S28A1_RAT
ID S28A1_RAT Reviewed; 648 AA.
AC Q62674;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Sodium/nucleoside cotransporter 1;
DE AltName: Full=Concentrative nucleoside transporter 1 {ECO:0000303|PubMed:11375981};
DE Short=CNT 1 {ECO:0000303|PubMed:11375981};
DE AltName: Full=Na(+)/nucleoside cotransporter 1 {ECO:0000303|PubMed:11375981};
DE AltName: Full=Sodium-coupled nucleoside transporter 1;
DE AltName: Full=Solute carrier family 28 member 1;
GN Name=Slc28a1; Synonyms=Cnt1 {ECO:0000303|PubMed:11375981};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RX PubMed=8027026; DOI=10.1016/s0021-9258(17)32370-0;
RA Huang Q.-Q., Yao S.Y.M., Ritzel M.W.L., Paterson A.R.P., Cass C.E.,
RA Young J.D.;
RT "Cloning and functional expression of a complementary DNA encoding a
RT mammalian nucleoside transport protein.";
RL J. Biol. Chem. 269:17757-17760(1994).
RN [2]
RP TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT
RP ASN-605 AND ASN-643.
RX PubMed=11375981; DOI=10.1074/jbc.m100518200;
RA Hamilton S.R., Yao S.Y., Ingram J.C., Hadden D.A., Ritzel M.W.,
RA Gallagher M.P., Henderson P.J., Cass C.E., Young J.D., Baldwin S.A.;
RT "Subcellular distribution and membrane topology of the mammalian
RT concentrative Na+-nucleoside cotransporter rCNT1.";
RL J. Biol. Chem. 276:27981-27988(2001).
CC -!- FUNCTION: Sodium-dependent and pyrimidine-selective transporter
CC (PubMed:8027026). Exhibits the transport characteristics of the
CC nucleoside transport system cit or N2 subtype (N2/cit) (selective for
CC pyrimidine nucleosides and adenosine) (PubMed:8027026). Transports
CC uridine, cytidine, thymidine, and nucleoside-derived drugs (By
CC similarity). {ECO:0000250|UniProtKB:O00337,
CC ECO:0000269|PubMed:8027026}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11375981};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11375981}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brush-border
CC membranes of the polarized epithelial cells of jejunum and renal
CC cortical tubules and in the bile canalicular membranes of liver
CC parenchymal cells. {ECO:0000269|PubMed:11375981}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; U10279; AAB03626.1; -; mRNA.
DR PIR; A54892; A54892.
DR RefSeq; NP_446315.1; NM_053863.1.
DR AlphaFoldDB; Q62674; -.
DR SMR; Q62674; -.
DR STRING; 10116.ENSRNOP00000025621; -.
DR ChEMBL; CHEMBL1287615; -.
DR TCDB; 2.A.41.2.2; the concentrative nucleoside transporter (cnt) family.
DR GlyGen; Q62674; 2 sites.
DR iPTMnet; Q62674; -.
DR PaxDb; Q62674; -.
DR GeneID; 116642; -.
DR KEGG; rno:116642; -.
DR CTD; 9154; -.
DR RGD; 621223; Slc28a1.
DR eggNOG; KOG3747; Eukaryota.
DR InParanoid; Q62674; -.
DR OrthoDB; 471043at2759; -.
DR PhylomeDB; Q62674; -.
DR Reactome; R-RNO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR PRO; PR:Q62674; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:1901474; F:azole transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005415; F:nucleoside:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0005350; F:pyrimidine nucleobase transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015389; F:pyrimidine- and adenine-specific:sodium symporter activity; IDA:RGD.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0045117; P:azole transmembrane transport; ISO:RGD.
DR GO; GO:0015861; P:cytidine transport; ISS:UniProtKB.
DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:RGD.
DR GO; GO:0015855; P:pyrimidine nucleobase transport; IDA:RGD.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:RGD.
DR GO; GO:0015862; P:uridine transport; ISS:UniProtKB.
DR InterPro; IPR008276; C_nuclsd_transpt.
DR InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR InterPro; IPR030212; CNT1/CNT2.
DR InterPro; IPR011657; CNT_C_dom.
DR InterPro; IPR002668; CNT_N_dom.
DR InterPro; IPR011642; Gate_dom.
DR PANTHER; PTHR10590; PTHR10590; 1.
DR PANTHER; PTHR10590:SF16; PTHR10590:SF16; 1.
DR Pfam; PF07670; Gate; 1.
DR Pfam; PF07662; Nucleos_tra2_C; 1.
DR Pfam; PF01773; Nucleos_tra2_N; 1.
DR TIGRFAMs; TIGR00804; nupC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..648
FT /note="Sodium/nucleoside cotransporter 1"
FT /id="PRO_0000070449"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..648
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11375981"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11375981"
SQ SEQUENCE 648 AA; 71001 MW; 7618B4436DAED1A8 CRC64;
MADNTQRQRE SISLTPMAHG LENMGAEFLE SMEEGRLPHS HSSLPEGEGG LNKAERKAFS
RWRSLQPTVQ ARSFCREHRQ LFGWICKGLL STACLGFLMV ACLLDLQRAL ALLIITCVVL
VFLAYDLLKR LLGSKLRRCV KFQGHSCLSL WLKRGLALAA GVGLILWLSL DTAQRPEQLV
SFAGICVFLV LLFAGSKHHR AVSWRAVSWG LGLQFVLGLF VIRTEPGFIA FQWLGDQIQV
FLSYTEAGSS FVFGEALVKD VFAFQVLPII IFFSCVMSVL YYLGLMQWVI LKIAWLMQVT
MGTSATETLS VAGNIFVSQT EAPLLIRPYL ADMTLSEVHV VMTGGYATIA GSLLGAYISF
GIDAASLIAA SVMAAPCALA LSKLVYPEVE ESKFRSENGV KLTYGDAQNL LEAASAGAAI
SVKVVANIAA NLIAFLAVLA FVNAALSWLG DMVDIQGLSF QLICSYVLRP VAFLMGVAWE
DCPVVAELLG IKFFLNEFVA YQELSQYKQR RLAGAEEWLG DKKQWISVRA EILTTYALCG
FANFSSIGIM LGGLTSLVPQ RRSDFSQIVL RALITGAFVS LLNACVAGIL YVPRGVEVDC
VSLLNQTVSS SSFEVYLCCR QVFQSTSSEF SQVALDNCCR FYNHTVCT
