##gff-version 3 P05129 UniProtKB Chain 1 697 . . . ID=PRO_0000055689;Note=Protein kinase C gamma type P05129 UniProtKB Domain 157 275 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P05129 UniProtKB Domain 351 614 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05129 UniProtKB Domain 615 685 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 P05129 UniProtKB Zinc finger 35 85 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P05129 UniProtKB Zinc finger 100 150 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P05129 UniProtKB Active site 480 480 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P05129 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 193 193 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 247 247 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 251 251 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.14 P05129 UniProtKB Binding site 357 365 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05129 UniProtKB Binding site 380 380 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05129 UniProtKB Modified residue 250 250 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 P05129 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 332 332 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 373 373 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 514 514 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 648 648 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255 P05129 UniProtKB Modified residue 655 655 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 674 674 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63318 P05129 UniProtKB Modified residue 675 675 . . . Note=Phosphotyrosine%3B by SYK;Ontology_term=ECO:0000250;evidence=ECO:0000250 P05129 UniProtKB Modified residue 687 687 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63319 P05129 UniProtKB Alternative sequence 1 20 . . . ID=VSP_056467;Note=In isoform 2. MAGLGPGVGDSEGGPRPLFC->MPRICDLRVSRRWEGPPDGR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P05129 UniProtKB Alternative sequence 21 133 . . . ID=VSP_056468;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P05129 UniProtKB Alternative sequence 553 588 . . . ID=VSP_056469;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P05129 UniProtKB Natural variant 63 63 . . . ID=VAR_080740;Note=In SCA14. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29053796;Dbxref=PMID:29053796 P05129 UniProtKB Natural variant 63 63 . . . ID=VAR_080741;Note=In SCA14. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29053796;Dbxref=dbSNP:rs386134159,PMID:29053796 P05129 UniProtKB Natural variant 101 101 . . . ID=VAR_017060;Note=In SCA14. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12644968;Dbxref=dbSNP:rs121918511,PMID:12644968 P05129 UniProtKB Natural variant 119 119 . . . ID=VAR_017061;Note=In SCA14. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12644968;Dbxref=dbSNP:rs121918512,PMID:12644968 P05129 UniProtKB Natural variant 128 128 . . . ID=VAR_017062;Note=In SCA14. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12644968;Dbxref=dbSNP:rs121918513,PMID:12644968 P05129 UniProtKB Natural variant 141 141 . . . ID=VAR_008755;Note=R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545390;Dbxref=PMID:9545390 P05129 UniProtKB Natural variant 415 415 . . . ID=VAR_008756;Note=H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545390;Dbxref=PMID:9545390 P05129 UniProtKB Natural variant 523 523 . . . ID=VAR_008757;Note=A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545390;Dbxref=PMID:9545390 P05129 UniProtKB Natural variant 659 659 . . . ID=VAR_008758;Note=R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9545390;Dbxref=dbSNP:rs752933837,PMID:9545390 P05129 UniProtKB Sequence conflict 314 317 . . . Note=RVRM->VSRT;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05129 UniProtKB Turn 50 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E73 P05129 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E73 P05129 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E73 P05129 UniProtKB Helix 75 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E73 P05129 UniProtKB Turn 86 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2E73 P05129 UniProtKB Beta strand 160 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 172 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 194 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 222 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Helix 233 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 239 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 254 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Helix 263 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Beta strand 271 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP P05129 UniProtKB Helix 280 283 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2UZP