ID   S28A2_MOUSE             Reviewed;         660 AA.
AC   O88627; Q8BJP1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Sodium/nucleoside cotransporter 2;
DE   AltName: Full=Concentrative nucleoside transporter 2 {ECO:0000303|PubMed:10721696};
DE            Short=CNT 2 {ECO:0000303|PubMed:10721696};
DE   AltName: Full=Na(+)/nucleoside cotransporter 2;
DE   AltName: Full=Sodium-coupled nucleoside transporter 2;
DE   AltName: Full=Sodium/purine nucleoside cotransporter;
DE            Short=SPNT;
DE   AltName: Full=Solute carrier family 28 member 2;
GN   Name=Slc28a2; Synonyms=Cnt2 {ECO:0000303|PubMed:10721696};
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 [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=10721696; DOI=10.1016/s0378-1119(99)00521-1;
RA   Patel D.H., Crawford C.R., Naeve C.W., Belt J.A.;
RT   "Cloning, genomic organization and chromosomal localization of the gene
RT   encoding the murine sodium-dependent, purine-selective, concentrative
RT   nucleoside transporter (CNT2).";
RL   Gene 242:51-58(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Sodium-dependent and purine-selective transporter. Exhibits
CC       the transport characteristics of the nucleoside transport system cif or
CC       N1 subtype (N1/cif) (selective for purine nucleosides and uridine).
CC       Plays a critical role in specific uptake and salvage of purine
CC       nucleosides in kidney and other tissues. May contribute to regulate the
CC       transport of organic compounds in testes across the blood-testis-
CC       barrier (By similarity). {ECO:0000250|UniProtKB:O43868}.
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:O43868};
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:0000250|UniProtKB:O43868};
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:0000250|UniProtKB:O43868};
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:O43868};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43868}; Multi-
CC       pass membrane protein {ECO:0000255}. Apicolateral cell membrane
CC       {ECO:0000250|UniProtKB:O43868}; Multi-pass membrane protein
CC       {ECO:0000255}.
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; AF079853; AAC28858.1; -; mRNA.
DR   EMBL; AK080957; BAC38094.1; -; mRNA.
DR   EMBL; AK152776; BAE31488.1; -; mRNA.
DR   EMBL; AL844566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16663.1; -.
DR   RefSeq; NP_766568.1; NM_172980.2.
DR   RefSeq; XP_006499664.1; XM_006499601.3.
DR   RefSeq; XP_011237878.1; XM_011239576.2.
DR   AlphaFoldDB; O88627; -.
DR   SMR; O88627; -.
DR   STRING; 10090.ENSMUSP00000106154; -.
DR   ChEMBL; CHEMBL1287613; -.
DR   GlyGen; O88627; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O88627; -.
DR   PhosphoSitePlus; O88627; -.
DR   EPD; O88627; -.
DR   MaxQB; O88627; -.
DR   PaxDb; 10090-ENSMUSP00000106154; -.
DR   ProteomicsDB; 260901; -.
DR   DNASU; 269346; -.
DR   Ensembl; ENSMUST00000028652.12; ENSMUSP00000028652.6; ENSMUSG00000027219.14.
DR   Ensembl; ENSMUST00000110524.2; ENSMUSP00000106153.2; ENSMUSG00000027219.14.
DR   Ensembl; ENSMUST00000110525.8; ENSMUSP00000106154.2; ENSMUSG00000027219.14.
DR   GeneID; 269346; -.
DR   KEGG; mmu:269346; -.
DR   UCSC; uc008mas.1; mouse.
DR   AGR; MGI:1913105; -.
DR   CTD; 9153; -.
DR   MGI; MGI:1913105; Slc28a2.
DR   VEuPathDB; HostDB:ENSMUSG00000027219; -.
DR   eggNOG; KOG3747; Eukaryota.
DR   GeneTree; ENSGT00390000016025; -.
DR   HOGENOM; CLU_016813_3_2_1; -.
