S29A3_HUMAN
ID S29A3_HUMAN Reviewed; 475 AA.
AC Q9BZD2; B2RB50; B4E2Z9; B7ZA37; Q0VAM9; Q5T465; Q7RTT8; Q8IVZ0; Q9BWI2;
AC Q9NUS9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Equilibrative nucleoside transporter 3;
DE Short=hENT3;
DE AltName: Full=Solute carrier family 29 member 3;
GN Name=SLC29A3; Synonyms=ENT3; ORFNames=UNQ717/PRO1380;
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 VARIANTS PHE-158; ILE-239 AND
RP VAL-326.
RC TISSUE=Placenta;
RX PubMed=11396612; DOI=10.1080/09687680118799;
RA Hyde R.J., Cass C.E., Young J.D., Baldwin S.A.;
RT "The ENT family of eukaryote nucleoside and nucleobase transporters: recent
RT advances in the investigation of structure/function relationships and the
RT identification of novel isoforms.";
RL Mol. Membr. Biol. 18:53-63(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PHE-158; ILE-239 AND
RP VAL-326.
RC TISSUE=Intestine;
RA Tse C.-M., Ward J.L., Toan S.-V., Leung G.P.H., To K.K.W.;
RT "Expression of human equilibrative nucleoside transporter-3 confers
RT cellular resistance to nucleoside drugs.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-18;
RP ILE-239 AND VAL-326.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP PHE-158; ILE-239 AND VAL-326.
RC TISSUE=Placenta, Skin fibroblast, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PHE-158;
RP ILE-239 AND VAL-326.
RC TISSUE=Eye, and Kidney;
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 [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF LEU-31 AND LEU-32.
RX PubMed=15701636; DOI=10.1074/jbc.m414337200;
RA Baldwin S.A., Yao S.Y.M., Hyde R.J., Ng A.M.L., Foppolo S., Barnes K.,
RA Ritzel M.W.L., Cass C.E., Young J.D.;
RT "Functional characterization of novel human and mouse equilibrative
RT nucleoside transporters (hENT3 and mENT3) located in intracellular
RT membranes.";
RL J. Biol. Chem. 280:15880-15887(2005).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [10]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-427, AND CHARACTERIZATION OF
RP VARIANTS HLAS ARG-116; SER-427; ARG-437 AND ARG-449.
RX PubMed=20595384; DOI=10.1074/jbc.m110.109199;
RA Kang N., Jun A.H., Bhutia Y.D., Kannan N., Unadkat J.D., Govindarajan R.;
RT "Human equilibrative nucleoside transporter-3 (hENT3) spectrum disorder
RT mutations impair nucleoside transport, protein localization, and
RT stability.";
RL J. Biol. Chem. 285:28343-28352(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP VARIANTS HLAS SER-427 AND ARG-437.
RX PubMed=18940313; DOI=10.1016/j.ajhg.2008.09.013;
RA Molho-Pessach V., Lerer I., Abeliovich D., Agha Z., Abu Libdeh A.,
RA Broshtilova V., Elpeleg O., Zlotogorski A.;
RT "The H syndrome is caused by mutations in the nucleoside transporter
RT hENT3.";
RL Am. J. Hum. Genet. 83:529-534(2008).
RN [13]
RP VARIANTS HLAS ARG-116; ARG-437 AND ARG-449.
RX PubMed=19336477; DOI=10.1093/hmg/ddp161;
RA Cliffe S.T., Kramer J.M., Hussain K., Robben J.H., de Jong E.K.,
RA de Brouwer A.P., Nibbeling E., Kamsteeg E.J., Wong M., Prendiville J.,
RA James C., Padidela R., Becknell C., van Bokhoven H., Deen P.M.,
RA Hennekam R.C., Lindeman R., Schenck A., Roscioli T., Buckley M.F.;
RT "SLC29A3 gene is mutated in pigmented hypertrichosis with insulin-dependent
RT diabetes mellitus syndrome and interacts with the insulin signaling
RT pathway.";
RL Hum. Mol. Genet. 18:2257-2265(2009).
RN [14]
RP VARIANTS HLAS CYS-134 AND ARG-437.
