ID S28A1_MOUSE Reviewed; 648 AA. AC E9PXX9; Q6P8I9; DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Sodium/nucleoside cotransporter 1 {ECO:0000250|UniProtKB:O00337}; DE AltName: Full=Concentrative nucleoside transporter 1; DE Short=CNT 1; DE AltName: Full=Na(+)/nucleoside cotransporter 1; DE AltName: Full=Sodium-coupled nucleoside transporter 1; DE AltName: Full=Solute carrier family 28 member 1 {ECO:0000312|MGI:MGI:3605073}; GN Name=Slc28a1 {ECO:0000312|MGI:MGI:3605073}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma CC membrane that imports uridine, thymidine and cytidine into cells by CC coupling their transport to the transmembrane sodium electrochemical CC gradient. Also transports adenosine, an atypical substrate transported CC with high apparent affinity, but low maximum velocity. Therefore, CC exhibits the transport characteristics of the nucleoside transport CC system cit or N2 subtype (N2/cit). Involved in renal nucleoside CC (re)absorption. {ECO:0000250|UniProtKB:O00337}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); CC Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; CC Evidence={ECO:0000250|UniProtKB:O00337}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Na(+)(out) + thymidine(out) = Na(+)(in) + thymidine(in); CC Xref=Rhea:RHEA:69891, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101; CC Evidence={ECO:0000250|UniProtKB:O00337}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine(out) + Na(+)(out) = cytidine(in) + Na(+)(in); CC Xref=Rhea:RHEA:69895, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101; CC Evidence={ECO:0000250|UniProtKB:O00337}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); CC Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; CC Evidence={ECO:0000250|UniProtKB:O00337}; CC -!- ACTIVITY REGULATION: Due to its high apparent affinity but slow CC transport, adenosine could act as a negative regulator of pyrimidine CC transport under some conditions. {ECO:0000250|UniProtKB:O00337}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00337}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell CC membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q62674}. CC -!- PTM: N-glycosylated. N-glycosylation is required for localization to CC the plasma membrane and the transporter activity. CC {ECO:0000250|UniProtKB:O00337}. CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT) CC (TC 2.A.41) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC061230; AAH61230.1; -; mRNA. DR CCDS; CCDS21402.1; -. DR RefSeq; NP_001004184.2; NM_001004184.3. DR RefSeq; XP_006541039.1; XM_006540976.3. DR RefSeq; XP_006541040.1; XM_006540977.3. DR RefSeq; XP_006541041.1; XM_006540978.3. DR RefSeq; XP_006541042.1; XM_006540979.3. DR AlphaFoldDB; E9PXX9; -. DR SMR; E9PXX9; -. DR STRING; 10090.ENSMUSP00000112421; -. DR GlyCosmos; E9PXX9; 3 sites, No reported glycans. DR GlyGen; E9PXX9; 3 sites. DR PhosphoSitePlus; E9PXX9; -. DR PaxDb; 10090-ENSMUSP00000026820; -. DR ProteomicsDB; 339181; -. DR Antibodypedia; 65918; 80 antibodies from 19 providers. DR DNASU; 434203; -. DR Ensembl; ENSMUST00000026820.11; ENSMUSP00000026820.5; ENSMUSG00000025726.12. DR Ensembl; ENSMUST00000119083.2; ENSMUSP00000112421.2; ENSMUSG00000025726.12. DR GeneID; 434203; -. DR KEGG; mmu:434203; -. DR UCSC; uc009ibs.1; mouse. DR AGR; MGI:3605073; -. DR CTD; 9154; -. DR MGI; MGI:3605073; Slc28a1. DR VEuPathDB; HostDB:ENSMUSG00000025726; -. DR eggNOG; KOG3747; Eukaryota. DR GeneTree; ENSGT00390000016025; -. DR HOGENOM; CLU_016813_3_2_1; -. DR InParanoid; E9PXX9; -. DR OMA; IVWHTVI; -. DR OrthoDB; 1333063at2759; -. DR PhylomeDB; E9PXX9; -. DR TreeFam; TF314131; -. DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane. DR BioGRID-ORCS; 434203; 3 hits in 76 CRISPR screens. DR ChiTaRS; Slc28a1; mouse. DR PRO; PR:E9PXX9; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; E9PXX9; Protein. DR Bgee; ENSMUSG00000025726; Expressed in proximal tubule and 27 