##gff-version 3 P16234 UniProtKB Signal peptide 1 23 . . . . P16234 UniProtKB Chain 24 1089 . . . ID=PRO_0000016760;Note=Platelet-derived growth factor receptor alpha P16234 UniProtKB Topological domain 24 528 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Topological domain 550 1089 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Domain 24 113 . . . Note=Ig-like C2-type 1 P16234 UniProtKB Domain 117 201 . . . Note=Ig-like C2-type 2 P16234 UniProtKB Domain 202 306 . . . Note=Ig-like C2-type 3 P16234 UniProtKB Domain 319 410 . . . Note=Ig-like C2-type 4 P16234 UniProtKB Domain 414 517 . . . Note=Ig-like C2-type 5 P16234 UniProtKB Domain 593 954 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16234 UniProtKB Region 1018 1089 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16234 UniProtKB Compositional bias 1029 1044 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16234 UniProtKB Compositional bias 1045 1060 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16234 UniProtKB Active site 818 818 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 P16234 UniProtKB Binding site 599 607 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16234 UniProtKB Binding site 627 627 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P16234 UniProtKB Site 578 579 . . . Note=Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein P16234 UniProtKB Modified residue 572 572 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734113;Dbxref=PMID:10734113 P16234 UniProtKB Modified residue 574 574 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734113;Dbxref=PMID:10734113 P16234 UniProtKB Modified residue 720 720 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095946,ECO:0000269|PubMed:8943348;Dbxref=PMID:11095946,PMID:8943348 P16234 UniProtKB Modified residue 731 731 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1646396;Dbxref=PMID:1646396 P16234 UniProtKB Modified residue 742 742 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1646396;Dbxref=PMID:1646396 P16234 UniProtKB Modified residue 754 754 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604334;Dbxref=PMID:17604334 P16234 UniProtKB Modified residue 762 762 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10733900;Dbxref=PMID:10733900 P16234 UniProtKB Modified residue 768 768 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8617789;Dbxref=PMID:8617789 P16234 UniProtKB Modified residue 849 849 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 P16234 UniProtKB Modified residue 988 988 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7535778;Dbxref=PMID:7535778 P16234 UniProtKB Modified residue 1018 1018 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7535778;Dbxref=PMID:7535778 P16234 UniProtKB Glycosylation 42 42 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 76 76 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 179 179 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 353 353 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 359 359 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 458 458 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16234 UniProtKB Disulfide bond 49 100 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16234 UniProtKB Disulfide bond 150 189 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16234 UniProtKB Disulfide bond 235 290 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16234 UniProtKB Disulfide bond 435 501 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16234 UniProtKB Alternative sequence 210 218 . . . ID=VSP_007833;Note=In isoform 2. ATSELDLEM->GTCIISFLL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P16234 UniProtKB Alternative sequence 219 1089 . . . ID=VSP_007834;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P16234 UniProtKB Alternative sequence 720 743 . . . ID=VSP_042015;Note=In isoform 3. YVILSFENNGDYMDMKQADTTQYV->SGQGCLSSGTLQELSVDLQARGPC;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P16234 UniProtKB Alternative sequence 744 1089 . . . ID=VSP_042016;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P16234 UniProtKB Natural variant 79 79 . . . ID=VAR_042032;Note=G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs36035373,PMID:17344846 P16234 UniProtKB Natural variant 426 426 . . . ID=VAR_042033;Note=G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55865821,PMID:17344846 P16234 UniProtKB Natural variant 478 478 . . . ID=VAR_034378;Note=S->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35597368,PMID:14702039,PMID:15489334,PMID:17344846 P16234 UniProtKB Natural variant 481 481 . . . ID=VAR_066460;Note=In a hypereosinophilic syndrome sample%3B does not lead to constitutive kinase activation. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 507 507 . . . ID=VAR_066461;Note=In a hypereosinophilic syndrome sample%3B does not lead to constitutive kinase activation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 555 555 . . . ID=VAR_083158;Note=In GISTPS%3B increased platelet-derived growth factor alpha-receptor activity%3B constitutively activated kinase. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17087943;Dbxref=dbSNP:rs121908589,PMID:17087943 P16234 UniProtKB Natural variant 561 561 . . . ID=VAR_066462;Note=In a GIST sample%3B constitutively activated kinase. V->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12522257,ECO:0000269|PubMed:15928335;Dbxref=dbSNP:rs121908586,PMID:12522257,PMID:15928335 P16234 UniProtKB Natural variant 562 562 . . . ID=VAR_066463;Note=In a hypereosinophilic syndrome sample%3B does not lead to constitutive kinase activation. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 570 570 . . . ID=VAR_066464;Note=In a hypereosinophilic syndrome sample%3B does not lead to constitutive kinase activation. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 650 650 . . . ID=VAR_066465;Note=In a hypereosinophilic syndrome sample%3B constitutively activated kinase. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 653 653 . . . ID=VAR_083159;Note=In GISTPS%3B uncertain significance. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25975287;Dbxref=PMID:25975287 P16234 UniProtKB Natural variant 659 659 . . . ID=VAR_066466;Note=In GIST sample%3B constitutively activated kinase. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15928335;Dbxref=dbSNP:rs1057519700,PMID:15928335 P16234 UniProtKB Natural variant 659 659 . . . ID=VAR_066467;Note=In a hypereosinophilic syndrome sample%3B constitutively activated kinase. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 705 705 . . . ID=VAR_066468;Note=In a hypereosinophilic syndrome sample%3B does not lead to constitutive kinase activation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 748 748 . . . ID=VAR_066469;Note=In a hypereosinophilic syndrome sample%3B constitutively activated kinase. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 764 764 . . . ID=VAR_042034;Note=R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34392012,PMID:17344846 P16234 UniProtKB Natural variant 829 829 . . . ID=VAR_042035;Note=In a glioblastoma multiforme sample%3B somatic mutation. