S29A1_HUMAN
ID S29A1_HUMAN Reviewed; 456 AA.
AC Q99808; B3KQV7; B3KQY5; Q5T9W9; Q9UJY2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 2-22.
RC TISSUE=Placenta;
RX PubMed=8986748; DOI=10.1038/nm0197-89;
RA Griffiths M., Beaumont N., Yao S.Y.M., Sundaram M., Boumah C.E., Davies A.,
RA Kwong F.Y.P., Coe I., Cass C.E., Young J.D., Baldwin S.A.;
RT "Cloning of a human nucleoside transporter implicated in the cellular
RT uptake of adenosine and chemotherapeutic drugs.";
RL Nat. Med. 3:89-93(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Graham K.A., Coe I.R., Carpenter P., Baldwin S.A., Young J.D., Cass C.E.;
RT "Genomic sequence of the human equilibrative nucleoside transporter 1
RT (hENT1).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Jejunum, and Small intestine;
RX PubMed=10755314; DOI=10.1007/s002800050040;
RA Lum P.Y., Ngo L.Y., Bakken A.H., Unadkat J.D.;
RT "Human intestinal es nucleoside transporter: molecular characterization and
RT nucleoside inhibitory profiles.";
RL Cancer Chemother. Pharmacol. 45:273-278(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12384580; DOI=10.1093/nar/gkf564;
RA Sankar N., Machado J., Abdulla P., Hilliker A.J., Coe I.R.;
RT "Comparative genomic analysis of equilibrative nucleoside transporters
RT suggests conserved protein structure despite limited sequence identity.";
RL Nucleic Acids Res. 30:4339-4350(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-453 AND
RP 453-ARG--VAL-456.
RX PubMed=12527552; DOI=10.1152/ajprenal.00215.2002;
RA Mangravite L.M., Xiao G., Giacomini K.M.;
RT "Localization of human equilibrative nucleoside transporters, hENT1 and
RT hENT2, in renal epithelial cells.";
RL Am. J. Physiol. 284:F902-F910(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Muscle;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48.
RC TISSUE=Leukemic T-cell;
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 [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH
RP STOM, AND SUBUNIT.
RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in
RT human erythrocyte membrane domains.";
RL Biochim. Biophys. Acta 1828:956-966(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-269 AND SER-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-293 AND VAL-455.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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. Inhibited by dipyridamole and dilazep (anticancer
CC chemotherapeutics drugs).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.62 mM for adenosine {ECO:0000269|PubMed:12527552};
CC Note=Vmax for adenosine uptake is about the same for SLC29A1 and
CC SLC29A2.;
CC -!- SUBUNIT: Identified in a complex with STOM.
CC {ECO:0000269|PubMed:23219802}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Apical cell membrane; Multi-pass membrane protein. Cell
CC membrane; Multi-pass membrane protein. Note=Predominantly localized in
CC the basolateral membrane in polarized MDCK cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99808-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99808-2; Sequence=VSP_056579;
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC Expressed in heart, brain, mammary gland, erythrocytes and placenta,
CC and also in fetal liver and spleen. {ECO:0000269|PubMed:12527552,
CC ECO:0000269|PubMed:23219802}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19349973}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; U81375; AAC51103.1; -; mRNA.
DR EMBL; AF190884; AAF02777.1; -; Genomic_DNA.
DR EMBL; AF079117; AAC62495.1; -; mRNA.
DR EMBL; AF495730; AAM11785.1; -; Genomic_DNA.
DR EMBL; AK090491; BAG52169.1; -; mRNA.
DR EMBL; AK090615; BAG52197.1; -; mRNA.
DR EMBL; AL139392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04255.1; -; Genomic_DNA.
DR EMBL; BC001382; AAH01382.1; -; mRNA.
DR EMBL; BC008954; AAH08954.1; -; mRNA.
DR CCDS; CCDS4908.1; -. [Q99808-1]
DR RefSeq; NP_001071643.1; NM_001078175.2. [Q99808-1]
DR RefSeq; NP_001071645.1; NM_001078177.1. [Q99808-1]
DR RefSeq; NP_001291391.1; NM_001304462.1. [Q99808-2]
DR RefSeq; NP_001291392.1; NM_001304463.1.
