ID PTPRR_HUMAN Reviewed; 657 AA. AC Q15256; B2R5Z7; B7Z3J1; F5GXR7; O00342; Q92682; Q9UE65; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=Receptor-type tyrosine-protein phosphatase R; DE Short=R-PTP-R; DE EC=3.1.3.48; DE AltName: Full=Ch-1PTPase; DE AltName: Full=NC-PTPCOM1; DE AltName: Full=Protein-tyrosine phosphatase PCPTP1; DE Flags: Precursor; GN Name=PTPRR; Synonyms=ECPTP, PTPRQ; 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 ALPHA), AND VARIANT ARG-314. RC TISSUE=Brain; RX PubMed=7557444; DOI=10.1016/0378-1119(95)00306-q; RA Shiozuka K., Watanabe Y., Ikeda T., Hashimoto S., Kawashima H.; RT "Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase."; RL Gene 162:279-284(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; GAMMA AND DELTA), TISSUE RP SPECIFICITY, AND VARIANT ARG-314. RC TISSUE=Brain, and Colon; RX PubMed=10705342; RX DOI=10.1002/(sici)1097-0185(20000301)258:3<221::aid-ar1>3.0.co;2-w; RA Augustine K.A., Silbiger S.M., Bucay N., Ulias L., Boynton A., RA Trebasky L.D., Medlock E.S.; RT "Protein tyrosine phosphatase (PC12, Br7,Sl) family: expression RT characterization in the adult human and mouse."; RL Anat. Rec. 258:221-234(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-314. RX PubMed=11147789; DOI=10.2337/diabetes.50.1.204; RA Bektas A., Hughes J.N., Warram J.H., Krolewski A.S., Doria A.; RT "Type 2 diabetes locus on 12q15: further mapping and mutation screening of RT two candidate genes."; RL Diabetes 50:204-208(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT ARG-314. RC TISSUE=Neuroblastoma; RA Knyazev P., Cheburkin Y., Knyazev Y., Ullrich A.; RT "Cloning and characterization of novel PTP (NC-PTPCOM) from neuronal RT cells."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 4), AND VARIANT RP ARG-314. RC TISSUE=Amygdala, and Substantia nigra; 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 289-657 (ISOFORM ALPHA), AND VARIANT ARG-314. RC TISSUE=Mammary gland; RA Knyazev P.G., Ullrich A.; RT "Molecular cloning and characterization of human epithelial cells specific RT protein tyrosine phosphatase (EC-PTP)."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-23. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 375-655. RX PubMed=16441242; DOI=10.1042/bj20051931; RA Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E., RA Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.; RT "Crystal structures and inhibitor identification for PTPN5, PTPRR and RT PTPN7: a family of human MAPK-specific protein tyrosine phosphatases."; RL Biochem. J. 395:483-491(2006). CC -!- FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as CC MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs CC bind to a dephosphorylated kinase interacting motif, phosphorylation of CC which by the protein kinase A complex releases the MAPKs for activation CC and translocation into the nucleus (By similarity). {ECO:0000250}. 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 with MAPKs. {ECO:0000250}. CC -!- INTERACTION: CC Q15256; P04626: ERBB2; NbExp=2; IntAct=EBI-2265659, EBI-641062; CC Q15256; P06213: INSR; NbExp=2; IntAct=EBI-2265659, EBI-475899; CC Q15256; P28482: MAPK1; NbExp=3; IntAct=EBI-2265659, EBI-959949; CC Q15256; Q16539: MAPK14; NbExp=3; IntAct=EBI-2265659, EBI-73946; CC Q15256-1; Q16539-1: MAPK14; NbExp=6; IntAct=EBI-16067395, EBI-15834191; CC Q15256-5; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-18347359, EBI-746969; CC Q15256-5; P28482: MAPK1; NbExp=3; IntAct=EBI-18347359, EBI-959949; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458}. CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type CC I membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform Delta]: Cytoplasm, perinuclear region. CC Note=Locates to the perinuclear areas within the cytoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm, perinuclear region. CC Note=Locates to the perinuclear areas within the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Alpha; CC IsoId=Q15256-1; Sequence=Displayed; CC Name=Gamma; CC IsoId=Q15256-3; Sequence=VSP_005156; CC Name=Delta; CC IsoId=Q15256-4; Sequence=VSP_005155, VSP_005158; CC Name=4; CC IsoId=Q15256-5; Sequence=VSP_046352, VSP_046353; CC -!- TISSUE SPECIFICITY: Detected in cerebrospinal fluid (at protein level) CC (PubMed:25326458). Expressed in brain, placenta, small intestine, CC stomach, uterus and weakly in the prostate. Isoform alpha has been CC observed only in the brain. Isoform gamma is expressed in brain, CC placenta and uterus. Isoform delta is expressed in brain, kidney, CC placenta, prostate, small intestine and uterus. CC {ECO:0000269|PubMed:10705342, ECO:0000269|PubMed:25326458}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 7 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA57957.