S28A1_RABIT
ID S28A1_RABIT Reviewed; 658 AA.
AC Q9MZT2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Small intestine;
RX PubMed=11028933; DOI=10.1023/a:1007510801253;
RA Gerstin K.M., Dresser M.J., Wang J., Giacomini K.M.;
RT "Molecular cloning of a Na+-dependent nucleoside transporter from rabbit
RT intestine.";
RL Pharm. Res. 17:906-910(2000).
CC -!- FUNCTION: Sodium-dependent and pyrimidine-selective transporter
CC (PubMed:11028933). Exhibits the transport characteristics of the
CC nucleoside transport system cit or N2 subtype (N2/cit) (selective for
CC pyrimidine nucleosides and adenosine) (PubMed:11028933). Transports
CC uridine, cytidine, thymidine, and nucleoside-derived drugs (By
CC similarity). {ECO:0000250|UniProtKB:O00337,
CC ECO:0000269|PubMed:11028933}.
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; AF161716; AAF80451.1; -; mRNA.
DR RefSeq; NP_001076260.1; NM_001082791.1.
DR AlphaFoldDB; Q9MZT2; -.
DR SMR; Q9MZT2; -.
DR STRING; 9986.ENSOCUP00000012330; -.
DR PRIDE; Q9MZT2; -.
DR GeneID; 100009595; -.
DR KEGG; ocu:100009595; -.
DR CTD; 9153; -.
DR eggNOG; KOG3747; Eukaryota.
DR InParanoid; Q9MZT2; -.
DR OrthoDB; 471043at2759; -.
DR Proteomes; UP000001811; 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:SF11; PTHR10590:SF11; 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..658
FT /note="Sodium/nucleoside cotransporter 1"
FT /id="PRO_0000070448"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..658
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 658 AA; 72313 MW; 48AE64DF6EEEBAF3 CRC64;
MEKASGRKSL ALSTAENGIE NAGLELTEEG INSEQTRRME VQGHSLSDDV RPATHQRSYL
QPLTKARTFC QRHASLFKKI LLGLLCLAYA AYFLAACILD FQRALALFVI TCLVILVLLL
HFLKKFLGKK LTRCLKPFKN SQLRLWIKRV FAGVSLVGLI LWLALDTAQR PEQLISFAGI
CMFVLILFAC SKHHSAVSWR TVFWGLGLQF VFGLLVIRTD PGFIAFQWLG DQVQIFLAYT
VAGSSFVLGD TLVNDVFAFQ SLPIIIFFGC VMSILYYLGL VQWVVQKIAW FLQVTMRTTA
TETLAVAGNI FVGMTEAPLL IRPYLADLTL SEIHAVMTSG FATISGTVLG AFISFGIDAS
SLISASVMGA PCALALSKLV YPEEEESKFK SKEGVKLPRG KESNVLEAAS NGATDAIALV
ANVAANLVAF LAVLAFINAA LSWLGELVDI QGLTFQVICS YILRPMVYMM GVEWTDCPMV
AEMVGIKFFT NEFVAYQQLS QYKKKRLSGM EEWIDGQKQW ISVRAEVITT FSLCGFANLS
SIGITLGGLT SMVPHRKSDL SKVVIRALFT GSCVSFISAC VAGILYVPRG AETDCVSFLS
TSFTNRSYET YVCCRELFQN TYLNGTNPPS FSGAWEDKAF SAMALANCCG FYNNTVCA