ID   S29A2_MOUSE             Reviewed;         456 AA.
AC   Q61672; Q9JIT8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Equilibrative nucleoside transporter 2 {ECO:0000303|PubMed:11085929};
DE            Short=mENT2 {ECO:0000303|PubMed:11085929};
DE   AltName: Full=36 kDa hydrophobic nucleolar protein;
DE   AltName: Full=36 kDa nucleolar protein HNP36 {ECO:0000303|PubMed:7639753};
DE   AltName: Full=Delayed-early response protein 12 {ECO:0000303|PubMed:7639753};
DE   AltName: Full=Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter {ECO:0000303|PubMed:11085929};
DE            Short=Equilibrative NBMPR-insensitive nucleoside transporter {ECO:0000303|PubMed:11085929};
DE   AltName: Full=Nucleoside transporter, ei-type {ECO:0000250|UniProtKB:Q14542};
DE   AltName: Full=Solute carrier family 29 member 2;
GN   Name=Slc29a2 {ECO:0000312|MGI:MGI:1345278};
GN   Synonyms=Der12, Ent2, Hnp36;
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] OF 64-456, AND INDUCTION BY PDGF AND FGF.
RC   STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX   PubMed=7639753; DOI=10.1006/bbrc.1995.2133;
RA   Williams J.B., Lanahan A.A.;
RT   "A mammalian delayed-early response gene encodes HNP36, a novel, conserved
RT   nucleolar protein.";
RL   Biochem. Biophys. Res. Commun. 213:325-333(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND
RP   MISCELLANEOUS.
RC   STRAIN=CD-1; TISSUE=Brain;
RX   PubMed=11085929; DOI=10.1042/bj3520363;
RA   Kiss A., Farah K., Kim J., Garriock R.J., Drysdale T.A., Hammond J.R.;
RT   "Molecular cloning and functional characterization of inhibitor-sensitive
RT   (mENT1) and inhibitor-resistant (mENT2) equilibrative nucleoside
RT   transporters from mouse brain.";
RL   Biochem. J. 352:363-372(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Bidirectional uniporter involved in the facilitative
CC       transport of nucleosides and nucleobases, and contributes to
CC       maintaining their cellular homeostasis (PubMed:11085929). Functions as
CC       a Na(+)-independent, passive transporter (By similarity). Involved in
CC       the transport of nucleosides such as inosine, adenosine, uridine,
CC       thymidine, cytidine and guanosine (PubMed:11085929). Also able to
CC       transport purine nucleobases (hypoxanthine, adenine, guanine) and
CC       pyrimidine nucleobases (thymine, uracil) (By similarity). Involved in
CC       nucleoside transport at basolateral membrane of kidney cells, allowing
CC       liver absorption of nucleoside metabolites (By similarity). Mediates
CC       apical nucleoside uptake into Sertoli cells, thereby regulating the
CC       transport of nucleosides in testis across the blood-testis-barrier (By
CC       similarity). Mediates both the influx and efflux of hypoxanthine in
CC       skeletal muscle microvascular endothelial cells to control the amount
CC       of intracellular hypoxanthine available for xanthine oxidase-mediated
CC       ROS production (By similarity). {ECO:0000250|UniProtKB:O54699,
CC       ECO:0000250|UniProtKB:Q14542, ECO:0000269|PubMed:11085929}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=inosine(in) = inosine(out); Xref=Rhea:RHEA:75375,
CC         ChEBI:CHEBI:17596; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75376;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75377;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343,
CC         ChEBI:CHEBI:16335; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75344;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75345;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(out) = uridine(in); Xref=Rhea:RHEA:71519,
CC         ChEBI:CHEBI:16704; Evidence={ECO:0000269|PubMed:11085929};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71520;
CC         Evidence={ECO:0000305|PubMed:11085929};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71521;
CC         Evidence={ECO:0000305|PubMed:11085929};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thymidine(in) = thymidine(out); Xref=Rhea:RHEA:75363,
CC         ChEBI:CHEBI:17748; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75364;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75365;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hypoxanthine(out) = hypoxanthine(in); Xref=Rhea:RHEA:71515,
CC         ChEBI:CHEBI:17368; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71516;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71517;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenine(out) = adenine(in); Xref=Rhea:RHEA:71523,
CC         ChEBI:CHEBI:16708; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71524;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71525;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(in) = cytidine(out); Xref=Rhea:RHEA:75367,
CC         ChEBI:CHEBI:17562; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75368;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75369;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thymine(out) = thymine(in); Xref=Rhea:RHEA:71527,
CC         ChEBI:CHEBI:17821; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71528;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71529;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uracil(in) = uracil(out); Xref=Rhea:RHEA:69404,
CC         ChEBI:CHEBI:17568; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69405;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69406;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531,
CC         ChEBI:CHEBI:16235; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71532;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71533;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371,
CC         ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75372;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:75373;
CC         Evidence={ECO:0000250|UniProtKB:Q14542};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q14542}; Multi-pass membrane protein
CC       {ECO:0000305}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q14542}; Multi-pass membrane protein
CC       {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q14542}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By platelet derived growth factor (PDGF) and fibroblast
CC       growth factor (FGF). {ECO:0000269|PubMed:7639753}.
CC   -!- MISCELLANEOUS: Transport activity is insensitive to nanomolar
CC       concentrations of the inhibitor nitrobenzylmercaptopurine riboside
CC       (NBMPR). {ECO:0000269|PubMed:11085929}.
CC   -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF183397; AAF78477.1; -; mRNA.
DR   EMBL; CH466612; EDL33088.1; -; Genomic_DNA.
DR   EMBL; BC048958; AAH48958.1; -; mRNA.
