S28A1_PIG
ID S28A1_PIG Reviewed; 647 AA.
AC O62667;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Sodium/nucleoside cotransporter 1;
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;
GN Name=SLC28A1; Synonyms=CNT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney cortex;
RX PubMed=9858747; DOI=10.1016/s0005-2736(98)00192-8;
RA Pajor A.M.;
RT "Sequence of a pyrimidine-selective Na+/nucleoside cotransporter from pig
RT kidney, pkCNT1.";
RL Biochim. Biophys. Acta 1415:266-269(1998).
CC -!- FUNCTION: Sodium-dependent and pyrimidine-selective transporter.
CC Exhibits the transport characteristics of the nucleoside transport
CC system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides
CC and adenosine). Transports uridine, cytidine, thymidine, and
CC nucleoside-derived drugs. {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 -!- 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:0000250|UniProtKB:O00337};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O00337}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; AF009673; AAC17947.1; -; mRNA.
DR RefSeq; NP_999277.1; NM_214112.1.
DR AlphaFoldDB; O62667; -.
DR SMR; O62667; -.
DR STRING; 9823.ENSSSCP00000002842; -.
DR PaxDb; O62667; -.
DR GeneID; 397200; -.
DR KEGG; ssc:397200; -.
DR CTD; 9154; -.
DR eggNOG; KOG3747; Eukaryota.
DR InParanoid; O62667; -.
DR OrthoDB; 471043at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005415; F:nucleoside:sodium symporter activity; IEA:InterPro.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015861; P:cytidine transport; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..647
FT /note="Sodium/nucleoside cotransporter 1"
FT /id="PRO_0000070447"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 34..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 647 AA; 70823 MW; EB93804706FAFD63 CRC64;
MEDNTPRQRD PISLTSVANG LENMGAELLE SLEEGRAPGS DSSPAEVGGG WSKAGPEHLG
RRSLQPALRV RRFCREHTQL FRWICTGLLC TAFAAFLLIA CLLDFQRALA LFVLFCVVLF
FLAHSLLKRL LGPKLLRCVK PLRHPCLNLW FKRGLALAAF LGLVLWLVLD TAQRPEQLVS
FGGICVFILL LFAGSKHHRA VSWRAVSWGL GLQFALGLFV IRTEPGFIAF QWLGDQIQIF
LSYTEAGSSF VFGEALVKDV FAFQVLPIIV FFSCAMSVLY YVGLMQWVIL KISWLMQATM
GTTATETLSV AGNIFVSQTE APLLIRPYLA DMTLSEIHVV MTGGYATIAG SLLGAYISFG
IDAASLIAAS VMAAPCALAL SKLVYPEVEE SKFKREEGVK LTYGDAQNLL EAASSGAAMS
VRVVTNIAAN LIAFLAVLAF INAALSWLGD MVDVQGLSFQ LICSYVLRPV AFLMGVAWED
CPVVAELLGM KLFLNEFVAY QELSGYKQRR LAGAEEWVGS RKQWISVRAE ILTTYALCGF
ANFSSIGIML GGLTSMVPQR KGDFSQIVLR ALCTGACVSL VNACVAGILY VPRGAEVDCV
SFLNTTLSSS SFEVYQCCRQ FFQSTSLEFS PEALDNCCRF YNHTICV
