##gff-version 3 P25106 UniProtKB Chain 1 362 . . . ID=PRO_0000070101;Note=Atypical chemokine receptor 3 P25106 UniProtKB Topological domain 1 40 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 41 61 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 62 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 82 102 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 103 118 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 119 139 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 140 162 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 163 183 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 184 213 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 214 234 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 235 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 253 273 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 274 296 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Transmembrane 297 319 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Topological domain 320 362 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Region 324 362 . . . Note=C-terminal cytoplasmic tail P25106 UniProtKB Modified residue 347 347 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56485 P25106 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56485 P25106 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56485 P25106 UniProtKB Glycosylation 13 13 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Glycosylation 22 22 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Glycosylation 39 39 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25106 UniProtKB Disulfide bond 117 196 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521 P25106 UniProtKB Natural variant 219 219 . . . ID=VAR_027477;Note=L->W;Dbxref=dbSNP:rs10183641 P25106 UniProtKB Natural variant 258 258 . . . ID=VAR_085335;Note=In OCABSN%3B no effect on protein levels and cell membrane location%3B lower binding affinity for CXCL12. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31211835;Dbxref=dbSNP:rs200582844,PMID:31211835 P25106 UniProtKB Mutagenesis 145 145 . . . Note=Does not result in CXCL12-inducible chemotaxis%2C calcium mobilization or ERK activation%2C and has no effect on CXCR7-mediated CXCL12 degradation%3B when associated with V-147. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20161793;Dbxref=PMID:20161793 P25106 UniProtKB Mutagenesis 147 147 . . . Note=Does not result in CXCL12-inducible chemotaxis%2C calcium mobilization or ERK activation%2C and has no effect on CXCR7-mediated CXCL12 degradation%3B when associated with A-145. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20161793;Dbxref=PMID:20161793 P25106 UniProtKB Sequence conflict 9 9 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25106 UniProtKB Sequence conflict 130 130 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25106 UniProtKB Sequence conflict 131 131 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25106 UniProtKB Sequence conflict 228 228 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25106 UniProtKB Sequence conflict 360 361 . . . Note=ST->NA;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25106 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 40 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 81 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 97 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 114 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 154 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Beta strand 183 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Turn 189 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 205 217 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Turn 218 221 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 222 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 245 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 252 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Helix 287 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4 P25106 UniProtKB Turn 316 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK8 P25106 UniProtKB Helix 320 330 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SK4