DR   InParanoid; O88627; -.
DR   OMA; RAVFLWF; -.
DR   OrthoDB; 1333063at2759; -.
DR   PhylomeDB; O88627; -.
DR   TreeFam; TF314131; -.
DR   Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR   Reactome; R-MMU-9748787; Azathioprine ADME.
DR   Reactome; R-MMU-9755088; Ribavirin ADME.
DR   BioGRID-ORCS; 269346; 0 hits in 76 CRISPR screens.
DR   PRO; PR:O88627; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O88627; Protein.
DR   Bgee; ENSMUSG00000027219; Expressed in jejunum and 40 other cell types or tissues.
DR   GO; GO:0016327; C:apicolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; IDA:ARUK-UCL.
DR   GO; GO:0030135; C:coated vesicle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR   GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005415; F:nucleoside:sodium symporter activity; ISO:MGI.
DR   GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015389; F:pyrimidine- and adenosine-specific:sodium symporter activity; ISO:MGI.
DR   GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0032238; P:adenosine transport; ISO:MGI.
DR   GO; GO:0035340; P:inosine transport; ISO:MGI.
DR   GO; GO:0006836; P:neurotransmitter transport; ISO:MGI.
DR   GO; GO:1901642; P:nucleoside transmembrane transport; ISO:MGI.
DR   GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR   GO; GO:1904823; P:purine nucleobase transmembrane transport; ISO:MGI.
DR   GO; GO:0015860; P:purine nucleoside transmembrane transport; ISO:MGI.
DR   GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:MGI.
DR   GO; GO:0001895; P:retina homeostasis; 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:SF11; SODIUM_NUCLEOSIDE COTRANSPORTER 2; 1.
DR   Pfam; PF07670; Gate; 1.
DR   Pfam; PF07662; Nucleos_tra2_C; 1.
DR   Pfam; PF01773; Nucleos_tra2_N; 1.
DR   Genevisible; O88627; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..660
FT                   /note="Sodium/nucleoside cotransporter 2"
FT                   /id="PRO_0000070451"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62773"
FT   CONFLICT        2
FT                   /note="E -> K (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="T -> R (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="C -> G (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="R -> K (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="A -> T (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="V -> I (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="A -> T (in Ref. 1; AAC28858)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   660 AA;  72916 MW;  64522D068A2138EC CRC64;
     MEKSKGRKSV SQATVENCME NPGLELMEGG NLEQRYTQEE VTQGHSLEDG LGHSSLWSRR
     IFQPFTKARS FFERHAGLFR KILLGLLCLA YAAYFLAACI LNFQRALALF VITCLVIFIL
     ACHFLKKFFP KEQLRCLKPL ENTHLNLWAK RVFVGLSVVG LILWLALDTA QRPEQLISFA
     GICMFILILF ACSKHHSAVC WRTVFWGLGL QFIFGILVIR TEPGFNAFQW LGDQIQIFLA
     YTVEGSSFVF GDTLVQNVFA FQSLPIIIFF GCVMSILYYL GLVQWVIQKV AWFLQITMGT
     TAAETLAVAG NIFVGMTEAP LLIRPYLADM TISEIHAVMT GGFATIAGTV LGAFISFGID
     ASSLISASVM AAPCALALSK LVYPEVEESK FKSKEGLKLP RGEERNILEA ASNGATDAIS
     LVANVAANLI AFLAVLAFIN ATLSWLGEMV DIHGLSFQVI CSYVLRPMVF MMGVQWADCP
     LVAEIVGVKF FINEFVAYQQ LSQYKNKRLS GVEEWINGEK QWISVKAEII TTFSLCGFAN
     LSSIGITLGG LTSMIPQRKS DLCKIVVRAL FTGACVSFIS ACMAGILYVP RGAETDCVSF
     LNTNFTNRTY ETYVCCRELF QSTSLNGTNM PSFSGPWQDN VSSLRNLASC CDLYTSTVCA
//