIENLV PGAQYQVVIY LRKGPLIGPP SDPVTFAIVP TGIKDLMLYP
LGPTAVVLSW TRPYLGVFRK YVVEMFYFNP ATMTSEWTTY YEIAATVSLT ASVRIANLLP
AWYYNFRVTM VTWGDPELSC CDSSTISFIT APVAPEITSV EYFNSLLYIS WTYGDDTTDL
SHSRMLHWMV VAEGKKKIKK SVTRNVMTAI LSLPPGDIYN LSVTACTERG SNTSMLRLVK
LEPAPPKSLF AVNKTQTSVT LLWVEEGVAD FFEVFCQQVG SSQKTKLQEP VAVSSHVVTI
SSLLPATAYN CSVTSFSHDS PSVPTFIAVS TMVTEMNPNV VVISVLAILS TLLIGLLLVT
LIILRKKHLQ MARECGAGTF VNFASLERDG KLPYNWRRSI FAFLTLLPSC LWTDYLLAFY
INPWSKNGLK KRKLTNPVQL DDFDAYIKDM AKDSDYKFSL QFEELKLIGL DIPHFAADLP
LNRCKNRYTN ILPYDFSRVR LVSMNEEEGA DYINANYIPG YNSPQEYIAT QGPLPETRND
FWKMVLQQKS QIIVMLTQCN EKRRVKCDHY WPFTEEPIAY GDITVEMISE EEQDDWACRH
FRINYADEMQ DVMHFNYTAW PDHGVPTANA AESILQFVHM VRQQATKSKG PMIIHCSAGV
GRTGTFIALD RLLQHIRDHE FVDILGLVSE MRSYRMSMVQ TEEQYIFIHQ CVQLMWMKKK
QQFCISDVIY ENVSKS
