##gff-version 3
Q13291	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Chain	21	335	.	.	.	ID=PRO_0000014959;Note=Signaling lymphocytic activation molecule	
Q13291	UniProtKB	Topological domain	21	237	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Transmembrane	238	258	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Topological domain	259	335	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Domain	29	138	.	.	.	Note=Ig-like V-type	
Q13291	UniProtKB	Domain	144	223	.	.	.	Note=Ig-like C2-type	
Q13291	UniProtKB	Motif	279	284	.	.	.	Note=ITSM 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11823424;Dbxref=PMID:11823424	
Q13291	UniProtKB	Motif	307	312	.	.	.	Note=SH2-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Motif	325	330	.	.	.	Note=ITSM 2;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:11313386,ECO:0000305|PubMed:11806999;Dbxref=PMID:11313386,PMID:11806999	
Q13291	UniProtKB	Modified residue	281	281	.	.	.	Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11689425,ECO:0000269|PubMed:11806999;Dbxref=PMID:11689425,PMID:11806999	
Q13291	UniProtKB	Modified residue	307	307	.	.	.	Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Glycosylation	53	53	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	57	57	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	102	102	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	150	150	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	155	155	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	189	189	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13291	UniProtKB	Disulfide bond	158	228	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q13291	UniProtKB	Disulfide bond	164	209	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q13291	UniProtKB	Alternative sequence	234	263	.	.	.	ID=VSP_002567;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7617038;Dbxref=PMID:7617038	
Q13291	UniProtKB	Alternative sequence	264	335	.	.	.	ID=VSP_058033;Note=In isoform 4. GKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVPESVQETNSITVYASVTLPES->ATLTTTNQYWSQNVLTQDQERCPGCLPMVKRTITRQQWKKKALRSMPKSRNQVLFRRNLTPSQLRTLAPPYMLLPQSLSQSLSRKQIPSQSMLV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:25710480;Dbxref=PMID:25710480	
Q13291	UniProtKB	Alternative sequence	289	298	.	.	.	ID=VSP_002568;Note=In isoform 2. PLQKKLDSFP->DTHHQTSDLF;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7617038;Dbxref=PMID:7617038	
Q13291	UniProtKB	Alternative sequence	299	335	.	.	.	ID=VSP_002569;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7617038;Dbxref=PMID:7617038	
Q13291	UniProtKB	Natural variant	11	11	.	.	.	ID=VAR_021924;Note=F->L;Dbxref=dbSNP:rs2295612	
Q13291	UniProtKB	Natural variant	81	81	.	.	.	ID=VAR_035524;Note=In a breast cancer sample%3B somatic mutation. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs1373814964,PMID:16959974	
Q13291	UniProtKB	Natural variant	333	333	.	.	.	ID=VAR_021925;Note=P->T;Dbxref=dbSNP:rs3796504	
Q13291	UniProtKB	Mutagenesis	269	269	.	.	.	Note=No effect on interaction with INPP5D/SHIP-1%2C PTPN11/SHP-2 and SH2D1A. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11313386;Dbxref=PMID:11313386	
Q13291	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Disrupts interaction with SH2D1A%3B when associated with A-325. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Mutagenesis	281	281	.	.	.	Note=Disrupts interaction with INPP5D/SHIP-1 and PTPN11/SHP-2%2C no effect on interaction with SH2D1A. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11313386,ECO:0000269|PubMed:11806999;Dbxref=PMID:11313386,PMID:11806999	
Q13291	UniProtKB	Mutagenesis	281	281	.	.	.	Note=Disrupts interaction with SH2D1A%3B when associated with F-327. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Mutagenesis	307	307	.	.	.	Note=No effect on interaction with PTPN11/SHP-2 and SH2D1A. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11313386;Dbxref=PMID:11313386	
Q13291	UniProtKB	Mutagenesis	325	325	.	.	.	Note=Disrupts interaction with SH2D1A%3B when associated with A-279. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Disrupts interaction with INPP5D/SHIP-1 and PTPN11/SHP-2%2C no effect on interaction with SH2D1A. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11313386,ECO:0000269|PubMed:11806999;Dbxref=PMID:11313386,PMID:11806999	
Q13291	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Disrupts interaction with SH2D1A%3B when associated with F-281. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11806999;Dbxref=PMID:11806999	
Q13291	UniProtKB	Beta strand	278	281	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D4T