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Equilibrative nucleoside transporter 3 (hENT3) (Solute carrier family 29 member 3)

 S29A3_HUMAN             Reviewed;         475 AA.
Q9BZD2; B2RB50; B4E2Z9; B7ZA37; Q0VAM9; Q5T465; Q7RTT8; Q8IVZ0;
Q9BWI2; Q9NUS9;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
05-DEC-2018, entry version 144.
RecName: Full=Equilibrative nucleoside transporter 3;
Short=hENT3;
AltName: Full=Solute carrier family 29 member 3;
Name=SLC29A3; Synonyms=ENT3; ORFNames=UNQ717/PRO1380;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PHE-158; ILE-239
AND VAL-326.
TISSUE=Placenta;
PubMed=11396612; DOI=10.1080/09687680118799;
Hyde R.J., Cass C.E., Young J.D., Baldwin S.A.;
"The ENT family of eukaryote nucleoside and nucleobase transporters:
recent advances in the investigation of structure/function
relationships and the identification of novel isoforms.";
Mol. Membr. Biol. 18:53-63(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12384580; DOI=10.1093/nar/gkf564;
Sankar N., Machado J., Abdulla P., Hilliker A.J., Coe I.R.;
"Comparative genomic analysis of equilibrative nucleoside transporters
suggests conserved protein structure despite limited sequence
identity.";
Nucleic Acids Res. 30:4339-4350(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PHE-158; ILE-239
AND VAL-326.
TISSUE=Intestine;
Tse C.-M., Ward J.L., Toan S.-V., Leung G.P.H., To K.K.W.;
"Expression of human equilibrative nucleoside transporter-3 confers
cellular resistance to nucleoside drugs.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-18; ILE-239 AND VAL-326.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS PHE-158; ILE-239 AND VAL-326.
TISSUE=Placenta, Skin fibroblast, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
PHE-158; ILE-239 AND VAL-326.
TISSUE=Eye, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF LEU-31 AND LEU-32.
PubMed=15701636; DOI=10.1074/jbc.M414337200;
Baldwin S.A., Yao S.Y.M., Hyde R.J., Ng A.M.L., Foppolo S., Barnes K.,
Ritzel M.W.L., Cass C.E., Young J.D.;
"Functional characterization of novel human and mouse equilibrative
nucleoside transporters (hENT3 and mENT3) located in intracellular
membranes.";
J. Biol. Chem. 280:15880-15887(2005).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[10]
SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-427, AND CHARACTERIZATION OF
VARIANTS HLAS ARG-116; SER-427; ARG-437 AND ARG-449.
PubMed=20595384; DOI=10.1074/jbc.M110.109199;
Kang N., Jun A.H., Bhutia Y.D., Kannan N., Unadkat J.D.,
Govindarajan R.;
"Human equilibrative nucleoside transporter-3 (hENT3) spectrum
disorder mutations impair nucleoside transport, protein localization,
and stability.";
J. Biol. Chem. 285:28343-28352(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
VARIANTS HLAS SER-427 AND ARG-437.
PubMed=18940313; DOI=10.1016/j.ajhg.2008.09.013;
Molho-Pessach V., Lerer I., Abeliovich D., Agha Z., Abu Libdeh A.,
Broshtilova V., Elpeleg O., Zlotogorski A.;
"The H syndrome is caused by mutations in the nucleoside transporter
hENT3.";
Am. J. Hum. Genet. 83:529-534(2008).
[13]
VARIANTS HLAS ARG-116; ARG-437 AND ARG-449.
PubMed=19336477; DOI=10.1093/hmg/ddp161;
Cliffe S.T., Kramer J.M., Hussain K., Robben J.H., de Jong E.K.,
de Brouwer A.P., Nibbeling E., Kamsteeg E.J., Wong M., Prendiville J.,
James C., Padidela R., Becknell C., van Bokhoven H., Deen P.M.,
Hennekam R.C., Lindeman R., Schenck A., Roscioli T., Buckley M.F.;
"SLC29A3 gene is mutated in pigmented hypertrichosis with insulin-
dependent diabetes mellitus syndrome and interacts with the insulin
signaling pathway.";
Hum. Mol. Genet. 18:2257-2265(2009).
[14]
VARIANTS HLAS CYS-134 AND ARG-437.
PubMed=20199539; DOI=10.1111/j.1365-2133.2010.09653.x;
Priya T.P., Philip N., Molho-Pessach V., Busa T., Dalal A.,
Zlotogorski A.;
"H syndrome: novel and recurrent mutations in SLC29A3.";
Br. J. Dermatol. 162:1132-1134(2010).
[15]
VARIANTS HLAS SER-427 AND ARG-437.