RX PubMed=20199539; DOI=10.1111/j.1365-2133.2010.09653.x;
RA Priya T.P., Philip N., Molho-Pessach V., Busa T., Dalal A., Zlotogorski A.;
RT "H syndrome: novel and recurrent mutations in SLC29A3.";
RL Br. J. Dermatol. 162:1132-1134(2010).
RN [15]
RP VARIANTS HLAS SER-427 AND ARG-437.
RX PubMed=20619369; DOI=10.1016/j.ejmg.2010.06.012;
RA Spiegel R., Cliffe S.T., Buckley M.F., Crow Y.J., Urquhart J., Horovitz Y.,
RA Tenenbaum-Rakover Y., Newman W.G., Donnai D., Shalev S.A.;
RT "Expanding the clinical spectrum of SLC29A3 gene defects.";
RL Eur. J. Med. Genet. 53:309-313(2010).
RN [16]
RP VARIANTS HLAS ARG-184 AND ARG-437.
RX PubMed=20399510; DOI=10.1016/j.ijporl.2010.03.053;
RA Ramot Y., Sayama K., Sheffer R., Doviner V., Hiller N.,
RA Kaufmann-Yehezkely M., Zlotogorski A.;
RT "Early-onset sensorineural hearing loss is a prominent feature of H
RT syndrome.";
RL Int. J. Pediatr. Otorhinolaryngol. 74:825-827(2010).
RN [17]
RP VARIANTS HLAS TRP-363 AND GLN-363.
RX PubMed=19889517; DOI=10.1016/j.jdermsci.2009.09.011;
RA Molho-Pessach V., Suarez J., Perrin C., Chiaverini C., Doviner V.,
RA Tristan-Clavijo E., Colmenero I., Giuliano F., Torrelo A., Zlotogorski A.;
RT "The H syndrome: two novel mutations affecting the same amino acid residue
RT of hENT3.";
RL J. Dermatol. Sci. 57:59-61(2010).
RN [18]
RP VARIANT HLAS ARG-437, AND VARIANTS VAL-163; PRO-281 AND MET-407.
RX PubMed=20140240; DOI=10.1371/journal.pgen.1000833;
RA Morgan N.V., Morris M.R., Cangul H., Gleeson D., Straatman-Iwanowska A.,
RA Davies N., Keenan S., Pasha S., Rahman F., Gentle D., Vreeswijk M.P.,
RA Devilee P., Knowles M.A., Ceylaner S., Trembath R.C., Dalence C.,
RA Kismet E., Koseoglu V., Rossbach H.C., Gissen P., Tannahill D., Maher E.R.;
RT "Mutations in SLC29A3, encoding an equilibrative nucleoside transporter
RT ENT3, cause a familial histiocytosis syndrome (Faisalabad histiocytosis)
RT and familial Rosai-Dorfman disease.";
RL PLoS Genet. 6:E1000833-E1000833(2010).
RN [19]
RP VARIANT HLAS GLN-363.
RX PubMed=21888995; DOI=10.1016/j.ejmg.2011.06.009;
RA Jonard L., Couloigner V., Pierrot S., Louha M., Gherbi S., Denoyelle F.,
RA Marlin S.;
RT "Progressive hearing loss associated with a unique cervical node due to a
RT homozygous SLC29A3 mutation: a very mild phenotype.";
RL Eur. J. Med. Genet. 55:56-58(2012).
CC -!- FUNCTION: Mediates both influx and efflux of nucleosides across the
CC membrane (equilibrative transporter). Mediates transport of adenine,
CC adenosine and uridine, as well as several nucleoside analog drugs, such
CC as anticancer and antiviral agents, including cladribine, cordycepin,
CC tubercidin and AZT. Does not transport hypoxanthine.
CC {ECO:0000269|PubMed:15701636}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.86 mM for adenosine {ECO:0000269|PubMed:15701636};
CC KM=2.02 mM for uridine {ECO:0000269|PubMed:15701636};
CC pH dependence:
CC Optimum pH is 5.5 for adenosine uptake.