DR RefSeq; NP_001291394.1; NM_001304465.1.
DR RefSeq; NP_001291395.1; NM_001304466.1.
DR RefSeq; XP_005248935.1; XM_005248878.3. [Q99808-1]
DR RefSeq; XP_005248936.1; XM_005248879.3. [Q99808-1]
DR RefSeq; XP_005248937.1; XM_005248880.3. [Q99808-1]
DR RefSeq; XP_005248938.1; XM_005248881.3. [Q99808-1]
DR RefSeq; XP_005248939.1; XM_005248882.3. [Q99808-1]
DR PDB; 6OB6; X-ray; 2.90 A; A/B=1-456.
DR PDB; 6OB7; X-ray; 2.30 A; A=1-456.
DR PDBsum; 6OB6; -.
DR PDBsum; 6OB7; -.
DR AlphaFoldDB; Q99808; -.
DR SMR; Q99808; -.
DR BioGRID; 108344; 114.
DR IntAct; Q99808; 35.
DR MINT; Q99808; -.
DR STRING; 9606.ENSP00000377424; -.
DR BindingDB; Q99808; -.
DR ChEMBL; CHEMBL1997; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00987; Cytarabine.
DR DrugBank; DB00900; Didanosine.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB01073; Fludarabine.
DR DrugBank; DB00544; Fluorouracil.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB01033; Mercaptopurine.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB00642; Pemetrexed.
DR DrugBank; DB00811; Ribavirin.
DR DrugBank; DB09327; Tegafur-uracil.
DR DrugBank; DB00432; Trifluridine.
DR DrugBank; DB00197; Troglitazone.
DR DrugBank; DB02745; Uridine.
DR DrugBank; DB00943; Zalcitabine.
DR DrugCentral; Q99808; -.
DR GuidetoPHARMACOLOGY; 1117; -.
DR TCDB; 2.A.57.1.1; the equilibrative nucleoside transporter (ent) family.
DR GlyConnect; 1219; 2 N-Linked glycans (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; Q99808; 2 sites, 2 N-linked glycans (1 site), 3 O-linked glycans (1 site).
DR iPTMnet; Q99808; -.
DR PhosphoSitePlus; Q99808; -.
DR SwissPalm; Q99808; -.
DR BioMuta; SLC29A1; -.
DR DMDM; 9296956; -.
DR EPD; Q99808; -.
DR jPOST; Q99808; -.
DR MassIVE; Q99808; -.
DR MaxQB; Q99808; -.
DR PaxDb; Q99808; -.
DR PeptideAtlas; Q99808; -.
DR PRIDE; Q99808; -.
DR ProteomicsDB; 78487; -. [Q99808-1]
DR Antibodypedia; 2790; 568 antibodies from 40 providers.
DR DNASU; 2030; -.
DR Ensembl; ENST00000371708.1; ENSP00000360773.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000371713.6; ENSP00000360778.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000371724.6; ENSP00000360789.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000371755.9; ENSP00000360820.3; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000393844.7; ENSP00000377427.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000651428.1; ENSP00000498610.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000652453.1; ENSP00000499107.1; ENSG00000112759.19. [Q99808-1]
DR Ensembl; ENST00000652680.1; ENSP00000498747.1; ENSG00000112759.19. [Q99808-1]
DR GeneID; 2030; -.
DR KEGG; hsa:2030; -.
DR MANE-Select; ENST00000371755.9; ENSP00000360820.3; NM_001372327.1; NP_001359256.1.
DR UCSC; uc003owu.2; human. [Q99808-1]
DR CTD; 2030; -.
DR DisGeNET; 2030; -.
DR GeneCards; SLC29A1; -.
DR HGNC; HGNC:11003; SLC29A1.
DR HPA; ENSG00000112759; Low tissue specificity.
DR MalaCards; SLC29A1; -.
DR MIM; 602193; gene.
DR neXtProt; NX_Q99808; -.
DR OpenTargets; ENSG00000112759; -.
DR PharmGKB; PA154; -.
DR VEuPathDB; HostDB:ENSG00000112759; -.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_6_0_1; -.
DR InParanoid; Q99808; -.
