##gff-version 3 P09215 UniProtKB Chain 1 673 . . . ID=PRO_0000055696;Note=Protein kinase C delta type P09215 UniProtKB Chain 1 327 . . . ID=PRO_0000421671;Note=Protein kinase C delta type regulatory subunit P09215 UniProtKB Chain 328 673 . . . ID=PRO_0000421672;Note=Protein kinase C delta type catalytic subunit P09215 UniProtKB Domain 1 106 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P09215 UniProtKB Domain 347 601 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P09215 UniProtKB Domain 602 673 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 P09215 UniProtKB Zinc finger 158 208 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P09215 UniProtKB Zinc finger 230 280 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P09215 UniProtKB Active site 471 471 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P09215 UniProtKB Binding site 353 361 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P09215 UniProtKB Binding site 376 376 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P09215 UniProtKB Site 48 48 . . . Note=Interaction with phosphotyrosine-containing peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P09215 UniProtKB Site 62 62 . . . Note=Interaction with phosphotyrosine-containing peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P09215 UniProtKB Site 67 67 . . . Note=Interaction with phosphotyrosine-containing peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P09215 UniProtKB Site 123 123 . . . Note=Interaction with phosphotyrosine-containing peptide;Ontology_term=ECO:0000250;evidence=ECO:0000250 P09215 UniProtKB Site 327 328 . . . Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09215 UniProtKB Modified residue 43 43 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28867 P09215 UniProtKB Modified residue 50 50 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 64 64 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17562707;Dbxref=PMID:17562707 P09215 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 141 141 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 155 155 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17562707;Dbxref=PMID:17562707 P09215 UniProtKB Modified residue 218 218 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 311 311 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18550549,ECO:0007744|PubMed:22673903;Dbxref=PMID:18550549,PMID:22673903 P09215 UniProtKB Modified residue 332 332 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18550549;Dbxref=PMID:18550549 P09215 UniProtKB Modified residue 372 372 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 449 449 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 505 505 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17569658,ECO:0000269|PubMed:18550549,ECO:0000269|PubMed:9677322;Dbxref=PMID:17569658,PMID:18550549,PMID:9677322 P09215 UniProtKB Modified residue 565 565 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 643 643 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P09215 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05655 P09215 UniProtKB Modified residue 662 662 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16396499,ECO:0007744|PubMed:22673903;Dbxref=PMID:16396499,PMID:22673903 P09215 UniProtKB Alternative sequence 327 673 . . . ID=VSP_004742;Note=In isoform 2. DNNGTYGKIWEGSNRCRLENFTFQKVLGKGSFGKVLLAELKGKERYFAIKYLKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRATFYAAEIICGLQFLHGKGIIYRDLKLDNVMLDKDGHIKIADFGMCKENIFGENRASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDIMEKLFERDPAKRLGVTGNIRLHPFFKTINWNLLEKRKVEPPFKPKVKSPSDYSNFDPEFLNEKPQLSFSDKNLIDSMDQTAFKGFSFVNPKYEQFLE->GESGSHIPLKLPFPDRAREKNSSETWDKTTTGPMARSGRGATGAALRTSPSRKYLAKAALARYCLQN;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10708593;Dbxref=PMID:10708593 P09215 UniProtKB Mutagenesis 505 505 . . . Note=Decrease in the phosphorylation level. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9677322;Dbxref=PMID:9677322 P09215 UniProtKB Sequence conflict 147 147 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09215 UniProtKB Sequence conflict 249 249 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09215 UniProtKB Beta strand 3 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 27 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 68 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 79 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Helix 88 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 113 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BDY P09215 UniProtKB Beta strand 233 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Turn 245 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Beta strand 258 261 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Turn 262 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3 P09215 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LF3