PTPRR_HUMAN
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 03-AUG-2022, entry version 198.
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 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: [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: 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}.
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};
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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 GlyGen; Q15256; 2 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; Q15256; -.
DR PeptideAtlas; Q15256; -.
DR PRIDE; Q15256; -.
DR ProteomicsDB; 24502; -.
DR ProteomicsDB; 60496; -. [Q15256-1]
DR ProteomicsDB; 60497; -. [Q15256-3]
DR ProteomicsDB; 60498; -. [Q15256-4]
DR Antibodypedia; 2547; 279 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 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; READKIW; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q15256; -.
DR TreeFam; TF331016; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q15256; -.
DR SignaLink; Q15256; -.
DR SIGNOR; Q15256; -.
DR BioGRID-ORCS; 5801; 9 hits in 1082 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 121 other tissues.
DR ExpressionAtlas; Q15256; baseline and differential.
DR Genevisible; Q15256; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 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; PTHR46198; 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; SSF52799; 1.
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; Cell membrane; Cytoplasm; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Receptor;
KW Reference proteome; Signal; Transmembrane; 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 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
