SLC29A1
entrez
2030
canonical
uniprot
Q99808
canonical
ensembl
ENSG00000112759
resolver
ensp
ENSP00000360789
resolver
ensp
ENSP00000360820
resolver
ensp
ENSP00000562079
resolver
ensp
ENSP00000562092
resolver
ensp
ENSP00000562101
resolver
ensp
ENSP00000562110
resolver
ensp
ENSP00000637846
resolver
ensp
ENSP00000637865
resolver
ensp
ENSP00000637866
resolver
genesymbol
SLC29A1
resolver
genesymbol_syn
ENT1
resolver
hgnc
HGNC:11003
resolver
uniprot
B3KQV7
resolver
uniprot
B3KQY5
resolver
uniprot
Q5T9W9
resolver
uniprot
Q9UJY2
resolver
uniprot_entry
S29A1_HUMAN
resolver
uniprot_sec
B3KQV7
resolver
uniprot_sec
B3KQY5
resolver
uniprot_sec
Q5T9W9
resolver
uniprot_sec
Q9UJY2
resolver
activity_regulation
ACTIVITY REGULATION: Transporter activity is sensitive to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) (PubMed:10722669, PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:21795683, PubMed:26406980, PubMed:27995448, PubMed:8986748). Inhibited by dilazep (PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:39737929). Inhibited by dipyridamole (PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:39737929). Inhibited by hypoxanthine (PubMed:15037197). Inhibited by azidothymidine (AZT) (PubMed:15037197). Inhibited by dideoxycytidine (ddC) (PubMed:15037197). Inhibited by dideoxyinosine (ddI) (PubMed:15037197). Inhibited by draflazine (PubMed:17379602). Inhibited by soluflazine (PubMed:17379602). Inhibited by cladribine (PubMed:27995448). Inhibited by capecitabine (PubMed:27995448). Inhibited by clofarabine (PubMed:27995448). Inhibited by ribavirin (PubMed:27995448). Modestly inhibited by acyclovir (PubMed:27995448). Modestly inhibited by 5-fluorouracil (PubMed:27995448). {ECO:0000269|PubMed:10722669, ECO:0000269|PubMed:14759222, ECO:0000269|PubMed:15037197, ECO:0000269|PubMed:17379602, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:26406980, ECO:0000269|PubMed:27995448, ECO:0000269|PubMed:39737929, ECO:0000269|PubMed:8986748}.
uniprot
proteins
amino_acid_sequence
MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARLVFVPLLLLCNIKPRRYLTVVFEHDAWFIFFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGAIMAFFLCLGLALGAVFSFLFRAIV
uniprot
proteins
function
FUNCTION: Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:10722669, PubMed:10755314, PubMed:12527552, PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:21795683, PubMed:26406980, PubMed:27995448, PubMed:35790189, PubMed:8986748). Functions as a Na(+)-independent transporter (PubMed:8986748). Involved in the transport of nucleosides such as adenosine, guanosine, inosine, uridine, thymidine and cytidine (PubMed:10722669, PubMed:10755314, PubMed:12527552, PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:26406980, PubMed:8986748, PubMed:39737929). Also transports purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (PubMed:21795683, PubMed:27995448). Also mediates the uptake of nicotinamide; contributes to maintaining nicotinamide homeostasis but also regulated nicotinamide biological roles (PubMed:39885119). Mediates basolateral nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis barrier (By similarity). Regulates inosine levels in brown adipocytes tissues (BAT) and extracellular inosine levels, which controls BAT-dependent energy expenditure (PubMed:35790189). {ECO:0000250|UniProtKB:O54698, ECO:0000269|PubMed:10722669, ECO:0000269|PubMed:10755314, ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:14759222, ECO:0000269|PubMed:15037197, ECO:0000269|PubMed:17379602, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:23639800, ECO:0000269|PubMed:26406980, ECO:0000269|PubMed:27995448, ECO:0000269|PubMed:35790189, ECO:0000269|PubMed:39737929, ECO:0000269|PubMed:39885119, ECO:0000269|PubMed:8986748}.
