##gff-version 3
P51993	UniProtKB	Chain	1	359	.	.	.	ID=PRO_0000221110;Note=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6	
P51993	UniProtKB	Topological domain	1	14	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Transmembrane	15	34	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Topological domain	35	359	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Region	73	112	.	.	.	Note=Determines site-specific fucosylation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604274;Dbxref=PMID:17604274	
P51993	UniProtKB	Glycosylation	46	46	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Glycosylation	91	91	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Glycosylation	153	153	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P51993	UniProtKB	Alternative sequence	348	359	.	.	.	ID=VSP_001780;Note=In isoform 2. RYQTRGIAAWFT->SGGLIYLRTRLPEASPA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7650030;Dbxref=PMID:7650030	
P51993	UniProtKB	Natural variant	124	124	.	.	.	ID=VAR_024463;Note=Found in individuals with plasma alpha(1%2C3)-fucosyltransferase deficiency and no clinically relevant phenotype%3B results in partial enzyme inactivation%3B complete enzyme inactivation when associated with V-244 and G-303. P->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11102976,ECO:0000269|PubMed:27535533,ECO:0000269|Ref.4;Dbxref=dbSNP:rs778805,PMID:11102976,PMID:27535533	
P51993	UniProtKB	Natural variant	230	230	.	.	.	ID=VAR_024464;Note=Q->K;Dbxref=dbSNP:rs364637	
P51993	UniProtKB	Natural variant	244	244	.	.	.	ID=VAR_065915;Note=Found in individuals with plasma alpha(1%2C3)-fucosyltransferase deficiency and no clinically relevant phenotype%3B complete enzyme inactivation when associated with S-124 and G-303. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102976;Dbxref=PMID:11102976	
P51993	UniProtKB	Natural variant	247	247	.	.	.	ID=VAR_065916;Note=Found in individuals with plasma alpha(1%2C3)-fucosyltransferase deficiency and no clinically relevant phenotype%3B complete enzyme inactivation. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11102976,ECO:0000269|PubMed:27535533,ECO:0000269|PubMed:8175676;Dbxref=dbSNP:rs17855739,PMID:11102976,PMID:27535533,PMID:8175676	
P51993	UniProtKB	Natural variant	303	303	.	.	.	ID=VAR_065917;Note=Found in individuals with plasma alpha(1%2C3)-fucosyltransferase deficiency and no clinically relevant phenotype%3B complete enzyme inactivation when associated with S-124 and V-244. R->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11102976,ECO:0000269|PubMed:27535533;Dbxref=dbSNP:rs61147939,PMID:11102976,PMID:27535533	
P51993	UniProtKB	Mutagenesis	73	73	.	.	.	Note=Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x%3B when associated with W-110%3B D-111 and I-112. Increases VIM2 glycolipid product%3B when associated with W-110%3B D-111 and I-112. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604274;Dbxref=PMID:17604274	
P51993	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Reduces dramatically alpha(1%2C3)fucosyltransferase activity towards type 2 chain acceptors. Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x%3B when associated with T-73%3B D-111 and I-112. Increases VIM2 glycolipid product%3B when associated with T-73%3B D-111 and I-112. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604274;Dbxref=PMID:17604274	
P51993	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x%3B when associated with T-73%3B W-110 and I-112. Increases VIM2 glycolipid product%3B when associated with T-73%3B W-110 and I-112. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604274;Dbxref=PMID:17604274	
P51993	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x%3B when associated with T-73%3B W-110 and D-111. Increases VIM2 glycolipid product%3B when associated with T-73%3B W-110 and D-111. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17604274;Dbxref=PMID:17604274