DR OMA; KIMFINS; -.
DR OrthoDB; 559763at2759; -.
DR PhylomeDB; Q99808; -.
DR TreeFam; TF313950; -.
DR PathwayCommons; Q99808; -.
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SignaLink; Q99808; -.
DR SIGNOR; Q99808; -.
DR BioGRID-ORCS; 2030; 18 hits in 1083 CRISPR screens.
DR ChiTaRS; SLC29A1; human.
DR GeneWiki; Equilibrative_nucleoside_transporter_1; -.
DR GenomeRNAi; 2030; -.
DR Pharos; Q99808; Tclin.
DR PRO; PR:Q99808; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99808; protein.
DR Bgee; ENSG00000112759; Expressed in mucosa of stomach and 163 other tissues.
DR ExpressionAtlas; Q99808; baseline and differential.
DR Genevisible; Q99808; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0032238; P:adenosine transport; IDA: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; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0098810; P:neurotransmitter reuptake; IMP:SynGO.
DR GO; GO:0006836; P:neurotransmitter transport; IDA:ARUK-UCL.
DR GO; GO:0001504; P:neurotransmitter uptake; ISS:ARUK-UCL.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:1901642; P:nucleoside transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0015858; P:nucleoside transport; IDA:UniProtKB.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0030431; P:sleep; IEA:Ensembl.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0015862; P:uridine transport; IMP:ARUK-UCL.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; TAS:Reactome.
DR Gene3D; 1.20.1250.20; -; 1.
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 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8986748"
FT CHAIN 2..456
FT /note="Equilibrative nucleoside transporter 1"
FT /id="PRO_0000209337"
FT TOPO_DOM 2..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..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 254..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 1
FT /note="M -> MRRERTRGPQAWEFPSPTKSGCSLQSLSRDLRELREGEKPEDQAETE
FT ESWQGLARKTPGKACAPEGGSCQPGKTENTITM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056579"
FT VARIANT 216
FT /note="I -> T (in dbSNP:rs45573936)"
FT /id="VAR_053668"
FT VARIANT 293
FT /note="A -> T (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036221"
FT VARIANT 391
FT /note="E -> K (in dbSNP:rs45458701)"
FT /id="VAR_053669"
FT VARIANT 455
FT /note="I -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs767108156)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036222"
FT MUTAGEN 453..456
FT /note="Missing: No effect on subcellular localization and
FT inosine transport."
FT /evidence="ECO:0000269|PubMed:12527552"
FT MUTAGEN 453
FT /note="R->A: No effect on subcellular localization and
FT inosine transport."
FT /evidence="ECO:0000269|PubMed:12527552"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 13..34
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 77..102
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 108..131
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 136..165
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 170..197
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 201..224
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 282..306
FT /evidence="ECO:0007829|PDB:6OB7"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:6OB7"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:6OB7"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6OB7"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6OB6"
FT HELIX 393..417
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:6OB7"
FT HELIX 424..449
FT /evidence="ECO:0007829|PDB:6OB7"
SQ SEQUENCE 456 AA; 50219 MW; F18535A95DEBC95D CRC64;
MTTSHQPQDR YKAVWLIFFM LGLGTLLPWN FFMTATQYFT NRLDMSQNVS LVTAELSKDA
QASAAPAAPL PERNSLSAIF NNVMTLCAML PLLLFTYLNS FLHQRIPQSV RILGSLVAIL
LVFLITAILV KVQLDALPFF VITMIKIVLI NSFGAILQGS LFGLAGLLPA SYTAPIMSGQ
GLAGFFASVA MICAIASGSE LSESAFGYFI TACAVIILTI ICYLGLPRLE FYRYYQQLKL
EGPGEQETKL DLISKGEEPR AGKEESGVSV SNSQPTNESH SIKAILKNIS VLAFSVCFIF
TITIGMFPAV TVEVKSSIAG SSTWERYFIP VSCFLTFNIF DWLGRSLTAV FMWPGKDSRW
LPSLVLARLV FVPLLLLCNI KPRRYLTVVF EHDAWFIFFM AAFAFSNGYL ASLCMCFGPK
KVKPAEAETA GAIMAFFLCL GLALGAVFSF LFRAIV
