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 11-MAY-2016, entry version 95. 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], AND TISSUE SPECIFICITY. 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: Plays a role in vesicle-mediated secretory processes. CC Required for normal accumulation of secretory vesicles in CC hippocampus, pituitary and pancreatic islets. Required for the CC accumulation of normal levels of insulin-containing vesicles and CC preventing their degradation. Plays a role in insulin secretion in CC response to glucose stimuli. Required for normal accumulation of CC the neurotransmitters norepinephrine, dopamine and serotonin in CC the brain. In females, but not in males, required for normal CC accumulation and secretion of pituitary hormones, such as CC luteinizing hormone (LH) and follicle-stimulating hormone (FSH). CC {ECO:0000250|UniProtKB:P80560}. 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|UniProtKB:P80560}; Single-pass type I CC membrane protein {ECO:0000250|UniProtKB:P80560}. Cytoplasmic CC vesicle, secretory vesicle, synaptic vesicle membrane CC {ECO:0000250|UniProtKB:P80560}; Single-pass type I membrane CC protein {ECO:0000250|UniProtKB:P80560}. CC -!- TISSUE SPECIFICITY: Detected in pancreatic islets and adrenal CC medulla. {ECO:0000269|PubMed:9100223}. CC -!- PTM: Subject to proteolytic cleavage at multiple sites. CC {ECO:0000250|UniProtKB:P80560}. 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 SMR; O02695; 722-1008. DR PRIDE; O02695; -. DR GeneID; 105474981; -. DR CTD; 5799; -. DR HOVERGEN; HBG105788; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0010554; P:neurotransmitter secretory pathway; ISS:UniProtKB. 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; IPR003595; Tyr_Pase_cat. 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 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 2: Evidence at transcript level; KW Acetylation; Cell junction; Cytoplasmic vesicle; Glycoprotein; KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Receptor; KW Signal; Synapse; Transmembrane; 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 434 434 Phosphoserine. FT {ECO:0000250|UniProtKB:P80560}. FT MOD_RES 435 435 Phosphoserine. FT {ECO:0000250|UniProtKB:P80560}. FT MOD_RES 690 690 Phosphoserine. FT {ECO:0000250|UniProtKB:P80560}. FT MOD_RES 696 696 Phosphoserine. FT {ECO:0000250|UniProtKB:Q63475}. 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 //