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P16234 UniProtKB Natural variant 842 845 . . . ID=VAR_066470;Note=In a GIST sample%3B constitutively activated kinase. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12522257,ECO:0000269|PubMed:15928335;Dbxref=PMID:12522257,PMID:15928335 P16234 UniProtKB Natural variant 842 842 . . . ID=VAR_066471;Note=In a GIST sample%3B imatinib resistant%2C constitutively activated kinase. D->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12522257,ECO:0000269|PubMed:15928335,ECO:0000269|PubMed:20972453;Dbxref=dbSNP:rs121908585,PMID:12522257,PMID:15928335,PMID:20972453 P16234 UniProtKB Natural variant 842 842 . . . ID=VAR_066472;Note=In a GIST sample%3B imatinib sensitive%2C constitutively activated kinase. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15928335;Dbxref=dbSNP:rs121913265,PMID:15928335 P16234 UniProtKB Natural variant 845 848 . . . ID=VAR_066473;Note=In a GIST sample%3B constitutively activated kinase. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12522257,ECO:0000269|PubMed:15928335;Dbxref=PMID:12522257,PMID:15928335 P16234 UniProtKB Natural variant 846 846 . . . ID=VAR_083160;Note=In GISTPS%3B uncertain significance. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14699510;Dbxref=dbSNP:rs121908588,PMID:14699510 P16234 UniProtKB Natural variant 849 849 . . . ID=VAR_066474;Note=In GIST. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15928335;Dbxref=PMID:15928335 P16234 UniProtKB Natural variant 849 849 . . . ID=VAR_066475;Note=In a hypereosinophilic syndrome sample%3B constitutively activated kinase. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21224473;Dbxref=PMID:21224473 P16234 UniProtKB Natural variant 996 996 . . . ID=VAR_042036;Note=In a metastatic melanoma sample%3B somatic mutation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs779173667,PMID:17344846 P16234 UniProtKB Natural variant 1071 1071 . . . ID=VAR_042037;Note=In a lung neuroendocrine carcinoma sample%3B somatic mutation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs376544204,PMID:17344846 P16234 UniProtKB Mutagenesis 572 572 . . . Note=Abolishes interaction with SRC-family members and impairs internalization of the activated receptor%3B when associated with F-574. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10734113,ECO:0000269|PubMed:14644164;Dbxref=PMID:10734113,PMID:14644164 P16234 UniProtKB Mutagenesis 574 574 . . . Note=Abolishes interaction with SRC-family members and impairs internalization of the activated receptor%3B when associated with F-572. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10734113,ECO:0000269|PubMed:14644164;Dbxref=PMID:10734113,PMID:14644164 P16234 UniProtKB Mutagenesis 720 720 . . . Note=Strongly reduced interaction with PTPN11 and GRB2. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8943348;Dbxref=PMID:8943348 P16234 UniProtKB Mutagenesis 731 731 . . . Note=No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1646396;Dbxref=PMID:1646396 P16234 UniProtKB Mutagenesis 742 742 . . . Note=No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1646396;Dbxref=PMID:1646396 P16234 UniProtKB Mutagenesis 762 762 . . . Note=Abolishes interaction with CRK. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10733900;Dbxref=PMID:10733900 P16234 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 46 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Turn 62 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RAM P16234 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RAM P16234 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 107 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 124 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RAM P16234 UniProtKB Beta strand 133 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 159 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Turn 174 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 184 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 197 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 203 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 216 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 224 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 266 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 270 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 286 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 301 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 308 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LBF P16234 UniProtKB Beta strand 560 565 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Beta strand 567 570 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Beta strand 572 574 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Helix 577 579 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Helix 584 586 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6JOL P16234 UniProtKB Helix 590 592 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 593 601 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 603 614 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 616 618 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 620 629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 635 651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 660 664 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 666 669 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 671 675 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 678 681 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6JOJ P16234 UniProtKB Helix 682 688 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 690 696 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Helix 769 774 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32 P16234 UniProtKB Helix 778 781 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5K5X P16234 UniProtKB Helix 792 811 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 821 823 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 824 827 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Turn 828 830 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 831 834 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 838 840 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 843 845 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 849 851 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Beta strand 853 857 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 859 861 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 864 869 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 874 889 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 903 910 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 923 932 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 937 939 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 943 953 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GRN P16234 UniProtKB Helix 956 971 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6A32