##gff-version 3 O54890 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Chain 26 787 . . . ID=PRO_0000016345;Note=Integrin beta-3 O54890 UniProtKB Topological domain 26 717 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Transmembrane 718 740 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Topological domain 741 787 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Domain 29 75 . . . Note=PSI;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Domain 134 376 . . . Note=VWFA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Domain 435 497 . . . Note=EGF-like 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Domain 498 547 . . . Note=EGF-like 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Domain 548 584 . . . Note=EGF-like 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Domain 585 628 . . . Note=EGF-like 4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Region 202 209 . . . Note=CX3CL1-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Region 202 209 . . . Note=Involved in CX3CL1-%2C NRG1-%2C FGF1- and IGF1-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Region 292 312 . . . Note=CX3CL1-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Motif 776 782 . . . Note=LIR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 146 146 . . . Note=In MIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 148 148 . . . Note=In ADMIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 148 148 . . . Note=In MIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 151 151 . . . Note=In ADMIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 152 152 . . . Note=In ADMIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 183 183 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 240 240 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 242 242 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 244 244 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 245 245 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 245 245 . . . Note=In MIDAS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 276 276 . . . Note=In ADMIDAS binding site and liganded-open conformation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Binding site 276 276 . . . Note=In LIMBS binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Modified residue 766 766 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 O54890 UniProtKB Modified residue 772 772 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Modified residue 778 778 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Modified residue 784 784 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Glycosylation 345 345 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Glycosylation 396 396 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Glycosylation 477 477 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Glycosylation 584 584 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Glycosylation 679 679 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O54890 UniProtKB Disulfide bond 30 48 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 38 460 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 41 63 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 51 74 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 202 209 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 257 298 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 399 411 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 431 458 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 462 482 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 473 485 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 487 496 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 498 528 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 511 526 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 520 531 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 533 546 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 548 569 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 553 567 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 561 572 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 574 583 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 585 608 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 592 606 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 600 611 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 613 623 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 626 629 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 633 680 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 639 660 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 642 656 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Disulfide bond 688 712 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05106 O54890 UniProtKB Mutagenesis 58 59 . . . Note=Mice display deficits in anxiety as well as in repetitive and social behaviors. Decreases levels of serotonin synapses in midbrain%2C SLC6A4 activity and location at integrin adhesion complexes in synapses. QG->PP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29038237;Dbxref=PMID:29038237 O54890 UniProtKB Sequence conflict 114 114 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O54890 UniProtKB Sequence conflict 389 389 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 O54890 UniProtKB Beta strand 777 780 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XQ1