CC {ECO:0000269|PubMed:15701636};
CC -!- INTERACTION:
CC Q9BZD2; O43889-2: CREB3; NbExp=3; IntAct=EBI-12701374, EBI-625022;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Late
CC endosome membrane. Lysosome membrane. Note=Observed in a punctate
CC intracellular pattern showing partial colocalization with late
CC endosomes/lysosomes. Not detected at the cell surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZD2-2; Sequence=VSP_037436;
CC -!- TISSUE SPECIFICITY: Widely expressed in both adult and fetal tissues.
CC Highest levels in placenta, uterus, ovary, spleen, lymph node and bone
CC marrow. Lowest levels in brain and heart.
CC {ECO:0000269|PubMed:15701636}.
CC -!- DISEASE: Histiocytosis-lymphadenopathy plus syndrome (HLAS)
CC [MIM:602782]: A syndrome characterized by the combination of features
CC from 2 or more of four histiocytic disorders, originally thought to be
CC distinct: Faisalabad histiocytosis (FHC), sinus histiocytosis with
CC massive lymphadenopathy (SHML), H syndrome, and pigmented
CC hypertrichosis with insulin-dependent diabetes mellitus syndrome
CC (PHID). FHC features include joint deformities, sensorineural hearing
CC loss, and subsequent development of generalized lymphadenopathy and
CC swellings in the eyelids that contain histiocytes. SHML causes lymph
CC node enlargement in children frequently accompanied by fever,
CC leukocytosis, elevated erythrocyte sedimentation rate, and polyclonal
CC hypergammaglobulinemia. H syndrome is characterized by cutaneous
CC hyperpigmentation and hypertrichosis, hepatosplenomegaly, heart
CC anomalies, and hypogonadism; hearing loss is found in about half of
CC patients. PHID is characterized by predominantly antibody-negative
CC insulin-dependent diabetes mellitus associated with pigmented
CC hypertrichosis and variable occurrence of other features of H syndrome.
CC {ECO:0000269|PubMed:18940313, ECO:0000269|PubMed:19336477,
CC ECO:0000269|PubMed:19889517, ECO:0000269|PubMed:20140240,
CC ECO:0000269|PubMed:20199539, ECO:0000269|PubMed:20399510,
CC ECO:0000269|PubMed:20595384, ECO:0000269|PubMed:20619369,
CC ECO:0000269|PubMed:21888995}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92041.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF326987; AAK00958.1; -; mRNA.
DR EMBL; BK000392; DAA00364.1; -; Genomic_DNA.
DR EMBL; AY288928; AAP41133.1; -; mRNA.
DR EMBL; AY358686; AAQ89049.1; -; mRNA.
DR EMBL; AK002022; BAA92041.1; ALT_INIT; mRNA.
DR EMBL; AK314497; BAG37097.1; -; mRNA.
DR EMBL; AK304503; BAG65311.1; -; mRNA.
DR EMBL; AK316152; BAH14523.1; -; mRNA.
DR EMBL; AL359183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000223; AAH00223.1; -; mRNA.
DR EMBL; BC041575; AAH41575.1; -; mRNA.
DR EMBL; BC120996; AAI20997.1; -; mRNA.
DR EMBL; BC120997; AAI20998.1; -; mRNA.
DR CCDS; CCDS7310.1; -. [Q9BZD2-1]
DR RefSeq; NP_001167569.1; NM_001174098.1.
DR RefSeq; NP_060814.4; NM_018344.5. [Q9BZD2-1]
DR RefSeq; XP_016871866.1; XM_017016377.1. [Q9BZD2-2]
DR AlphaFoldDB; Q9BZD2; -.
DR SMR; Q9BZD2; -.
DR BioGRID; 120597; 5.
DR IntAct; Q9BZD2; 2.
DR STRING; 9606.ENSP00000362285; -.
DR DrugBank; DB00640; Adenosine.
DR TCDB; 2.A.57.1.6; the equilibrative nucleoside transporter (ent) family.
DR GlyGen; Q9BZD2; 1 site.
DR iPTMnet; Q9BZD2; -.
DR PhosphoSitePlus; Q9BZD2; -.
DR BioMuta; SLC29A3; -.
DR DMDM; 313104188; -.
DR EPD; Q9BZD2; -.
DR jPOST; Q9BZD2; -.
DR MassIVE; Q9BZD2; -.
DR MaxQB; Q9BZD2; -.
