##gff-version 3
P15153	UniProtKB	Chain	1	189	.	.	.	ID=PRO_0000042046;Note=Ras-related C3 botulinum toxin substrate 2	
P15153	UniProtKB	Propeptide	190	192	.	.	.	ID=PRO_0000042047;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Motif	32	40	.	.	.	Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P15153	UniProtKB	Binding site	10	17	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Binding site	57	61	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Binding site	115	118	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Modified residue	39	39	.	.	.	Note=ADP-ribosylasparagine%3B by botulinum toxin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Modified residue	147	147	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
P15153	UniProtKB	Modified residue	189	189	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P15153	UniProtKB	Lipidation	189	189	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1903399;Dbxref=PMID:1903399	
P15153	UniProtKB	Glycosylation	32	32	.	.	.	Note=O-linked (GlcNAc) tyrosine%3B by Photorhabdus PAU_02230;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24141704;Dbxref=PMID:24141704	
P15153	UniProtKB	Natural variant	29	29	.	.	.	ID=VAR_036569;Note=In a breast cancer sample%3B somatic mutation. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974	
P15153	UniProtKB	Natural variant	34	34	.	.	.	ID=VAR_085472;Note=In IMD73B%3B uncertain significance%3B increased interaction with PAK1 compared to wild-type%3B potential gain-of-function variant. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30654050;Dbxref=dbSNP:rs1927393826,PMID:30654050	
P15153	UniProtKB	Natural variant	56	192	.	.	.	ID=VAR_085473;Note=In IMD73C%3B strong decrease in protein expression. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25512081;Dbxref=PMID:25512081	
P15153	UniProtKB	Natural variant	57	57	.	.	.	ID=VAR_017452;Note=In IMD73A%3B dominant-negative mutant%3B binds GDP%2C but not GTP%3B inhibits oxidase activation and superoxide anion production in vitro. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10758162;Dbxref=dbSNP:rs74315507,PMID:10758162	
P15153	UniProtKB	Natural variant	62	62	.	.	.	ID=VAR_085474;Note=In IMD73B%3B gain-of-function variant%3B exhibits impaired GAP-mediated GTP hydrolysis%2C resulting in sustained GTP association and prolonged RAC2-driven activation of downstream effectors%3B when transfected into cells%2C shows increased basal reactive oxygen species production following stimulation by PMA compared to cells transfected with wild-type%3B increased interaction with PAK1%2C compared to wild-type. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30723080,ECO:0000269|PubMed:31382036;Dbxref=dbSNP:rs1555908409,PMID:30723080,PMID:31382036	
P15153	UniProtKB	Natural variant	92	92	.	.	.	ID=VAR_085475;Note=In IMD73B%3B uncertain significance%3B cells transfected with this variant show higher production of reactive oxygen species compared to wild-type%3B potential gain-of-function variant. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31071452;Dbxref=dbSNP:rs1927078072,PMID:31071452	
P15153	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Abolishes in vitro prenylation. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1903399;Dbxref=PMID:1903399	
P15153	UniProtKB	Beta strand	3	11	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	16	25	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	39	46	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	49	56	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	62	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Turn	65	67	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	68	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	77	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	87	95	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	97	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	106	108	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	110	115	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	117	119	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	123	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Turn	131	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	139	149	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Beta strand	152	156	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Turn	159	161	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T	
P15153	UniProtKB	Helix	165	175	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W2T