uniprot
proteins
mass_dalton
50219
uniprot
proteins
mutagenesis
MUTAGEN 30; /note="N->A: Decreased nicotinamide transport activity."; /evidence="ECO:0000269|PubMed:39885119"; MUTAGEN 33; /note="M->I: No effect on the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 48; /note="N->Q: Glycosylation-defective."; /evidence="ECO:0000269|PubMed:11584005"; MUTAGEN 87; /note="C->S: Loss of nucleobase transport; when associated with S-193; S-213; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-193; S-213; S-222; S-297; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 92; /note="L->P: Resistance to nitrobenzylmercaptopurine riboside (NBMPR) and dilazep but not dipyridamole."; /evidence="ECO:0000269|PubMed:14759222"; MUTAGEN 92; /note="L->Q: 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."; /evidence="ECO:0000269|PubMed:14759222"; MUTAGEN 154; /note="G->S: Decreased affinity for cytidine and adenosine but not uridine. Resistance to azidothymidine (AZT), dideoxyinosine (ddI), nitrobenzylmercaptopurine riboside (NBMPR), dilazep, dipyridamole and hypoxanthine but not dideoxycytidine (ddC)."; /evidence="ECO:0000269|PubMed:15037197"; MUTAGEN 179; /note="G->L: Reduction of the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 193; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-213; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-213; S-222; S-297; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 209; /note="F->A: Reduction of the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 213; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-222; S-297; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 222; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-297; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 277; /note="N->Q: No effect on glycosylation."; /evidence="ECO:0000269|PubMed:11584005"; MUTAGEN 288; /note="N->Q: No effect on glycosylation."; /evidence="ECO:0000269|PubMed:11584005"; MUTAGEN 297; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 308; /note="P->A: Reduction of the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 333; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 334; /note="F->C,I,V,S: Decrease in the transport capacity but no change in affinity for adenosine. Resistance to dipyridamole and dilazep, little or no effect on the sensitivities to nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 334; /note="F->Y: 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), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 338; /note="N->A: No change in the transport capacity but decrease in affinity for adenosine. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 338; /note="N->C: 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, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 338; /note="N->M,D: Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 338; /note="N->Q: Impaired protein folding and/or altered trafficking. Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 338; /note="N->S: Decrease in the transport capacity and substrate affinity for adenosine. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine."; /evidence="ECO:0000269|PubMed:17379602"; MUTAGEN 341; /note="D->A: Decreased nicotinamide transport activity."; /evidence="ECO:0000269|PubMed:39885119"; MUTAGEN 378; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 390; /note="F->A: No effect on the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 407; /note="N->A: Decreased nicotinamide transport activity."; /evidence="ECO:0000269|PubMed:39885119"; MUTAGEN 414; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-416 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 416; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-414 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378 and S-439."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 439; /note="C->S: Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-414 and S-416. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378 and S-416."; /evidence="ECO:0000269|PubMed:21795683"; MUTAGEN 442; /note="L->I: Reduction of the transport activity for adenosine."; /evidence="ECO:0000269|PubMed:27995448"; MUTAGEN 453..456; /note="Missing: No effect on subcellular localization and inosine transport."; /evidence="ECO:0000269|PubMed:12527552"; MUTAGEN 453; /note="R->A: No effect on subcellular localization and inosine transport."; /evidence="ECO:0000269|PubMed:12527552
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:10722669, ECO:0000269|PubMed:19349973}.
uniprot
proteins
protein_family
SLC29A/ENT transporter (TC 2.A.57) family
uniprot
proteins
pubmed
10722669
uniprot
proteins
pubmed
10755314
uniprot
proteins
pubmed
11311901
uniprot
proteins
pubmed
11584005
uniprot
proteins
pubmed
12384580
uniprot
proteins
pubmed
12527552
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14759222
uniprot
proteins
pubmed
15037197
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15501974
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17379602
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21795683
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23219802
uniprot
proteins
pubmed
23639800
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26406980
uniprot
proteins
pubmed
27995448
uniprot
proteins
pubmed
31235912
uniprot
proteins
pubmed
35790189
uniprot
proteins
pubmed
39737929
uniprot
proteins
pubmed
39885119
uniprot
proteins
pubmed
8986748
uniprot
proteins
sequence_length
456
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:23639800}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11584005, ECO:0000269|PubMed:15501974, ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:26406980}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basolateral membrane of Sertoli cells (PubMed:23639800). Localized to the cell membrane of erythrocytes (PubMed:11584005, PubMed:23219802). {ECO:0000269|PubMed:11584005, ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:23639800}.
uniprot
proteins
transmembrane_region
TRANSMEM 15..36; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 80..103; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 109..131; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 141..163; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 173..194; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 203..224; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 289..312; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 329..350; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 359..377; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 394..416; /note="Helical; Name=10"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6"; TRANSMEM 431..450; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:31235912, ECO:0007744|PDB:6OB6
uniprot
proteins