ID PTPX_MACNE STANDARD; PRT; 1013 AA. AC O02695; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Receptor-type protein-tyrosine phosphatase N2 precursor (EC 3.1.3.48) DE (R-PTP-N2) (M1851). GN PTPRN2. OS Macaca nemestrina (Pig-tailed macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae; OC Cercopithecinae; Macaca. OX NCBI_TaxID=9545; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pancreatic islets; RX MEDLINE=97254813; 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. CC -!- SUBCELLULAR LOCATION: Type I membrane protein (Probable). 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 (By similarity). CC -!- SIMILARITY: Contains 1 protein-tyrosine phosphatase domain. 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; -. DR HSSP; P18052; 1YFO. DR InterPro; IPR000387; TYR_phosphatase. DR InterPro; IPR000242; Tyr_PP. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. KW Hydrolase; Receptor; Glycoprotein; Signal; Transmembrane. FT SIGNAL 1 19 POTENTIAL. FT CHAIN 20 1013 RECEPTOR-TYPE PROTEIN-TYROSINE FT PHOSPHATASE N2. FT DOMAIN 20 613 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 614 634 POTENTIAL. FT DOMAIN 635 1013 CYTOPLASMIC (POTENTIAL). FT DOMAIN 768 1002 PROTEIN-TYROSINE PHOSPHATASE. FT ACT_SITE 943 943 PHOSPHOCYSTEINE INTERMEDIATE (POTENTIAL). FT SITE 425 426 CLEAVAGE SITE (BY SIMILARITY). FT CARBOHYD 562 562 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 1013 AA; 111190 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 //