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAB01957.1; Type=Frameshift; Evidence={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; D64053; BAA10930.1; -; mRNA. DR EMBL; U42361; AAD09447.1; -; mRNA. DR EMBL; U77917; AAB54007.1; -; mRNA. DR EMBL; U77916; AAB54006.1; -; mRNA. DR EMBL; AF263029; AAG47642.1; -; Genomic_DNA. DR EMBL; AF263016; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263017; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263018; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263019; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263020; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263021; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263022; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263023; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263024; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263025; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263026; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263027; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; AF263028; AAG47642.1; JOINED; Genomic_DNA. DR EMBL; Z79693; CAB01957.1; ALT_FRAME; mRNA. DR EMBL; AK295951; BAH12227.1; -; mRNA. DR EMBL; AK312376; BAG35294.1; -; mRNA. DR EMBL; AC083809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC140066; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X82635; CAA57957.1; ALT_FRAME; mRNA. DR CCDS; CCDS44945.1; -. [Q15256-3] DR CCDS; CCDS55847.1; -. [Q15256-4] DR CCDS; CCDS55848.1; -. [Q15256-5] DR CCDS; CCDS8998.1; -. [Q15256-1] DR RefSeq; NP_001193944.1; NM_001207015.1. [Q15256-5] DR RefSeq; NP_001193945.1; NM_001207016.1. [Q15256-4] DR RefSeq; NP_002840.2; NM_002849.3. [Q15256-1] DR RefSeq; NP_570897.2; NM_130846.2. [Q15256-3] DR PDB; 2A8B; X-ray; 2.30 A; A=375-655. DR PDBsum; 2A8B; -. DR AlphaFoldDB; Q15256; -. DR SMR; Q15256; -. DR BioGRID; 111765; 104. DR DIP; DIP-42066N; -. DR ELM; Q15256; -. DR IntAct; Q15256; 88. DR MINT; Q15256; -. DR STRING; 9606.ENSP00000283228; -. DR BindingDB; Q15256; -. DR ChEMBL; CHEMBL3425390; -. DR DEPOD; PTPRR; -. DR GlyCosmos; Q15256; 2 sites, 1 glycan. DR GlyGen; Q15256; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q15256; -. DR PhosphoSitePlus; Q15256; -. DR BioMuta; PTPRR; -. DR DMDM; 134039192; -. DR EPD; Q15256; -. DR jPOST; Q15256; -. DR MassIVE; Q15256; -. DR MaxQB; Q15256; -. DR PaxDb; 9606-ENSP00000283228; -. DR PeptideAtlas; Q15256; -. DR ProteomicsDB; 24502; -. DR ProteomicsDB; 60496; -. [Q15256-1] DR ProteomicsDB; 60497; -. [Q15256-3] DR ProteomicsDB; 60498; -. [Q15256-4] DR Antibodypedia; 2547; 299 antibodies from 29 providers. DR DNASU; 5801; -. DR Ensembl; ENST00000283228.7; ENSP00000283228.2; ENSG00000153233.13. [Q15256-1] DR Ensembl; ENST00000342084.8; ENSP00000339605.4; ENSG00000153233.13. [Q15256-5] DR Ensembl; ENST00000378778.5; ENSP00000368054.1; ENSG00000153233.13. [Q15256-4] DR Ensembl; ENST00000440835.6; ENSP00000391750.2; ENSG00000153233.13. [Q15256-3] DR Ensembl; ENST00000549308.5; ENSP00000446943.1; ENSG00000153233.13. [Q15256-3] DR GeneID; 5801; -. DR KEGG; hsa:5801; -. DR MANE-Select; ENST00000283228.7; ENSP00000283228.2; NM_002849.4; NP_002840.2. DR UCSC; uc001swh.3; human. [Q15256-1] DR AGR; HGNC:9680; -. DR CTD; 5801; -. DR DisGeNET; 5801; -. DR GeneCards; PTPRR; -. DR HGNC; HGNC:9680; PTPRR. DR HPA; ENSG00000153233; Tissue enhanced (brain, endometrium, intestine). DR MIM; 602853; gene. DR neXtProt; NX_Q15256; -. DR OpenTargets; ENSG00000153233; -. DR PharmGKB; PA34025; -. DR VEuPathDB; HostDB:ENSG00000153233; -. DR eggNOG; KOG0789; Eukaryota. DR GeneTree; ENSGT00940000157212; -. DR HOGENOM; CLU_001645_10_0_1; -. DR InParanoid; Q15256; -. DR OMA; NCVELFI; -. DR OrthoDB; 2914248at2759; -. DR PhylomeDB; Q15256; -. DR TreeFam; TF331016; -. DR BRENDA; 3.1.3.48; 2681. DR PathwayCommons; Q15256; -. DR SABIO-RK; Q15256; -. DR SignaLink; Q15256; -. DR SIGNOR; Q15256; -. DR BioGRID-ORCS; 5801; 9 hits in 1177 CRISPR screens. DR ChiTaRS; PTPRR; human. DR EvolutionaryTrace; Q15256; -. DR GeneWiki; PTPRR; -. DR GenomeRNAi; 5801; -. DR Pharos; Q15256; Tbio. DR PRO; PR:Q15256; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q15256; Protein. DR Bgee; ENSG00000153233; Expressed in endothelial cell and 123 other cell types or tissues. DR ExpressionAtlas; Q15256; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc. DR GO; GO:0038128; P:ERBB2 signaling pathway; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEP:UniProtKB. DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd14611; R-PTPc-R; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. 