DR PaxDb; Q9BZD2; -.
DR PeptideAtlas; Q9BZD2; -.
DR PRIDE; Q9BZD2; -.
DR ProteomicsDB; 79812; -. [Q9BZD2-1]
DR ProteomicsDB; 79813; -. [Q9BZD2-2]
DR Antibodypedia; 68472; 107 antibodies from 19 providers.
DR DNASU; 55315; -.
DR Ensembl; ENST00000373189.6; ENSP00000362285.5; ENSG00000198246.9. [Q9BZD2-1]
DR GeneID; 55315; -.
DR KEGG; hsa:55315; -.
DR MANE-Select; ENST00000373189.6; ENSP00000362285.5; NM_018344.6; NP_060814.4.
DR UCSC; uc001jrr.5; human. [Q9BZD2-1]
DR CTD; 55315; -.
DR DisGeNET; 55315; -.
DR GeneCards; SLC29A3; -.
DR HGNC; HGNC:23096; SLC29A3.
DR HPA; ENSG00000198246; Low tissue specificity.
DR MalaCards; SLC29A3; -.
DR MIM; 602782; phenotype.
DR MIM; 612373; gene.
DR neXtProt; NX_Q9BZD2; -.
DR OpenTargets; ENSG00000198246; -.
DR Orphanet; 1782; Dysosteosclerosis.
DR Orphanet; 168569; H syndrome.
DR PharmGKB; PA134950750; -.
DR VEuPathDB; HostDB:ENSG00000198246; -.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_6_1_1; -.
DR InParanoid; Q9BZD2; -.
DR OMA; FWNLGDL; -.
DR OrthoDB; 559763at2759; -.
DR PhylomeDB; Q9BZD2; -.
DR TreeFam; TF313950; -.
DR PathwayCommons; Q9BZD2; -.
DR Reactome; R-HSA-5619063; Defective SLC29A3 causes histiocytosis-lymphadenopathy plus syndrome (HLAS).
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR SignaLink; Q9BZD2; -.
DR BioGRID-ORCS; 55315; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC29A3; human.
DR GenomeRNAi; 55315; -.
DR Pharos; Q9BZD2; Tbio.
DR PRO; PR:Q9BZD2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BZD2; protein.
DR Bgee; ENSG00000198246; Expressed in mucosa of urinary bladder and 160 other tissues.
DR ExpressionAtlas; Q9BZD2; baseline and differential.
DR Genevisible; Q9BZD2; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR030193; ENT3.
DR InterPro; IPR002259; Eqnu_transpt.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR PANTHER; PTHR10332:SF17; PTHR10332:SF17; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endosome; Glycoprotein; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Equilibrative nucleoside transporter 3"
FT /id="PRO_0000209343"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P65"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037436"
FT VARIANT 18
FT /note="R -> G (in dbSNP:rs2277257)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_018662"
FT VARIANT 116
FT /note="M -> R (in HLAS; partially retained in the
FT endoplasmic reticulum; results in reduced nucleoside
FT transport; dbSNP:rs267607057)"
FT /evidence="ECO:0000269|PubMed:19336477,
FT ECO:0000269|PubMed:20595384"
FT /id="VAR_067801"
FT VARIANT 134
FT /note="R -> C (in HLAS; dbSNP:rs1430557607)"
FT /evidence="ECO:0000269|PubMed:20199539"
FT /id="VAR_067802"
FT VARIANT 158
FT /note="S -> F (in dbSNP:rs780668)"
FT /evidence="ECO:0000269|PubMed:11396612,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_018663"
FT VARIANT 163
FT /note="G -> V (in dbSNP:rs143557881)"
FT /evidence="ECO:0000269|PubMed:20140240"
FT /id="VAR_067803"
FT VARIANT 184
FT /note="S -> R (in HLAS; dbSNP:rs1023257012)"
FT /evidence="ECO:0000269|PubMed:20399510"
FT /id="VAR_067804"
