S28A2_MOUSE
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 03-AUG-2022, entry version 157.
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.
CC {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}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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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 iPTMnet; O88627; -.
DR PhosphoSitePlus; O88627; -.
DR EPD; O88627; -.
DR MaxQB; O88627; -.
DR PaxDb; O88627; -.
DR PRIDE; O88627; -.
DR ProteomicsDB; 260901; -.
DR DNASU; 269346; -.
DR Ensembl; ENSMUST00000028652; ENSMUSP00000028652; ENSMUSG00000027219.
DR Ensembl; ENSMUST00000110524; ENSMUSP00000106153; ENSMUSG00000027219.
DR Ensembl; ENSMUST00000110525; ENSMUSP00000106154; ENSMUSG00000027219.
DR GeneID; 269346; -.
DR KEGG; mmu:269346; -.
DR UCSC; uc008mas.1; mouse.
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; FITGQPK; -.
DR OrthoDB; 471043at2759; -.
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 BioGRID-ORCS; 269346; 0 hits in 71 CRISPR screens.
DR PRO; PR:O88627; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88627; protein.
DR Bgee; ENSMUSG00000027219; Expressed in jejunum and 37 other tissues.
DR Genevisible; O88627; MM.
DR GO; GO:0031526; C:brush border membrane; IDA:ARUK-UCL.
DR GO; GO:0030135; C:coated vesicle; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO: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 adenine-specific:sodium symporter activity; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
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; 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..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
