S28A2_RAT
ID S28A2_RAT Reviewed; 659 AA.
AC Q62773; Q9QWI3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sodium/nucleoside cotransporter 2;
DE AltName: Full=Concentrative nucleoside transporter 2 {ECO:0000303|PubMed:8967974};
DE Short=CNT 2 {ECO:0000303|PubMed:8967974};
DE Short=rCNT2 {ECO:0000303|PubMed:8967974};
DE AltName: Full=Na(+)/nucleoside cotransporter 2;
DE AltName: Full=Sodium-coupled nucleoside transporter 2;
DE AltName: Full=Sodium/purine nucleoside cotransporter {ECO:0000303|PubMed:7775409};
DE Short=SPNT {ECO:0000303|PubMed:7775409};
DE AltName: Full=Solute carrier family 28 member 2;
GN Name=Slc28a2; Synonyms=Cnt2, Spnt {ECO:0000303|PubMed:7775409};
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], FUNCTION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7775409; DOI=10.1074/jbc.270.23.13596;
RA Che M., Ortiz D.F., Arias I.M.;
RT "Primary structure and functional expression of a cDNA encoding the bile
RT canalicular, purine-specific Na(+)-nucleoside cotransporter.";
RL J. Biol. Chem. 270:13596-13599(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RX PubMed=8967974;
RA Yao S.Y., Ng A.M., Ritzel M.W., Gati W.P., Cass C.E., Young J.D.;
RT "Transport of adenosine by recombinant purine- and pyrimidine-selective
RT sodium/nucleoside cotransporters from rat jejunum expressed in Xenopus
RT laevis oocytes.";
RL Mol. Pharmacol. 50:1529-1535(1996).
RN [3]
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=1315767; DOI=10.1016/s0021-9258(19)50144-2;
RA Che M., Nishida T., Gatmaitan Z., Arias I.M.;
RT "A nucleoside transporter is functionally linked to ectonucleotidases in
RT rat liver canalicular membrane.";
RL J. Biol. Chem. 267:9684-9688(1992).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sodium-dependent and purine-selective (PubMed:7775409,
CC PubMed:8967974, PubMed:1315767). Exhibits the transport characteristics
CC of the nucleoside transport system cif or N1 subtype (N1/cif)
CC (selective for purine nucleosides and uridine) (PubMed:7775409,
CC PubMed:8967974, PubMed:1315767). Accepts purine, analogs of purine
CC nucleosides and uridine, and exhibits high affinity for adenosine
CC (PubMed:7775409). {ECO:0000269|PubMed:1315767,
CC ECO:0000269|PubMed:7775409, ECO:0000269|PubMed:8967974}.
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:0000269|PubMed:7775409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine(out) + Na(+)(out) = inosine(in) + Na(+)(in);
CC Xref=Rhea:RHEA:69931, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:7775409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(out) + Na(+)(out) = guanosine(in) + Na(+)(in);
CC Xref=Rhea:RHEA:69935, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:7775409};
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:0000269|PubMed:7775409};
CC -!- ACTIVITY REGULATION: Inhibited by formycin B, partially inhibited by
CC purine analog ara-A. {ECO:0000269|PubMed:7775409}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43868}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (in bile canalicular membrane
CC vesicles (CMV) but not in sinusoidal vesicles), jejunum, spleen and
CC heart (PubMed:7775409). Also expressed in brain and skeletal muscle
CC (PubMed:7775409). Not expressed in kidney, muscle and lung
CC (PubMed:7775409). {ECO:0000269|PubMed:7775409}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; U25055; AAA80640.1; -; mRNA.
DR EMBL; U66723; AAD00159.1; -; mRNA.
DR PIR; A57532; A57532.
DR RefSeq; NP_113852.1; NM_031664.1.
DR AlphaFoldDB; Q62773; -.
DR SMR; Q62773; -.
DR STRING; 10116.ENSRNOP00000034564; -.
DR BindingDB; Q62773; -.
DR ChEMBL; CHEMBL1287616; -.
DR TCDB; 2.A.41.2.1; the concentrative nucleoside transporter (cnt) family.
DR iPTMnet; Q62773; -.
DR PhosphoSitePlus; Q62773; -.
DR PaxDb; Q62773; -.
DR PeptideAtlas; Q62773; -.
DR PRIDE; Q62773; -.
DR GeneID; 60423; -.
DR KEGG; rno:60423; -.
DR UCSC; RGD:61840; rat.
DR CTD; 9153; -.
DR RGD; 61840; Slc28a2.
DR eggNOG; KOG3747; Eukaryota.
DR InParanoid; Q62773; -.
DR OrthoDB; 471043at2759; -.
DR PhylomeDB; Q62773; -.
DR Reactome; R-RNO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR PRO; PR:Q62773; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0030135; C:coated vesicle; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0012506; C:vesicle membrane; IDA:ARUK-UCL.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005415; F:nucleoside:sodium symporter activity; IDA:RGD.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015389; F:pyrimidine- and adenine-specific:sodium symporter activity; ISO:RGD.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0032238; P:adenosine transport; ISO:RGD.
DR GO; GO:0035340; P:inosine transport; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:RGD.
DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:RGD.
DR GO; GO:1904823; P:purine nucleobase transmembrane transport; ISO:RGD.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; ISO:RGD.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:RGD.
DR GO; GO:0001895; P:retina homeostasis; IDA:RGD.
DR GO; GO:0015862; P:uridine transport; ISO:RGD.
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 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..659
FT /note="Sodium/nucleoside cotransporter 2"
FT /id="PRO_0000070452"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 419
FT /note="A -> G (in Ref. 2; AAD00159)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="I -> V (in Ref. 2; AAD00159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 72615 MW; 0CE9B49E5D1FE453 CRC64;
MAKSEGRKSA SQDTSENGME NPGLELMEVG NLEQGKTLEE VTQGHSLKDG LGHSSLWRRI
LQPFTKARSF YQRHAGLFKK ILLGLLCLAY AAYLLAACIL NFRRALALFV ITCLVIFILA
CHFLKKFFAK KSIRCLKPLK NTRLRLWLKR VFMGAAVVGL ILWLALDTAQ RPEQLISFAG
ICMFILILFA CSKHHSAVSW RTVFWGLGLQ FVFGILVIRT EPGFNAFQWL GDQIQIFLAY
TVEGSSFVFG DTLVQSVFAF QSLPIIIFFG CVMSILYYLG LVQWVIQKIA WFLQITMGTT
AAETLAVAGN IFVGMTEAPL LIRPYLADMT LSEIHAVMTG GFATIAGTVL GAFISFGIDA
SSLISASVMA APCALALSKL VYPEVEESKF KSKEGVKLPR GEERNILEAA SNGATDAIAL
VANVAANLIA FLAVLAFINS TLSWLGEMVD IHGLTFQVIC SYVLRPMVFM MGVQWADCPL
VAEIVGVKFF INEFVAYQQL SQYKNKRLSG VEEWINGEKQ WISVKAEIIA TFSLCGFANL
TSIGITLGGL TSMVPQRKSD LCKLVVRALF TGACVSFISA CMAGILYVPR GAETDCVSFL
NTNFTNRTYE TYVCCRELFQ STLLNGTNMP SFSGPWQDKE SSLRNLAKCC DLYTSTVCA
