ID PTPR2_MACNE Reviewed; 1013 AA. AC O02695; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 16-SEP-2015, entry version 89. DE RecName: Full=Receptor-type tyrosine-protein phosphatase N2; DE Short=R-PTP-N2; DE EC=3.1.3.48; DE AltName: Full=M1851; DE Flags: Precursor; GN Name=PTPRN2; OS Macaca nemestrina (Pig-tailed macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9545; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pancreatic islet; RX PubMed=9100223; RA Lagasse J., Jelinek L., Sexson S., Lofton-Day C.E., Breininger J., RA Sheppard P., Kindsvogel W., Hagopian W.A.; RT "An islet-cell protein tyrosine phosphatase is a likely precursor to RT the 37-kDa autoantigen in type 1 diabetes: human and macaque RT sequences, tissue distribution, unique and shared epitopes, and RT predictive autoantibodies."; RL Mol. Med. 3:163-173(1997). CC -!- FUNCTION: Implicated in development of nervous system and CC pancreatic endocrine cells. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC membrane {ECO:0000250}; Single-pass type I membrane protein CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Brain, prostate, pancreatic islets. Lower CC expression in spinal cord, thyroid, adrenal medulla and CC gastrointestinal tract. CC -!- PTM: Appears to undergo multiple proteolytic cleavage at CC consecutive basic residues. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 8 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00160}. 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; U91574; AAC51186.1; -; mRNA. DR RefSeq; NP_001292849.1; NM_001305920.1. DR ProteinModelPortal; O02695; -. DR PRIDE; O02695; -. DR GeneID; 105474981; -. DR HOVERGEN; HBG105788; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTPase_domain. DR InterPro; IPR021613; Receptor_IA-2_dom. DR InterPro; IPR029403; RESP18_dom. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR Pfam; PF11548; Receptor_IA-2; 1. DR Pfam; PF14948; RESP18; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 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 2: Evidence at transcript level; KW Acetylation; Cytoplasmic vesicle; Glycoprotein; Hydrolase; Membrane; KW Protein phosphatase; Receptor; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 1013 Receptor-type tyrosine-protein FT phosphatase N2. FT /FTId=PRO_0000025455. FT TOPO_DOM 20 613 Extracellular. {ECO:0000255}. FT TRANSMEM 614 634 Helical. {ECO:0000255}. FT TOPO_DOM 635 1013 Cytoplasmic. {ECO:0000255}. FT DOMAIN 743 1003 Tyrosine-protein phosphatase. FT {ECO:0000255|PROSITE-ProRule:PRU00160}. FT REGION 943 949 Substrate binding. {ECO:0000250}. FT ACT_SITE 943 943 Phosphocysteine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044}. FT BINDING 911 911 Substrate. {ECO:0000250}. FT BINDING 988 988 Substrate. {ECO:0000250}. FT SITE 425 426 Cleavage. {ECO:0000250}. FT MOD_RES 968 968 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q92932}. FT CARBOHYD 562 562 N-linked (GlcNAc...). {ECO:0000255}. SQ SEQUENCE 1013 AA; 111191 MW; 4808D43937A2EF59 CRC64; MALPLLLLLL LLLPPRVLPA APSSVPHGRQ LPGRLGCLLE EGLCGASEAC VNDGVFGRCQ KVPAMDFYRY EVSPVALQRL RVALQKLSGT GFTWQDDYTQ YVMDQELADL PKTYLRHPEA SGPARPSKHS IGSERRYSQE GGAALAKAFR RHLPFLEALS QAPASDALAR TRMAQDRPRA EGDDRFSKSI LTYVAHTSVL TYPPGPQAQL PEDLLPRTLS QLQPDELSPK VDSSVERHHL MAALSAYAAQ RPPAPPGKGS LEPQYLLRAP SRMPRPLLSP AVPQKWPSPL GDPEDPPSTG EGARIHTLLK DLQRQPAEAR GLSDLELDSM AELMAGLMQG MDHRGALGGP GKAALGESGE QADGPKAALR GESFPDDGVQ DDDDRLYQEV HRLSATLGGL LQDHGSRLSP GALPFAKPLK MERKKSERPE ASLSSEEETA GVENVKSQTY SKDLLGQQPH SEPGAGAFGE LQNQMPGPSE EEQSLPAGAQ EALGDGLQLE VKPSEEEARG YIVTDRDPLR PEEGRQLVED VARLLQMPSS TFADVEVLGP AVTFKVGANV QNVTTADVEK ATVDNKDKLE ETSGLKILQT GVGSKSKLKF LPPQAEQEDS TKFIALTLVS LACILGVLLA SGLIYCLRHS SQHRLKEKLS GLGRDPGADA TAAYQELCRQ RMATRPPDRP EGPHTSRISS VSSQFSDGPM PSPSARSSAS SWSEEPVQSN MDISTGHMIL SYMEDHLKNK NRLEKEWEAL CAYQAEPNSS LVAQKEENVP KNRSLAVLTY DHSRVLLKAE NSHSHSDYIN ASPIMDHDPR NPAYIATQGP LPATVADFWQ MVWESGCVVI VMLTPLTENG VRQCYHYWPD EGSNLYHIYE VNLVSEHIWC EDFLVRSFYL KNLQTNETRT VTQFHFLSWY DRGVPSSSRS LLDFRRKVNK CYRGRSCPII VHCSDGAGRS GTYVLIDMVL NKMAKGAKEI DIAATLEHLR DQRPGMVQTK EQFEFALTAV AEEVNAILKA LPQ //