##gff-version 3
P46638	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Chain	2	215	.	.	.	ID=PRO_0000121159;Note=Ras-related protein Rab-11B	
P46638	UniProtKB	Propeptide	216	218	.	.	.	ID=PRO_0000370816;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51157	
P46638	UniProtKB	Region	184	218	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P46638	UniProtKB	Motif	40	48	.	.	.	Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P46638	UniProtKB	Compositional bias	196	218	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P46638	UniProtKB	Binding site	18	26	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Binding site	66	70	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Binding site	124	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Binding site	154	156	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylglycine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Modified residue	4	4	.	.	.	Note=Citrulline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24463520;Dbxref=PMID:24463520	
P46638	UniProtKB	Modified residue	215	215	.	.	.	Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51157	
P46638	UniProtKB	Lipidation	214	214	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Lipidation	215	215	.	.	.	Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15907	
P46638	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Dominant negative mutant locked in the inactive GDP-bound form%3B partially relocalizes to the Golgi and alters endocytic recycling. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10942597;Dbxref=PMID:10942597	
P46638	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Constitutively active mutant locked in the active GTP-bound form%3B alters endocytic recycling. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10942597;Dbxref=PMID:10942597