DR   EMBL; X86682; CAA60381.1; ALT_INIT; mRNA.
DR   CCDS; CCDS50354.1; -.
DR   PIR; JC4195; JC4195.
DR   RefSeq; NP_031880.2; NM_007854.3.
DR   AlphaFoldDB; Q61672; -.
DR   SMR; Q61672; -.
DR   BioGRID; 199208; 1.
DR   STRING; 10090.ENSMUSP00000157780; -.
DR   ChEMBL; CHEMBL1287612; -.
DR   TCDB; 2.A.57.1.2; the equilibrative nucleoside transporter (ent) family.
DR   GlyCosmos; Q61672; 1 site, No reported glycans.
DR   GlyGen; Q61672; 1 site.
DR   iPTMnet; Q61672; -.
DR   PhosphoSitePlus; Q61672; -.
DR   SwissPalm; Q61672; -.
DR   EPD; Q61672; -.
DR   MaxQB; Q61672; -.
DR   PaxDb; 10090-ENSMUSP00000025826; -.
DR   PeptideAtlas; Q61672; -.
DR   ProteomicsDB; 253379; -.
DR   Antibodypedia; 16257; 175 antibodies from 23 providers.
DR   DNASU; 13340; -.
DR   Ensembl; ENSMUST00000236152.2; ENSMUSP00000157780.2; ENSMUSG00000024891.7.
DR   GeneID; 13340; -.
DR   KEGG; mmu:13340; -.
DR   UCSC; uc008gbv.2; mouse.
DR   AGR; MGI:1345278; -.
DR   CTD; 3177; -.
DR   MGI; MGI:1345278; Slc29a2.
DR   VEuPathDB; HostDB:ENSMUSG00000024891; -.
DR   eggNOG; KOG1479; Eukaryota.
DR   GeneTree; ENSGT00950000182898; -.
DR   HOGENOM; CLU_021611_6_0_1; -.
DR   InParanoid; Q61672; -.
DR   OMA; FNIMDWV; -.
DR   OrthoDB; 517168at2759; -.
DR   PhylomeDB; Q61672; -.
DR   TreeFam; TF313950; -.
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; 13340; 1 hit in 81 CRISPR screens.
DR   PRO; PR:Q61672; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q61672; Protein.
DR   Bgee; ENSMUSG00000024891; Expressed in ectoplacental cone and 94 other cell types or tissues.
DR   ExpressionAtlas; Q61672; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IGI:MGI.
DR   GO; GO:0015207; F:adenine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015212; F:cytidine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015208; F:guanine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IGI:ARUK-UCL.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IGI:ARUK-UCL.
DR   GO; GO:0015210; F:uracil transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015853; P:adenine transport; ISS:UniProtKB.
DR   GO; GO:0032238; P:adenosine transport; IGI:ARUK-UCL.
DR   GO; GO:0015861; P:cytidine transport; ISS:UniProtKB.
DR   GO; GO:1903716; P:guanine transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015854; P:guanine transport; ISO:MGI.
DR   GO; GO:0035344; P:hypoxanthine transport; ISS:UniProtKB.
DR   GO; GO:0035340; P:inosine transport; ISS:UniProtKB.
DR   GO; GO:0006836; P:neurotransmitter transport; ISO:MGI.
DR   GO; GO:0001504; P:neurotransmitter uptake; IGI:ARUK-UCL.
DR   GO; GO:0015851; P:nucleobase transport; ISS:UniProtKB.
DR   GO; GO:1901642; P:nucleoside transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0015858; P:nucleoside transport; IDA:MGI.
DR   GO; GO:1904823; P:purine nucleobase transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015860; P:purine nucleoside transmembrane transport; IGI:ARUK-UCL.
DR   GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:MGI.
DR   GO; GO:0035364; P:thymine transport; ISS:UniProtKB.
DR   GO; GO:1903791; P:uracil transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015862; P:uridine transport; IDA:UniProtKB.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR034764; ENT1/ENT2.
DR   InterPro; IPR002259; Eqnu_transpt.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   NCBIfam; TIGR00939; 2a57; 1.
DR   PANTHER; PTHR10332; EQUILIBRATIVE NUCLEOSIDE TRANSPORTER; 1.
DR   PANTHER; PTHR10332:SF8; EQUILIBRATIVE NUCLEOSIDE TRANSPORTER 2; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   PIRSF; PIRSF016379; ENT; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   Genevisible; Q61672; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..456
FT                   /note="Equilibrative nucleoside transporter 2"
FT                   /id="PRO_0000209341"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          248..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14542"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   456 AA;  50255 MW;  A9FE7CA037A4468F CRC64;
     MARGNAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ GRLAGTNSSA ETMGTNHTSP
     TDTFNFNNWV TLLSQLPLLL FTLLNSFLYQ CIPESVRILG SLLAILLLFA LTAALVKVDL
     SPGLFFSVTM ASVWFINSFC AVLQGSLFGQ LGTMPSTYST LFLSGQGLAG IFAALAMLMS
     LASGVDAQTS ALGYFITPCV GILLSIVCYL SLPHLKFARY YLTEKLSQAP TQELETKAEL
     LQADEKNGVP ISPQQASPTL DLDPEKEPEP EEPQKPGKPS VFVVFRKIWL TALCLVLVFT
     VTLSVFPAIT AMVTTSSNSP GKWGLFFNPI CCFLLFNVMD WLGRSLTSYF LWPDEDSQQL
     LPLLVCLRFL FVPLFMLCHV PQHARLPIIF RQDAYFITFM LLFAVSNGYL VSLTMCLAPR
     QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL
//