##gff-version 3 Q9BSW2 UniProtKB Chain 1 731 . . . ID=PRO_0000283046;Note=EF-hand calcium-binding domain-containing protein 4B Q9BSW2 UniProtKB Domain 84 119 . . . Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Region 1 45 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BSW2 UniProtKB Region 349 540 . . . Note=Proline-rich domain (PRD) which mediates interaction with VAV1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27016526;Dbxref=PMID:27016526 Q9BSW2 UniProtKB Region 426 466 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BSW2 UniProtKB Region 494 528 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9BSW2 UniProtKB Coiled coil 201 382 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9BSW2 UniProtKB Binding site 97 97 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Binding site 99 99 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Binding site 101 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Binding site 103 103 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Binding site 108 108 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 Q9BSW2 UniProtKB Binding site 552 559 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63000 Q9BSW2 UniProtKB Binding site 600 604 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63000 Q9BSW2 UniProtKB Binding site 659 661 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63000 Q9BSW2 UniProtKB Lipidation 729 729 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27016526;Dbxref=PMID:27016526 Q9BSW2 UniProtKB Alternative sequence 374 395 . . . ID=VSP_060977;Note=In isoform 1. ERNKHLRDERDICFQKNKAAKA->CVGGHWPVLRAPPRSLGSEGPV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9BSW2 UniProtKB Alternative sequence 396 731 . . . ID=VSP_060978;Note=In isoform 1. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9BSW2 UniProtKB Natural variant 7 7 . . . ID=VAR_031483;Note=R->G;Dbxref=dbSNP:rs9788233 Q9BSW2 UniProtKB Natural variant 98 98 . . . ID=VAR_031484;Note=A->T;Dbxref=dbSNP:rs17836273 Q9BSW2 UniProtKB Natural variant 128 128 . . . ID=VAR_031485;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs242017,PMID:15489334 Q9BSW2 UniProtKB Natural variant 136 136 . . . ID=VAR_031486;Note=H->P;Dbxref=dbSNP:rs34088152 Q9BSW2 UniProtKB Natural variant 154 154 . . . ID=VAR_031487;Note=E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs242018,PMID:15489334 Q9BSW2 UniProtKB Natural variant 212 212 . . . ID=VAR_031488;Note=H->Q;Dbxref=dbSNP:rs36030417 Q9BSW2 UniProtKB Mutagenesis 63 63 . . . Note=Loss of calcium-binding and interaction with the dynein-dynactin complex%3B when associated with A-65%3B A-97 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30814157;Dbxref=PMID:30814157 Q9BSW2 UniProtKB Mutagenesis 65 65 . . . Note=Loss of calcium-binding and interaction with the dynein-dynactin complex%3B when associated with A-63%3B A-97 and A-99. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30814157;Dbxref=PMID:30814157 Q9BSW2 UniProtKB Mutagenesis 97 99 . . . Note=In EF2MUT%3B enhanced STIM1 clustering and elevated cytoplasmic Ca2+%2C thereby causing cell death in T-cells. Loss of calcium-binding. Can rescue JNK phosphorylation when expressed in CRACR2A-depleted T-cells. No effect on its localization to the Golgi membrane. DAD->AAA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20418871,ECO:0000269|PubMed:27016526,ECO:0000269|PubMed:31092558;Dbxref=PMID:20418871,PMID:27016526,PMID:31092558 Q9BSW2 UniProtKB Mutagenesis 97 97 . . . Note=Loss of calcium-binding and interaction with the dynein-dynactin complex%3B when associated with A-63%3B A-65 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30814157;Dbxref=PMID:30814157 Q9BSW2 UniProtKB Mutagenesis 99 99 . . . Note=Loss of calcium-binding and interaction with the dynein-dynactin complex%3B when associated with A-63%3B A-65 and A-97. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30814157;Dbxref=PMID:30814157 Q9BSW2 UniProtKB Mutagenesis 559 559 . . . Note=GDP-binding mutant with reduced GTPase activity and protein stability. Reduced ability to activate JNK signaling pathway. Failure to localize to the microtubule organizing center and Golgi apparatus membrane%2C instead shows a predominant localization to the cytoplasm. T->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27016526,ECO:0000269|PubMed:31092558;Dbxref=PMID:27016526,PMID:31092558 Q9BSW2 UniProtKB Mutagenesis 604 604 . . . Note=GTP-binding mutant with reduced GTPase activity but increased protein stability. Increased ability to activate JNK signaling pathway. No effect on its localization to the microtubule organizing center or Golgi apparatus membrane. Q->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27016526,ECO:0000269|PubMed:31092558;Dbxref=PMID:27016526,PMID:31092558 Q9BSW2 UniProtKB Mutagenesis 658 658 . . . Note=GTP/GDP-binding defective mutant with reduced GTPase activity and protein stability. Failure to localize to the microtubule organizing center and Golgi apparatus membrane%2C instead shows a predominant localization to the cytoplasm. N->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27016526,ECO:0000269|PubMed:31092558;Dbxref=PMID:27016526,PMID:31092558 Q9BSW2 UniProtKB Mutagenesis 729 731 . . . Note=Failure to localize to the Golgi membrane. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27016526;Dbxref=PMID:27016526 Q9BSW2 UniProtKB Sequence conflict 424 424 . . . Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BSW2 UniProtKB Helix 48 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Helix 86 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD Q9BSW2 UniProtKB Helix 106 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6PSD