##gff-version 3
P01501	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P01501	UniProtKB	Propeptide	22	43	.	.	.	ID=PRO_0000035148;Note=Removed by a dipeptidylpeptidase;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:20403370,ECO:0000305|PubMed:20472009,ECO:0000305|PubMed:5592400;Dbxref=PMID:20403370,PMID:20472009,PMID:5592400	
P01501	UniProtKB	Peptide	44	69	.	.	.	ID=PRO_0000035149;Note=Melittin;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20403370,ECO:0000269|PubMed:20472009,ECO:0000269|PubMed:5592400;Dbxref=PMID:20403370,PMID:20472009,PMID:5592400	
P01501	UniProtKB	Site	57	57	.	.	.	Note=Important for the flexibility at the center of the helix%2C flexibility that is important for the stability of the voltage-gated pore;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2187536;Dbxref=PMID:2187536	
P01501	UniProtKB	Modified residue	44	44	.	.	.	Note=N-formylglycine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:5139483;Dbxref=PMID:5139483	
P01501	UniProtKB	Modified residue	69	69	.	.	.	Note=Glutamine amide;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:5592400;Dbxref=PMID:5592400	
P01501	UniProtKB	Natural variant	53	53	.	.	.	Note=In melittin-S. T->S	
P01501	UniProtKB	Natural variant	64	64	.	.	.	Note=In melittin-2%3B possibly an artifact. K->S	
P01501	UniProtKB	Natural variant	66	66	.	.	.	Note=In melittin-2%3B possibly an artifact. K->KK	
P01501	UniProtKB	Mutagenesis	44	57	.	.	.	Note=Very important decrease of hemolytic activity and capacity of lowering the surface tension of aqueous solutions. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:5139482;Dbxref=PMID:5139482	
P01501	UniProtKB	Mutagenesis	53	53	.	.	.	Note=In MelP5%3B increase in size of pores (10-12 monomers) that form at lower concentrations of the toxin%3B when associated with 65--A--L-69. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28720433;Dbxref=PMID:28720433	
P01501	UniProtKB	Mutagenesis	57	57	.	.	.	Note=Loss of flexibility in the center of the helix%2C is twice as effective as melittin as a hemolytic agent but has very poor voltage-gated pore activity in planar bilayers and voltage-dependent ion conductionce is supported only at very high ionic strengths. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2187536;Dbxref=PMID:2187536	
P01501	UniProtKB	Mutagenesis	65	69	.	.	.	Note=In MelP5%3B increase in size of pores (10-12 monomers) that form at lower concentrations of the toxin%3B when associated with 65--A--L-69. RKRQQ->AAQQL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28720433;Dbxref=PMID:28720433	
P01501	UniProtKB	Helix	45	54	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6O4M	
P01501	UniProtKB	Helix	56	61	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6O4M	
P01501	UniProtKB	Helix	64	68	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6O4M