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0031526; C:brush border membrane; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:1901474; F:azole transmembrane transporter activity; ISO:MGI. DR GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; ISO:MGI. DR GO; GO:0015389; F:pyrimidine- and adenosine-specific:sodium symporter activity; ISS:UniProtKB. DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:MGI. DR GO; GO:0045117; P:azole transmembrane transport; ISO:MGI. DR GO; GO:0015861; P:cytidine transport; ISO:MGI. DR GO; GO:0180015; P:nucleoside import across plasma membrane; ISS:UniProtKB. DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:MGI. DR GO; GO:0015855; P:pyrimidine nucleobase transport; ISO:MGI. DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:MGI. DR GO; GO:0015862; P:uridine transport; ISO:MGI. DR InterPro; IPR008276; C_nuclsd_transpt. DR InterPro; IPR018270; C_nuclsd_transpt_met_bac. DR InterPro; IPR011657; CNT_C_dom. DR InterPro; IPR002668; CNT_N_dom. DR InterPro; IPR011642; Gate_dom. DR NCBIfam; TIGR00804; nupC; 1. DR PANTHER; PTHR10590; SODIUM/NUCLEOSIDE COTRANSPORTER; 1. DR PANTHER; PTHR10590:SF16; SODIUM_NUCLEOSIDE COTRANSPORTER 1; 1. DR Pfam; PF07670; Gate; 1. DR Pfam; PF07662; Nucleos_tra2_C; 1. DR Pfam; PF01773; Nucleos_tra2_N; 1. PE 2: Evidence at transcript level; KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..648 FT /note="Sodium/nucleoside cotransporter 1" FT /id="PRO_0000455292" FT TOPO_DOM 1..83 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 105..108 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 130..147 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 148..168 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 169..175 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 197..201 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 202..222 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 223..265 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 287..294 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 295..318 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 319..339 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 361 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 362..380 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 381..427 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 428..448 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 449..470 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 471..491 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 492..531 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 532..552 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 553..571 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT TRANSMEM 572..592 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 593..648 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q62674" FT CARBOHYD 605 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 625 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 643 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 96 FT /note="G -> S (in Ref. 2; AAH61230)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="K -> E (in Ref. 2; AAH61230)" FT /evidence="ECO:0000305" SQ SEQUENCE 648 AA; 71174 MW; C32DCEA9133147E1 CRC64; MADDTPRQRE SISLTPVAHG LENMGAEFLE IMEEGQLPHR HSSLPEGGGS RSKAVWKPFS RWRSLQPTVQ ARSLCREHWQ LFEWISKGLL STAYIGFLIV ACLLDFPRAL ALFVITCVVL VFLAYNLLKR LLGSKLKKCV KFQGHSCLSL WLKRGLALAA GLGVILWLSL DTAQRPEQLV SFAGICVFLV LLFAGSKHHR AVSWRAVSWG LGLQFVLGLF VIRTEPGFVA FQWLGDQIRV FLSYTEAGSS FVFGEALVKD VFAFQVLPII VFFSCVMSVL YYLGLMQWVI LKIAWLMQVT MGTSATETLS VAGNIFVSQT EAPLLIRPYL ADMTLSEVHV VMTGGYATIA GSLLGAYISF GIDASSLIAA SVMAAPCALA LSKLVYPEVE ESKFRSEEGV KLTYGDAQNL VEAASAGAAI SVKVVANIAA NLIAFLAVLA FINAALSWLG DMVDIQGLSF QLICSYVLRP VAFLMGVAWE DCPVVAELLG IKLFLNEFVA YQELSQYKQR RLAGAEEWLG DKKQWISVRA EILTTYALCG FANFSSIGIM LGGLTSMVPQ RRSDFSQIVL RALITGAFVS LVNACVAGIL YVPRGVEVDC MSLLNQTVSS SSFEVYLCCR QVFQNTSLEF GQEALHNCCR FYNHTVCT //