S29A1_MOUSE
ID S29A1_MOUSE Reviewed; 460 AA.
AC Q9JIM1; Q99K84; Q9DBT8; Q9JHF0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Equilibrative nucleoside transporter 1;
DE AltName: Full=Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter;
DE Short=Equilibrative NBMPR-sensitive nucleoside transporter;
DE AltName: Full=Nucleoside transporter, es-type;
DE AltName: Full=Solute carrier family 29 member 1;
GN Name=Slc29a1; Synonyms=Ent1;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=11027664; DOI=10.1006/bbrc.2000.3665;
RA Choi D.-S., Handa M., Young H., Gordon A.S., Diamond I., Messing R.O.;
RT "Genomic organization and expression of the mouse equilibrative,
RT nitrobenzylthioinosine-sensitive nucleoside transporter 1 (ENT1) gene.";
RL Biochem. Biophys. Res. Commun. 277:200-208(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, and Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary tumor;
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).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
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: Mediates both influx and efflux of nucleosides across the
CC membrane (equilibrative transporter). It is sensitive (ES) to low
CC concentrations of the inhibitor nitrobenzylmercaptopurine riboside
CC (NBMPR) and is sodium-independent. It has a higher affinity for
CC adenosine. Resistant to dipyridamole and dilazep inhibition (anticancer
CC chemotherapeutics drugs).
CC -!- SUBUNIT: Identified in a complex with STOM. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Apical cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Predominantly localized in the basolateral membrane in polarized
CC MDCK cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ent1b;
CC IsoId=Q9JIM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIM1-2; Sequence=VSP_010471;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, spleen, lung, liver and
CC testis. Lower level of expression in brain and kidney.
CC {ECO:0000269|PubMed:11027664}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; AF218255; AAF64035.2; -; Genomic_DNA.
DR EMBL; AF218255; AAF64036.2; -; Genomic_DNA.
DR EMBL; AF305501; AAG22828.1; -; mRNA.
DR EMBL; AF131212; AAF78452.1; -; mRNA.
DR EMBL; AK004756; BAB23537.1; -; mRNA.
DR EMBL; AK050089; BAC34063.1; -; mRNA.
DR EMBL; BC004828; AAH04828.1; -; mRNA.
DR EMBL; BC006812; AAH06812.1; -; mRNA.
DR CCDS; CCDS28813.1; -. [Q9JIM1-2]
DR CCDS; CCDS57096.1; -. [Q9JIM1-1]
DR RefSeq; NP_001186042.1; NM_001199113.1. [Q9JIM1-1]
DR RefSeq; NP_001186043.1; NM_001199114.1. [Q9JIM1-1]
DR RefSeq; NP_001186044.1; NM_001199115.1. [Q9JIM1-2]
DR RefSeq; NP_001186045.1; NM_001199116.1. [Q9JIM1-2]
DR RefSeq; NP_075018.1; NM_022880.3. [Q9JIM1-2]
DR RefSeq; XP_006524831.1; XM_006524768.1.
DR RefSeq; XP_006524832.1; XM_006524769.2.
DR RefSeq; XP_006524833.1; XM_006524770.3.
DR RefSeq; XP_006524834.1; XM_006524771.1.
DR AlphaFoldDB; Q9JIM1; -.
DR SMR; Q9JIM1; -.
DR BioGRID; 211010; 8.
DR STRING; 10090.ENSMUSP00000131976; -.
DR BindingDB; Q9JIM1; -.
DR ChEMBL; CHEMBL1287611; -.
DR GlyGen; Q9JIM1; 1 site.
DR iPTMnet; Q9JIM1; -.
DR PhosphoSitePlus; Q9JIM1; -.
DR SwissPalm; Q9JIM1; -.
DR EPD; Q9JIM1; -.
DR jPOST; Q9JIM1; -.
DR MaxQB; Q9JIM1; -.
DR PaxDb; Q9JIM1; -.
DR PRIDE; Q9JIM1; -.
DR ProteomicsDB; 256876; -. [Q9JIM1-1]
DR ProteomicsDB; 256877; -. [Q9JIM1-2]
DR Antibodypedia; 2790; 568 antibodies from 40 providers.
