##gff-version 3 O08565 UniProtKB Chain 1 349 . . . ID=PRO_0000069358;Note=C-X-C chemokine receptor type 4 O08565 UniProtKB Topological domain 1 35 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 36 60 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 61 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 75 96 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 97 107 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 108 127 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 128 151 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 152 171 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 172 192 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 193 213 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 214 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 239 258 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 259 279 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Transmembrane 280 299 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Topological domain 300 349 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 O08565 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08565 UniProtKB Region 1 18 . . . Note=Important for chemokine binding and signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 91 94 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 110 114 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 132 144 . . . Note=Involved in dimerization%3B when bound to chemokine;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 183 187 . . . Note=Chemokine binding%2C important for signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 188 207 . . . Note=Involved in dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 263 265 . . . Note=Involved in dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Region 325 349 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08565 UniProtKB Motif 130 132 . . . Note=Important for signaling;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Compositional bias 1 15 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08565 UniProtKB Compositional bias 332 349 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08565 UniProtKB Site 168 168 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Site 285 285 . . . Note=Chemokine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Modified residue 9 9 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 18 18 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine%3B by PKC and GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine%3B by PKC and GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine%3B by GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine%3B by GRK6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Modified residue 348 348 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Glycosylation 8 8 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08565 UniProtKB Glycosylation 15 15 . . . Note=O-linked (Xyl...) (chondroitin sulfate) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Disulfide bond 25 271 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 O08565 UniProtKB Disulfide bond 106 183 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 O08565 UniProtKB Cross-link 328 328 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61073 O08565 UniProtKB Sequence conflict 143 144 . . . Note=RP->SA