##gff-version 3 Q9QUM4 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Chain 25 343 . . . ID=PRO_0000014960;Note=Signaling lymphocytic activation molecule Q9QUM4 UniProtKB Topological domain 25 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Transmembrane 243 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Topological domain 266 343 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Domain 29 138 . . . Note=Ig-like V-type Q9QUM4 UniProtKB Domain 145 228 . . . Note=Ig-like C2-type Q9QUM4 UniProtKB Region 320 343 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9QUM4 UniProtKB Motif 286 291 . . . Note=ITSM 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291 Q9QUM4 UniProtKB Motif 313 318 . . . Note=SH2-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Motif 333 338 . . . Note=ITSM 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291 Q9QUM4 UniProtKB Compositional bias 325 343 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9QUM4 UniProtKB Modified residue 288 288 . . . Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291 Q9QUM4 UniProtKB Modified residue 315 315 . . . Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291 Q9QUM4 UniProtKB Modified residue 335 335 . . . Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13291 Q9QUM4 UniProtKB Glycosylation 54 54 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 58 58 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 126 126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 151 151 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 158 158 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 211 211 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Glycosylation 226 226 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9QUM4 UniProtKB Disulfide bond 161 232 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q9QUM4 UniProtKB Disulfide bond 167 212 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q9QUM4 UniProtKB Alternative sequence 296 343 . . . ID=VSP_002570;Note=In isoform Short. PQEKKLHDALTDQDPCTTIYVAATEPAPESVQEPNPTTVYASVTLPES->VRSMPHLAGVSVIFRTGFLIAALHTTMVLQGLLE;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10570270;Dbxref=PMID:10570270 Q9QUM4 UniProtKB Mutagenesis 288 288 . . . Note=Greatly reduces SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11477403;Dbxref=PMID:11477403 Q9QUM4 UniProtKB Mutagenesis 315 315 . . . Note=Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation%2C no effect on interaction with SH2D1A%3B when associated with A-335. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11477403;Dbxref=PMID:11477403 Q9QUM4 UniProtKB Mutagenesis 335 335 . . . Note=Abolishes SLAMF1:SH2D1A-mediated intracellular tyrosine phosphorylation%2C no effect on interaction with SH2D1A%3B when associated with A-315. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11477403;Dbxref=PMID:11477403