PubMed=20619369; DOI=10.1016/j.ejmg.2010.06.012;
Spiegel R., Cliffe S.T., Buckley M.F., Crow Y.J., Urquhart J.,
Horovitz Y., Tenenbaum-Rakover Y., Newman W.G., Donnai D.,
Shalev S.A.;
"Expanding the clinical spectrum of SLC29A3 gene defects.";
Eur. J. Med. Genet. 53:309-313(2010).
[16]
VARIANTS HLAS ARG-184 AND ARG-437.
PubMed=20399510; DOI=10.1016/j.ijporl.2010.03.053;
Ramot Y., Sayama K., Sheffer R., Doviner V., Hiller N.,
Kaufmann-Yehezkely M., Zlotogorski A.;
"Early-onset sensorineural hearing loss is a prominent feature of H
syndrome.";
Int. J. Pediatr. Otorhinolaryngol. 74:825-827(2010).
[17]
VARIANTS HLAS TRP-363 AND GLN-363.
PubMed=19889517; DOI=10.1016/j.jdermsci.2009.09.011;
Molho-Pessach V., Suarez J., Perrin C., Chiaverini C., Doviner V.,
Tristan-Clavijo E., Colmenero I., Giuliano F., Torrelo A.,
Zlotogorski A.;
"The H syndrome: two novel mutations affecting the same amino acid
residue of hENT3.";
J. Dermatol. Sci. 57:59-61(2010).
[18]
VARIANT HLAS ARG-437, AND VARIANTS VAL-163; PRO-281 AND MET-407.
PubMed=20140240; DOI=10.1371/journal.pgen.1000833;
Morgan N.V., Morris M.R., Cangul H., Gleeson D.,
Straatman-Iwanowska A., Davies N., Keenan S., Pasha S., Rahman F.,
Gentle D., Vreeswijk M.P., Devilee P., Knowles M.A., Ceylaner S.,
Trembath R.C., Dalence C., Kismet E., Koseoglu V., Rossbach H.C.,
Gissen P., Tannahill D., Maher E.R.;
"Mutations in SLC29A3, encoding an equilibrative nucleoside
transporter ENT3, cause a familial histiocytosis syndrome (Faisalabad
histiocytosis) and familial Rosai-Dorfman disease.";
PLoS Genet. 6:E1000833-E1000833(2010).
[19]
VARIANT HLAS GLN-363.
PubMed=21888995; DOI=10.1016/j.ejmg.2011.06.009;
Jonard L., Couloigner V., Pierrot S., Louha M., Gherbi S.,
Denoyelle F., Marlin S.;
"Progressive hearing loss associated with a unique cervical node due
to a homozygous SLC29A3 mutation: a very mild phenotype.";
Eur. J. Med. Genet. 55:56-58(2012).
-!- FUNCTION: Mediates both influx and efflux of nucleosides across
the membrane (equilibrative transporter). Mediates transport of
adenine, adenosine and uridine, as well as several nucleoside
analog drugs, such as anticancer and antiviral agents, including
cladribine, cordycepin, tubercidin and AZT. Does not transport
hypoxanthine. {ECO:0000269|PubMed:15701636}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.86 mM for adenosine {ECO:0000269|PubMed:15701636};
KM=2.02 mM for uridine {ECO:0000269|PubMed:15701636};
pH dependence:
Optimum pH is 5.5 for adenosine uptake.
{ECO:0000269|PubMed:15701636};
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-12701374, EBI-625022;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Late
endosome membrane. Lysosome membrane. Note=Observed in a punctate
intracellular pattern showing partial colocalization with late
endosomes/lysosomes. Not detected at the cell surface.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BZD2-1; Sequence=Displayed;
Name=2;
IsoId=Q9BZD2-2; Sequence=VSP_037436;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in both adult and fetal
tissues. Highest levels in placenta, uterus, ovary, spleen, lymph
node and bone marrow. Lowest levels in brain and heart.
{ECO:0000269|PubMed:15701636}.
-!- DISEASE: Histiocytosis-lymphadenopathy plus syndrome (HLAS)
[MIM:602782]: A syndrome characterized by the combination of
features from 2 or more of four histiocytic disorders, originally
thought to be distinct: Faisalabad histiocytosis (FHC), sinus
histiocytosis with massive lymphadenopathy (SHML), H syndrome, and
pigmented hypertrichosis with insulin-dependent diabetes mellitus
syndrome (PHID). FHC features include joint deformities,
sensorineural hearing loss, and subsequent development of
generalized lymphadenopathy and swellings in the eyelids that
contain histiocytes. SHML causes lymph node enlargement in
children frequently accompanied by fever, leukocytosis, elevated
erythrocyte sedimentation rate, and polyclonal
hypergammaglobulinemia. H syndrome is characterized by cutaneous
hyperpigmentation and hypertrichosis, hepatosplenomegaly, heart
anomalies, and hypogonadism; hearing loss is found in about half
of patients. PHID is characterized by predominantly antibody-
negative insulin-dependent diabetes mellitus associated with
pigmented hypertrichosis and variable occurrence of other features
of H syndrome. {ECO:0000269|PubMed:18940313,
ECO:0000269|PubMed:19336477, ECO:0000269|PubMed:19889517,
ECO:0000269|PubMed:20140240, ECO:0000269|PubMed:20199539,
ECO:0000269|PubMed:20399510, ECO:0000269|PubMed:20595384,
ECO:0000269|PubMed:20619369, ECO:0000269|PubMed:21888995}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92041.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF326987; AAK00958.1; -; mRNA.
