##gff-version 3 P70658 UniProtKB Chain 1 359 . . . ID=PRO_0000069355;Note=C-X-C chemokine receptor type 4 P70658 UniProtKB Topological domain 1 40 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 41 65 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 66 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 80 101 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 102 112 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 113 132 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 133 156 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 157 176 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 177 202 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 203 223 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 224 248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 249 268 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 269 289 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Transmembrane 290 309 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Topological domain 310 359 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70658 UniProtKB Region 1 23 . . . Note=Important for chemokine binding and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 96 99 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 115 119 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 137 149 . . . Note=Involved in dimerization%3B when bound to chemokine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 193 197 . . . Note=Chemokine binding%2C important for signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 198 217 . . . Note=Involved in dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 273 275 . . . Note=Involved in dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Region 335 359 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P70658 UniProtKB Motif 135 137 . . . Note=Important for signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Compositional bias 342 359 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P70658 UniProtKB Site 173 173 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Site 295 295 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Modified residue 9 9 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 14 14 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 23 23 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P70658 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine%3B by PKC and GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine%3B by PKC and GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine%3B by GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine%3B by GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Glycosylation 13 13 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70658 UniProtKB Glycosylation 20 20 . . . Note=O-linked (Xyl...) (chondroitin sulfate) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Disulfide bond 30 281 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 P70658 UniProtKB Disulfide bond 111 193 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 P70658 UniProtKB Cross-link 338 338 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 P70658 UniProtKB Alternative sequence 6 7 . . . ID=VSP_001891;Note=In isoform CXCR4-A. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9295051;Dbxref=PMID:9295051 P70658 UniProtKB Sequence conflict 216 216 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305