##gff-version 3 P01730 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15340161,ECO:0000269|PubMed:2592374;Dbxref=PMID:15340161,PMID:2592374 P01730 UniProtKB Chain 26 458 . . . ID=PRO_0000014621;Note=T-cell surface glycoprotein CD4 P01730 UniProtKB Topological domain 26 396 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01730 UniProtKB Transmembrane 397 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01730 UniProtKB Topological domain 419 458 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P01730 UniProtKB Domain 26 125 . . . Note=Ig-like V-type P01730 UniProtKB Domain 126 203 . . . Note=Ig-like C2-type 1 P01730 UniProtKB Domain 204 317 . . . Note=Ig-like C2-type 2 P01730 UniProtKB Domain 318 374 . . . Note=Ig-like C2-type 3 P01730 UniProtKB Region 427 455 . . . Note=HIV-1 Vpu-susceptibility domain P01730 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2105883;Dbxref=PMID:2105883 P01730 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2105883;Dbxref=PMID:2105883 P01730 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2105883;Dbxref=PMID:2105883 P01730 UniProtKB Lipidation 419 419 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1618861;Dbxref=PMID:1618861 P01730 UniProtKB Lipidation 422 422 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1618861;Dbxref=PMID:1618861 P01730 UniProtKB Glycosylation 296 296 . . . ID=CAR_000053;Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:2001369,ECO:0000269|PubMed:2592374;Dbxref=PMID:19159218,PMID:2001369,PMID:2592374 P01730 UniProtKB Glycosylation 325 325 . . . ID=CAR_000054;Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2001369,ECO:0000269|PubMed:2592374;Dbxref=PMID:2001369,PMID:2592374 P01730 UniProtKB Disulfide bond 41 109 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2592374;Dbxref=PMID:2592374 P01730 UniProtKB Disulfide bond 155 184 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2592374;Dbxref=PMID:2592374 P01730 UniProtKB Disulfide bond 328 370 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:2592374;Dbxref=PMID:2592374 P01730 UniProtKB Natural variant 191 191 . . . ID=VAR_023459;Note=K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs28917504 P01730 UniProtKB Natural variant 227 227 . . . ID=VAR_023460;Note=F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8;Dbxref=dbSNP:rs11064419 P01730 UniProtKB Natural variant 265 265 . . . ID=VAR_003906;Note=In OKT4-negative populations. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1708753,ECO:0000269|PubMed:1961196,ECO:0000269|Ref.8;Dbxref=dbSNP:rs28919570,PMID:1708753,PMID:1961196 P01730 UniProtKB Mutagenesis 65 65 . . . Note=Increases the affinity for MHCII%3B when associated with W-70%3B R-85 and R-88. Q->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21900604;Dbxref=PMID:21900604 P01730 UniProtKB Mutagenesis 68 68 . . . Note=Abrogates the interaction with MHCII and T cell activation. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7604010;Dbxref=PMID:7604010 P01730 UniProtKB Mutagenesis 70 70 . . . Note=Increases the affinity for MHCII%3B when associated with Y-65%3B R-85 and R-88. T->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21900604;Dbxref=PMID:21900604 P01730 UniProtKB Mutagenesis 85 85 . . . Note=Increases the affinity for MHCII%3B when associated with Y-65%3B W-70 and R-88. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21900604;Dbxref=PMID:21900604 P01730 UniProtKB Mutagenesis 88 88 . . . Note=Increases the affinity for MHCII%3B when associated with Y-65%3B W-70 and R-85. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21900604;Dbxref=PMID:21900604 P01730 UniProtKB Mutagenesis 265 265 . . . Note=Has no effect on the interaction with MHCII. Impairs recognition by OKT4 antibody. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7604010;Dbxref=PMID:7604010 P01730 UniProtKB Mutagenesis 432 432 . . . Note=No effect. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8124721;Dbxref=PMID:8124721 P01730 UniProtKB Mutagenesis 433 433 . . . Note=About 75%25 loss of internalization. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2105883;Dbxref=PMID:2105883 P01730 UniProtKB Mutagenesis 433 433 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8124721;Dbxref=PMID:8124721 P01730 UniProtKB Mutagenesis 438 439 . . . Note=Loss of Nef-induced CD4 down-modulation. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8124721;Dbxref=PMID:8124721 P01730 UniProtKB Mutagenesis 440 440 . . . Note=No effect. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8124721;Dbxref=PMID:8124721 P01730 UniProtKB Mutagenesis 445 445 . . . Note=Loss of homodimerization%3B when associated with A-447. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9168119;Dbxref=PMID:9168119 P01730 UniProtKB Mutagenesis 447 447 . . . Note=Loss of homodimerization%3B when associated with A-445. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9168119;Dbxref=PMID:9168119 P01730 UniProtKB Mutagenesis 457 458 . . . Note=Abolished interaction with SPG21 and induced T-cell activation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11113139;Dbxref=PMID:11113139 P01730 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQA P01730 UniProtKB Beta strand 60 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 73 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NY6 P01730 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Helix 84 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 105 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 114 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NY1 P01730 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1G9N P01730 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 158 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CDJ P01730 UniProtKB Beta strand 162 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 180 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Beta strand 191 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4H8W P01730 UniProtKB Helix 398 421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KLU P01730 UniProtKB Beta strand 426 428 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KLU P01730 UniProtKB Helix 432 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3B71 P01730 UniProtKB Beta strand 440 442 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBR