##gff-version 3 Q00238 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q00238 UniProtKB Chain 28 545 . . . ID=PRO_0000014788;Note=Intercellular adhesion molecule 1 Q00238 UniProtKB Topological domain 28 492 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Transmembrane 493 517 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Topological domain 518 545 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Domain 41 103 . . . Note=Ig-like C2-type 1 Q00238 UniProtKB Domain 128 193 . . . Note=Ig-like C2-type 2 Q00238 UniProtKB Domain 230 297 . . . Note=Ig-like C2-type 3 Q00238 UniProtKB Domain 325 389 . . . Note=Ig-like C2-type 4 Q00238 UniProtKB Domain 423 476 . . . Note=Ig-like C2-type 5 Q00238 UniProtKB Region 343 365 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q00238 UniProtKB Motif 177 179 . . . Note=Cell attachment site;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 47 47 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 154 154 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 183 183 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 309 309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 344 344 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 396 396 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Glycosylation 464 464 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q00238 UniProtKB Disulfide bond 48 92 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 52 96 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 135 186 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 237 290 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 332 382 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 414 430 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05362 Q00238 UniProtKB Disulfide bond 430 469 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 Q00238 UniProtKB Disulfide bond 442 469 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05362