##gff-version 3 P80560 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P80560 UniProtKB Chain 28 1001 . . . ID=PRO_0000025456;Note=Receptor-type tyrosine-protein phosphatase N2 P80560 UniProtKB Chain 414 1001 . . . ID=PRO_0000438090;Note=IA-2beta71;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17611635;Dbxref=PMID:17611635 P80560 UniProtKB Chain 464 1001 . . . ID=PRO_0000438071;Note=IA-2beta64;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17611635;Dbxref=PMID:17611635 P80560 UniProtKB Chain 489 1001 . . . ID=PRO_0000438072;Note=IA-2beta60;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17611635;Dbxref=PMID:17611635 P80560 UniProtKB Topological domain 28 600 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P80560 UniProtKB Transmembrane 601 621 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P80560 UniProtKB Topological domain 622 1001 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P80560 UniProtKB Domain 731 991 . . . Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160 P80560 UniProtKB Region 1 407 . . . Note=Involved in localization to secretory granules%3B interaction with CPE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21210912;Dbxref=PMID:21210912 P80560 UniProtKB Region 271 296 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Region 308 359 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Region 394 459 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Region 663 705 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Motif 652 661 . . . Note=Tyrosine-based internalization motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63475 P80560 UniProtKB Motif 990 996 . . . Note=Leucine-based sorting signal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16262730;Dbxref=PMID:16262730 P80560 UniProtKB Compositional bias 403 459 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Compositional bias 671 705 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P80560 UniProtKB Active site 931 931 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044 P80560 UniProtKB Binding site 899 899 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P80560 UniProtKB Binding site 931 937 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P80560 UniProtKB Binding site 976 976 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P80560 UniProtKB Site 413 414 . . . Note=Cleavage;Ontology_term=ECO:0000250;evidence=ECO:0000250 P80560 UniProtKB Modified residue 259 259 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 P80560 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P80560 UniProtKB Modified residue 422 422 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P80560 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P80560 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P80560 UniProtKB Modified residue 684 684 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63475 P80560 UniProtKB Modified residue 697 697 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63475 P80560 UniProtKB Modified residue 956 956 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92932 P80560 UniProtKB Glycosylation 550 550 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P80560 UniProtKB Mutagenesis 990 991 . . . Note=Impairs localization to secretory granules%2C promotes location at the TGN%2C decreases interaction with alpha- and gamma-type adaptin subunits. EE->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16262730,ECO:0000269|PubMed:21210912;Dbxref=PMID:16262730,PMID:21210912 P80560 UniProtKB Mutagenesis 995 996 . . . Note=Impairs localization to secretory granules%2C promotes location at the plasma membrane%2C defective ind gamma endocytosis%2C highly decreases interaction with alpha- and gamma-type adaptin subunits. IL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262730;Dbxref=PMID:16262730 P80560 UniProtKB Sequence conflict 121 121 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 266 266 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 369 369 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 370 371 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 395 395 . . . Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 411 411 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 414 414 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 586 586 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 P80560 UniProtKB Sequence conflict 662 662 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305