##gff-version 3 P05540 UniProtKB Signal peptide 1 27 . . . . P05540 UniProtKB Chain 28 457 . . . ID=PRO_0000014629;Note=T-cell surface glycoprotein CD4 P05540 UniProtKB Topological domain 28 394 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P05540 UniProtKB Transmembrane 395 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P05540 UniProtKB Topological domain 418 457 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P05540 UniProtKB Domain 28 127 . . . Note=Ig-like V-type P05540 UniProtKB Domain 128 206 . . . Note=Ig-like C2-type 1 P05540 UniProtKB Domain 207 316 . . . Note=Ig-like C2-type 2 P05540 UniProtKB Domain 317 374 . . . Note=Ig-like C2-type 3 P05540 UniProtKB Modified residue 432 432 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01730 P05540 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P01730 P05540 UniProtKB Lipidation 418 418 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P05540 UniProtKB Lipidation 421 421 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P05540 UniProtKB Glycosylation 186 186 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Glycosylation 297 297 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Glycosylation 392 392 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P05540 UniProtKB Disulfide bond 43 111 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Disulfide bond 158 187 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Disulfide bond 328 370 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Mutagenesis 186 186 . . . Note=No change in secretion%3B when associated with S-297. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Mutagenesis 297 297 . . . Note=No change in secretion%3B when associated with T-186. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113054;Dbxref=PMID:2113054 P05540 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 235 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 252 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 261 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 294 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 303 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 321 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 336 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 349 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 365 374 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID P05540 UniProtKB Beta strand 377 385 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CID