##gff-version 3
Q92185	UniProtKB	Chain	1	356	.	.	.	ID=PRO_0000149282;Note=Alpha-N-acetylneuraminide alpha-2%2C8-sialyltransferase	
Q92185	UniProtKB	Topological domain	1	29	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Transmembrane	30	48	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Topological domain	49	356	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Active site	322	322	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	143	143	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	166	166	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	274	274	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	275	275	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	276	276	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	296	296	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Binding site	310	310	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Glycosylation	71	71	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Glycosylation	119	119	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Glycosylation	214	214	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Glycosylation	245	245	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92185	UniProtKB	Disulfide bond	138	287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Disulfide bond	152	347	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43173	
Q92185	UniProtKB	Alternative sequence	128	135	.	.	.	ID=VSP_047583;Note=In isoform 2. ATPFQLPL->MQSPSFVK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|Ref.5,ECO:0000303|Ref.6	
Q92185	UniProtKB	Alternative sequence	136	356	.	.	.	ID=VSP_047584;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|Ref.5,ECO:0000303|Ref.6	
Q92185	UniProtKB	Mutagenesis	188	188	.	.	.	Note=Enzyme activity is 42%25 of the wild-type. A 2.5-fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 2.3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348864;Dbxref=PMID:18348864	
Q92185	UniProtKB	Mutagenesis	189	189	.	.	.	Note=Enzyme activity is 91%25 of the wild-type. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348864;Dbxref=PMID:18348864	
Q92185	UniProtKB	Mutagenesis	190	190	.	.	.	Note=Enzyme activity is 33%25 of the wild-type. A 2-fold increase in Km value for ganglioside GM3 and 1.25 fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3. S->A	
Q92185	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Enzyme activity is 20%25 of the wild-type. A 10-fold increase in Km value for ganglioside GM3. A 5-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348864;Dbxref=PMID:18348864	
Q92185	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Enzyme activity is 19%25 of the wild-type. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348864;Dbxref=PMID:18348864	
Q92185	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Enzyme activity is 98%25 of the wild-type. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348864;Dbxref=PMID:18348864