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 InterPro; IPR008356; Tyr_Pase_KIM-con. DR InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5. DR PANTHER; PTHR46198; PROTEIN-TYROSINE-PHOSPHATASE; 1. DR PANTHER; PTHR46198:SF2; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE R; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF001997; PTPRR; 1. DR PRINTS; PR01778; KIMPTPASE. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR Genevisible; Q15256; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Glycoprotein; KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Proteoglycan; KW Receptor; Reference proteome; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..657 FT /note="Receptor-type tyrosine-protein phosphatase R" FT /id="PRO_0000025459" FT TOPO_DOM 22..227 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 228..248 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 249..657 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 393..647 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 588 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 554 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 588..594 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 632 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62132" FT MOD_RES 339 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250|UniProtKB:Q62132" FT CARBOHYD 23 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458" FT CARBOHYD 129 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..245 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:10705342" FT /id="VSP_005156" FT VAR_SEQ 1..206 FT /note="Missing (in isoform Delta)" FT /evidence="ECO:0000303|PubMed:10705342" FT /id="VSP_005155" FT VAR_SEQ 1..7 FT /note="MRRAVCF -> MQSISKQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046352" FT VAR_SEQ 8..119 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046353" FT VAR_SEQ 207..209 FT /note="SPE -> MNQ (in isoform Delta)" FT /evidence="ECO:0000303|PubMed:10705342" FT /id="VSP_005158" FT VARIANT 249 FT /note="Y -> H (in dbSNP:rs35987017)" FT /id="VAR_057140" FT VARIANT 314 FT /note="K -> R (in dbSNP:rs3803036)" FT /evidence="ECO:0000269|PubMed:10705342, FT ECO:0000269|PubMed:11147789, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:7557444, ECO:0000269|Ref.4, FT ECO:0000269|Ref.7" FT /id="VAR_014283" FT VARIANT 386 FT /note="V -> I (in dbSNP:rs35387004)" FT /id="VAR_057141" FT VARIANT 439 FT /note="V -> I (in dbSNP:rs35390084)" FT /id="VAR_057142" FT CONFLICT 407 FT /note="P -> S (in Ref. 5; BAH12227)" FT /evidence="ECO:0000305" FT HELIX 380..386 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 442..445 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 446..452 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 455..457 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 473..483 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 487..492 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 494..499 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 507..512 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 515..524 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 529..537 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 540..549 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 554..556 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 562..576 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 584..587 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 589..592 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 593..611 FT /evidence="ECO:0007829|PDB:2A8B" FT STRAND 612..614 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 616..626 FT /evidence="ECO:0007829|PDB:2A8B" FT HELIX 634..648 FT /evidence="ECO:0007829|PDB:2A8B" SQ SEQUENCE 657 AA; 73834 MW; 42CD98F37AC5B638 CRC64; MRRAVCFPAL CLLLNLHAAG CFSGNNDHFL AINQKKSGKP VFIYKHSQDI EKSLDIAPQK IYRHSYHSSS EAQVSKRHQI VNSAFPRPAY DPSLNLLAMD GQDLEVENLP IPAANVIVVT LQMDVNKLNI TLLRIFRQGV AAALGLLPQQ VHINRLIGKK NSIELFVSPI NRKTGISDAL PSEEVLRSLN INVLHQSLSQ FGITEVSPEK NVLQGQHEAD KIWSKEGFYA VVIFLSIFVI IVTCLMILYR LKERFQLSLR QDKEKNQEIH LSPITLQPAL SEAKTVHSMV QPEQAPKVLN VVVDPQGRGA PEIKATTATS VCPSPFKMKP IGLQERRGSN VSLTLDMSSL GNIEPFVSIP TPREKVAMEY LQSASRILTR SQLRDVVASS HLLQSEFMEI PMNFVDPKEI DIPRHGTKNR YKTILPNPLS RVCLRPKNVT DSLSTYINAN YIRGYSGKEK AFIATQGPMI NTVDDFWQMV WQEDSPVIVM ITKLKEKNEK CVLYWPEKRG IYGKVEVLVI SVNECDNYTI RNLVLKQGSH TQHVKHYWYT SWPDHKTPDS AQPLLQLMLD VEEDRLASQG RGPVVVHCSA GIGRTGCFIA TSIGCQQLKE EGVVDALSIV CQLRMDRGGM VQTSEQYEFV HHALCLYESR LSAETVQ //