##gff-version 3
Q9ET39	UniProtKB	Signal peptide	1	30	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Chain	31	351	.	.	.	ID=PRO_0000014962;Note=SLAM family member 6	
Q9ET39	UniProtKB	Topological domain	31	239	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Transmembrane	240	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Topological domain	263	351	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Domain	36	130	.	.	.	Note=Ig-like V-type	
Q9ET39	UniProtKB	Domain	147	210	.	.	.	Note=Ig-like C2-type	
Q9ET39	UniProtKB	Region	272	295	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9ET39	UniProtKB	Motif	293	298	.	.	.	Note=ITSM 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291	
Q9ET39	UniProtKB	Motif	317	322	.	.	.	Note=ITSM 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291	
Q9ET39	UniProtKB	Compositional bias	273	295	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9ET39	UniProtKB	Modified residue	319	319	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96DU3	
Q9ET39	UniProtKB	Glycosylation	82	82	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	101	101	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	112	112	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	152	152	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	159	159	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	186	186	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	193	193	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Glycosylation	218	218	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9ET39	UniProtKB	Disulfide bond	162	229	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9ET39	UniProtKB	Disulfide bond	168	210	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q9ET39	UniProtKB	Alternative sequence	305	328	.	.	.	ID=VSP_058034;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21422172;Dbxref=PMID:21422172	
Q9ET39	UniProtKB	Alternative sequence	328	331	.	.	.	ID=VSP_010404;Note=In isoform 2. ETVA->AEYS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11132158;Dbxref=PMID:11132158	
Q9ET39	UniProtKB	Alternative sequence	332	351	.	.	.	ID=VSP_010405;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11132158;Dbxref=PMID:11132158	
Q9ET39	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-319 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	295	295	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-335 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-295 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	319	319	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-335 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-295 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-319 and F-349. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Decreases inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-295 and F-319. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-295 and F-335. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125	
Q9ET39	UniProtKB	Mutagenesis	349	349	.	.	.	Note=Strong inhibitory signaling in germinal center formation (absence of SH2D1A/SAP)%3B when associated with F-319 and F-335. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683125;Dbxref=PMID:22683125