DR DNASU; 63959; -.
DR Ensembl; ENSMUST00000051574; ENSMUSP00000063096; ENSMUSG00000023942. [Q9JIM1-1]
DR Ensembl; ENSMUST00000064889; ENSMUSP00000063757; ENSMUSG00000023942. [Q9JIM1-2]
DR Ensembl; ENSMUST00000097317; ENSMUSP00000094923; ENSMUSG00000023942. [Q9JIM1-1]
DR Ensembl; ENSMUST00000163492; ENSMUSP00000129242; ENSMUSG00000023942. [Q9JIM1-2]
DR Ensembl; ENSMUST00000166119; ENSMUSP00000128763; ENSMUSG00000023942. [Q9JIM1-1]
DR Ensembl; ENSMUST00000167692; ENSMUSP00000131976; ENSMUSG00000023942. [Q9JIM1-1]
DR Ensembl; ENSMUST00000171847; ENSMUSP00000126703; ENSMUSG00000023942. [Q9JIM1-2]
DR GeneID; 63959; -.
DR KEGG; mmu:63959; -.
DR UCSC; uc008crb.2; mouse. [Q9JIM1-1]
DR CTD; 2030; -.
DR MGI; MGI:1927073; Slc29a1.
DR VEuPathDB; HostDB:ENSMUSG00000023942; -.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_6_0_1; -.
DR InParanoid; Q9JIM1; -.
DR OMA; KIMFINS; -.
DR PhylomeDB; Q9JIM1; -.
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; 63959; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc29a1; mouse.
DR PRO; PR:Q9JIM1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JIM1; protein.
DR Bgee; ENSMUSG00000023942; Expressed in gastrula and 210 other tissues.
DR ExpressionAtlas; Q9JIM1; baseline and differential.
DR Genevisible; Q9JIM1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IMP:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0032238; P:adenosine transport; IMP:ARUK-UCL.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0098810; P:neurotransmitter reuptake; ISO:MGI.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:MGI.
DR GO; GO:0001504; P:neurotransmitter uptake; IMP:ARUK-UCL.
DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:MGI.
DR GO; GO:0015858; P:nucleoside transport; IDA:MGI.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:MGI.
DR GO; GO:0030431; P:sleep; ISO:MGI.
DR GO; GO:0015862; P:uridine transport; ISO:MGI.
DR InterPro; IPR030195; ENT1.
DR InterPro; IPR034764; ENT1/ENT2.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR PANTHER; PTHR10332:SF9; PTHR10332:SF9; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00939; 2a57; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..460
FT /note="Equilibrative nucleoside transporter 1"
FT /id="PRO_0000209338"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 255..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99808"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99808"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 254..256
FT /note="SKG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11085929,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_010471"
FT CONFLICT 54
FT /note="D -> G (in Ref. 3; BAB23537)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="I -> T (in Ref. 4; AAH04828)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="I -> V (in Ref. 4; AAH04828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50192 MW; FE37EEA155F9AB2F CRC64;
MTTSHQPQDR YKAVWLIFFV LGLGTLLPWN FFMTATKYFT NRLDVSQNVS SDTDQSCEST
KALADPTVAL PARSSLSAIF NNVMTLCAML PLLVFTCLNS FLHQRISQSV RILGSLLAIL
LVFLVTAALV KVEMDALIFF VITMIKIVLI NSFGAILQAS LFGLAGVLPA NYTAPIMSGQ
GLAGFFTSVA MICAIASGSE LSESAFGYFI TACAVVILAI LCYLALPRTE FYRHYLQLNL
AGPAEQETKL DLISKGEEPK GRREESGVPG PNSPPTNRNQ SIKAILKSIC VPALSVCFIF
TVTIGLFPAV TAEVESSIAG TSPWKSYFIP VACFLNFNVF DWLGRSLTAV CMWPGQDSRW
LPVLVASRIV FIPLLMLCNV KARHCGAQRH HFVFKHDAWF IAFMAAFAFS NGYLASLCMC
FGPKKVKPAE AETAGNIMSF FLCLGLALGA VLSFLLRALV
