##gff-version 3 Q99808 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8986748;Dbxref=PMID:8986748 Q99808 UniProtKB Chain 2 456 . . . ID=PRO_0000209337;Note=Equilibrative nucleoside transporter 1 Q99808 UniProtKB Topological domain 2 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 13 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 30 82 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 83 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 108 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 112 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 131 138 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 139 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 158 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Transmembrane 175 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 200 206 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 228 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 292 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 312 323 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 324 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 343 359 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Transmembrane 360 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 379 393 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Transmembrane 394 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 414 431 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q99808 UniProtKB Topological domain 453 456 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Region 254 276 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99808 UniProtKB Site 277 277 . . . Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Site 288 288 . . . Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Site 414 414 . . . Note=Essential for nucleobase transport;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q99808 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q99808 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q99808 UniProtKB Glycosylation 48 48 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11584005,ECO:0000269|PubMed:19349973;Dbxref=PMID:11584005,PMID:19349973 Q99808 UniProtKB Alternative sequence 1 1 . . . ID=VSP_056579;Note=In isoform 2. M->MRRERTRGPQAWEFPSPTKSGCSLQSLSRDLRELREGEKPEDQAETEESWQGLARKTPGKACAPEGGSCQPGKTENTITM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q99808 UniProtKB Natural variant 216 216 . . . ID=VAR_053668;Note=Decreased inosine transport. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35790189;Dbxref=dbSNP:rs45573936,PMID:35790189 Q99808 UniProtKB Natural variant 293 293 . . . ID=VAR_036221;Note=In a colorectal cancer sample%3B somatic mutation. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q99808 UniProtKB Natural variant 391 391 . . . ID=VAR_053669;Note=E->K;Dbxref=dbSNP:rs45458701 Q99808 UniProtKB Natural variant 455 455 . . . ID=VAR_036222;Note=In a colorectal cancer sample%3B somatic mutation. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs767108156,PMID:16959974 Q99808 UniProtKB Mutagenesis 33 33 . . . Note=No effect on the transport activity for adenosine. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 48 48 . . . Note=Glycosylation-defective. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Mutagenesis 87 87 . . . Note=Loss of nucleobase transport%3B when associated with S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 92 92 . . . Note=Resistance to nitrobenzylmercaptopurine riboside (NBMPR) and dilazep but not dipyridamole. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14759222;Dbxref=PMID:14759222 Q99808 UniProtKB Mutagenesis 92 92 . . . Note=Increase in the transport capacity and decrease in affinity for inosine. Increase in the transport capacity but no change in affinity for adenosine. Resistance to nitrobenzylmercaptopurine riboside (NBMPR) and dilazep but not dipyridamole. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14759222;Dbxref=PMID:14759222 Q99808 UniProtKB Mutagenesis 154 154 . . . Note=Decreased affinity for cytidine and adenosine but not uridine. Resistance to azidothymidine (AZT)%2C dideoxyinosine (ddI)%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C dilazep%2C dipyridamole and hypoxanthine but not dideoxycytidine (ddC). G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037197;Dbxref=PMID:15037197 Q99808 UniProtKB Mutagenesis 179 179 . . . Note=Reduction of the transport activity for adenosine. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 193 193 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 209 209 . . . Note=Reduction of the transport activity for adenosine. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 213 213 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-222%3B S-297%3B S-333%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-222%3B S-297%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 222 222 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-297%3B S-333%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-297%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 277 277 . . . Note=No effect on glycosylation. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Mutagenesis 288 288 . . . Note=No effect on glycosylation. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584005;Dbxref=PMID:11584005 Q99808 UniProtKB Mutagenesis 297 297 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-333%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 308 308 . . . Note=Reduction of the transport activity for adenosine. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 333 333 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-378%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 334 334 . . . Note=Decrease in the transport capacity but no change in affinity for adenosine. Resistance to dipyridamole and dilazep%2C little or no effect on the sensitivities to nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. F->C%2CI%2CV%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 334 334 . . . Note=Increase in the transport capacity but no change in affinity for adenosine. Resistance to dipyridamole and increase in the sensitivity to dilazep. Little or no effect on the sensitivities to nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 338 338 . . . Note=No change in the transport capacity but decrease in affinity for adenosine. Resistance to dipyridamole%2C dilazep%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 338 338 . . . Note=Impaired protein folding and/or altered trafficking. Decrease in the transport capacity but no change in affinity for adenosine. No effect on the sensitivity to dipyridamole. Resistance to dilazep%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. N->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 338 338 . . . Note=Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole%2C dilazep%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. N->M%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 338 338 . . . Note=Impaired protein folding and/or altered trafficking. Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole%2C dilazep%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 338 338 . . . Note=Decrease in the transport capacity and substrate affinity for adenosine. Resistance to dipyridamole%2C dilazep%2C nitrobenzylmercaptopurine riboside (NBMPR)%2C draflazine and soluflazine. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17379602;Dbxref=PMID:17379602 Q99808 UniProtKB Mutagenesis 378 378 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-414%3B S-416 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 390 390 . . . Note=No effect on the transport activity for adenosine. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 414 414 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-416 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 416 416 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-414 and S-439. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378 and S-439. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 439 439 . . . Note=Loss of nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378%3B S-414 and S-416. No change in nucleobase transport%3B when associated with S-87%3B S-193%3B S-213%3B S-222%3B S-297%3B S-333%3B S-378 and S-416. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21795683;Dbxref=PMID:21795683 Q99808 UniProtKB Mutagenesis 442 442 . . . Note=Reduction of the transport activity for adenosine. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27995448;Dbxref=PMID:27995448 Q99808 UniProtKB Mutagenesis 453 456 . . . Note=No effect on subcellular localization and inosine transport. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12527552;Dbxref=PMID:12527552 Q99808 UniProtKB Mutagenesis 453 453 . . . Note=No effect on subcellular localization and inosine transport. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12527552;Dbxref=PMID:12527552 Q99808 UniProtKB Helix 10 12 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 13 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 36 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 77 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 108 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 136 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 170 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 201 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 230 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 237 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 282 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Turn 307 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 311 313 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 325 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 334 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Turn 348 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 360 367 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 368 370 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 371 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Beta strand 380 382 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Beta strand 384 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB6 Q99808 UniProtKB Helix 393 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 418 421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7 Q99808 UniProtKB Helix 424 449 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OB7