FT VARIANT 239
FT /note="V -> I (in dbSNP:rs2252996)"
FT /evidence="ECO:0000269|PubMed:11396612,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_018664"
FT VARIANT 281
FT /note="L -> P (in dbSNP:rs79737301)"
FT /evidence="ECO:0000269|PubMed:20140240"
FT /id="VAR_067805"
FT VARIANT 326
FT /note="I -> V (in dbSNP:rs2487068)"
FT /evidence="ECO:0000269|PubMed:11396612,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_018665"
FT VARIANT 363
FT /note="R -> Q (in HLAS; dbSNP:rs387907066)"
FT /evidence="ECO:0000269|PubMed:19889517,
FT ECO:0000269|PubMed:21888995"
FT /id="VAR_067806"
FT VARIANT 363
FT /note="R -> W (in HLAS; dbSNP:rs387907067)"
FT /evidence="ECO:0000269|PubMed:19889517"
FT /id="VAR_067807"
FT VARIANT 407
FT /note="V -> M (in dbSNP:rs144517514)"
FT /evidence="ECO:0000269|PubMed:20140240"
FT /id="VAR_067808"
FT VARIANT 427
FT /note="G -> S (in HLAS; almost total loss of nucleoside
FT transport; dbSNP:rs121912583)"
FT /evidence="ECO:0000269|PubMed:18940313,
FT ECO:0000269|PubMed:20595384, ECO:0000269|PubMed:20619369"
FT /id="VAR_057884"
FT VARIANT 437
FT /note="G -> R (in HLAS; results in reduced nucleoside
FT transport; dbSNP:rs121912584)"
FT /evidence="ECO:0000269|PubMed:18940313,
FT ECO:0000269|PubMed:19336477, ECO:0000269|PubMed:20140240,
FT ECO:0000269|PubMed:20199539, ECO:0000269|PubMed:20399510,
FT ECO:0000269|PubMed:20595384, ECO:0000269|PubMed:20619369"
FT /id="VAR_057885"
FT VARIANT 449
FT /note="T -> R (in HLAS; results in reduced nucleoside
FT transport; dbSNP:rs267607058)"
FT /evidence="ECO:0000269|PubMed:19336477,
FT ECO:0000269|PubMed:20595384"
FT /id="VAR_067809"
FT VARIANT 452
FT /note="V -> E (in dbSNP:rs999940)"
FT /id="VAR_018666"
FT MUTAGEN 31
FT /note="L->A: Localization at the cell surface; when
FT associated with A-32."
FT /evidence="ECO:0000269|PubMed:15701636"
FT MUTAGEN 32
FT /note="L->A: Localization at the cell surface; when
FT associated with A-31."
FT /evidence="ECO:0000269|PubMed:15701636"
FT MUTAGEN 427
FT /note="G->A,F,Y,T: Results in impaired nucleoside
FT transport."
FT /evidence="ECO:0000269|PubMed:20595384"
FT CONFLICT 32
FT /note="L -> P (in Ref. 5; BAG37097)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> A (in Ref. 5; BAA92041)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> S (in Ref. 5; BAG65311)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Q -> R (in Ref. 5; BAA92041)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="M -> I (in Ref. 5; BAG65311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 51815 MW; DBF0918ECA6D5A70 CRC64;
MAVVSEDDFQ HSSNSTYRTT SSSLRADQEA LLEKLLDRPP PGLQRPEDRF CGTYIIFFSL
GIGSLLPWNF FITAKEYWMF KLRNSSSPAT GEDPEGSDIL NYFESYLAVA STVPSMLCLV
ANFLLVNRVA VHIRVLASLT VILAIFMVIT ALVKVDTSSW TRGFFAVTIV CMVILSGAST
VFSSSIYGMT GSFPMRNSQA LISGGAMGGT VSAVASLVDL AASSDVRNSA LAFFLTATVF
LVLCMGLYLL LSRLEYARYY MRPVLAAHVF SGEEELPQDS LSAPSVASRF IDSHTPPLRP
ILKKTASLGF CVTYVFFITS LIYPAICTNI ESLNKGSGSL WTTKFFIPLT TFLLYNFADL
CGRQLTAWIQ VPGPNSKALP GFVLLRTCLI PLFVLCNYQP RVHLKTVVFQ SDVYPALLSS
LLGLSNGYLS TLALLYGPKI VPRELAEATG VVMSFYVCLG LTLGSACSTL LVHLI
