##gff-version 3
Q8VIM0	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Chain	20	281	.	.	.	ID=PRO_0000042102;Note=Hepatitis A virus cellular receptor 2 homolog	
Q8VIM0	UniProtKB	Topological domain	20	193	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Transmembrane	194	214	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Topological domain	215	281	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Domain	20	125	.	.	.	Note=Ig-like V-type	
Q8VIM0	UniProtKB	Region	139	160	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8VIM0	UniProtKB	Region	252	270	.	.	.	Note=Interaction with BAG6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22863785;Dbxref=PMID:22863785	
Q8VIM0	UniProtKB	Binding site	61	61	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	62	62	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	112	112	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	115	115	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	117	117	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	119	119	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Binding site	120	120	.	.	.	Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphotyrosine%3B by ITK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8TDQ0	
Q8VIM0	UniProtKB	Glycosylation	74	74	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Glycosylation	100	100	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Glycosylation	146	146	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8TDQ0	
Q8VIM0	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8VIM0	UniProtKB	Disulfide bond	38	111	.	.	.	Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Disulfide bond	52	63	.	.	.	Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Disulfide bond	58	110	.	.	.	Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:20083673,ECO:0007744|PDB:3KAA;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Alternative sequence	133	217	.	.	.	ID=VSP_058116;Note=In isoform 2. AKVTPAQTAHGDSTTASPRTLTTERNGSETQTLVTLHNNNGTKISTWADEIKDSGETIRTAIHIGVGVSAGLTLALIIGVLILKW->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14556006;Dbxref=PMID:14556006	
Q8VIM0	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Greatly decreases phosphatidylserine binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20083673;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Mutagenesis	60	62	.	.	.	Note=Decreases phosphatidylserine binding. WSQ->VFE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20083673;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Mutagenesis	62	62	.	.	.	Note=No effect on phagocytic activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19224762;Dbxref=PMID:19224762	
Q8VIM0	UniProtKB	Mutagenesis	112	112	.	.	.	Note=Abolishes phagocytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19224762;Dbxref=PMID:19224762	
Q8VIM0	UniProtKB	Mutagenesis	118	119	.	.	.	Note=Decreases phosphatidylserine binding. LM->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20083673;Dbxref=PMID:20083673	
Q8VIM0	UniProtKB	Mutagenesis	120	121	.	.	.	Note=Decreases phosphatidylserine binding%2C abolishes phagocytic activity. ND->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19224762,ECO:0000269|PubMed:20083673;Dbxref=PMID:19224762,PMID:20083673	
Q8VIM0	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Abolishes phosphorylation%2C disrupts interaction with PIK3R1 and PIK3R2%2C no LGALS9-mediated disruption of interaction with BAG6%3B when associated with F-263. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21807895,ECO:0000269|PubMed:22863785;Dbxref=PMID:21807895,PMID:22863785	
Q8VIM0	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Abolishes phosphorylation%2C disrupts interaction with PIK3R1 and PIK3R2%2C no LGALS9-mediated disruption of interaction with BAG6%3B when associated with F-256. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21807895,ECO:0000269|PubMed:22863785;Dbxref=PMID:21807895,PMID:22863785	
Q8VIM0	UniProtKB	Beta strand	26	28	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	51	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	60	62	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	66	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	72	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	81	85	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Helix	89	91	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	96	100	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Helix	103	105	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	107	113	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	116	119	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA	
Q8VIM0	UniProtKB	Beta strand	125	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KAA