##gff-version 3 P09793 UniProtKB Signal peptide 1 35 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Chain 36 223 . . . ID=PRO_0000014735;Note=Cytotoxic T-lymphocyte protein 4 P09793 UniProtKB Topological domain 36 161 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Topological domain 183 223 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Domain 36 145 . . . Note=Ig-like V-type P09793 UniProtKB Region 46 50 . . . Note=Homodimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16410 P09793 UniProtKB Region 134 139 . . . Note=Important for interaction with CD80 and CD86;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16410 P09793 UniProtKB Region 150 155 . . . Note=Homodimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16410 P09793 UniProtKB Modified residue 201 201 . . . Note=Phosphotyrosine%3B by TXK and JAK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16410 P09793 UniProtKB Glycosylation 108 108 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P09793 UniProtKB Disulfide bond 58 129 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11052947,ECO:0007744|PDB:1DQT;Dbxref=PMID:11052947 P09793 UniProtKB Disulfide bond 85 103 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11052947,ECO:0007744|PDB:1DQT;Dbxref=PMID:11052947 P09793 UniProtKB Disulfide bond 157 157 . . . Note=Interchain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P09793 UniProtKB Sequence conflict 182 182 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09793 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 54 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 68 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 81 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DQT P09793 UniProtKB Beta strand 103 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 125 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56 P09793 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E56