EMBL; BK000392; DAA00364.1; -; Genomic_DNA.
EMBL; AY288928; AAP41133.1; -; mRNA.
EMBL; AY358686; AAQ89049.1; -; mRNA.
EMBL; AK002022; BAA92041.1; ALT_INIT; mRNA.
EMBL; AK314497; BAG37097.1; -; mRNA.
EMBL; AK304503; BAG65311.1; -; mRNA.
EMBL; AK316152; BAH14523.1; -; mRNA.
EMBL; AL359183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000223; AAH00223.1; -; mRNA.
EMBL; BC041575; AAH41575.1; -; mRNA.
EMBL; BC120996; AAI20997.1; -; mRNA.
EMBL; BC120997; AAI20998.1; -; mRNA.
CCDS; CCDS7310.1; -. [Q9BZD2-1]
RefSeq; NP_001167569.1; NM_001174098.1.
RefSeq; NP_060814.4; NM_018344.5. [Q9BZD2-1]
RefSeq; XP_016871866.1; XM_017016377.1. [Q9BZD2-2]
UniGene; Hs.438419; -.
ProteinModelPortal; Q9BZD2; -.
IntAct; Q9BZD2; 1.
STRING; 9606.ENSP00000362285; -.
TCDB; 2.A.57.1.6; the equilibrative nucleoside transporter (ent) family.
iPTMnet; Q9BZD2; -.
PhosphoSitePlus; Q9BZD2; -.
BioMuta; SLC29A3; -.
DMDM; 313104188; -.
EPD; Q9BZD2; -.
MaxQB; Q9BZD2; -.
PaxDb; Q9BZD2; -.
PeptideAtlas; Q9BZD2; -.
PRIDE; Q9BZD2; -.
ProteomicsDB; 79812; -.
ProteomicsDB; 79813; -. [Q9BZD2-2]
Ensembl; ENST00000373189; ENSP00000362285; ENSG00000198246. [Q9BZD2-1]
Ensembl; ENST00000642647; ENSP00000495980; ENSG00000198246. [Q9BZD2-1]
GeneID; 55315; -.
KEGG; hsa:55315; -.
UCSC; uc001jrr.5; human. [Q9BZD2-1]
CTD; 55315; -.
DisGeNET; 55315; -.
EuPathDB; HostDB:ENSG00000198246.7; -.
GeneCards; SLC29A3; -.
H-InvDB; HIX0008903; -.
HGNC; HGNC:23096; SLC29A3.
HPA; HPA046085; -.
HPA; HPA054976; -.
HPA; HPA057905; -.
MalaCards; SLC29A3; -.
MIM; 602782; phenotype.
MIM; 612373; gene.
neXtProt; NX_Q9BZD2; -.
OpenTargets; ENSG00000198246; -.
Orphanet; 1782; Dysosteosclerosis.
Orphanet; 168569; H syndrome.
PharmGKB; PA134950750; -.
eggNOG; KOG1479; Eukaryota.
eggNOG; ENOG410Y3MT; LUCA.
GeneTree; ENSGT00940000153807; -.
HOVERGEN; HBG108444; -.
InParanoid; Q9BZD2; -.
KO; K15014; -.
OMA; CNYQPRV; -.
OrthoDB; EOG091G09WB; -.
PhylomeDB; Q9BZD2; -.
TreeFam; TF313950; -.
Reactome; R-HSA-5619063; Defective SLC29A3 causes histiocytosis-lymphadenopathy plus syndrome (HLAS).
Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
ChiTaRS; SLC29A3; human.
GenomeRNAi; 55315; -.
PRO; PR:Q9BZD2; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000198246; Expressed in 190 organ(s), highest expression level in chorionic villus.
CleanEx; HS_SLC29A3; -.
Genevisible; Q9BZD2; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
InterPro; IPR030193; ENT3.
InterPro; IPR002259; Eqnu_transpt.
PANTHER; PTHR10332; PTHR10332; 1.
PANTHER; PTHR10332:SF17; PTHR10332:SF17; 1.
Pfam; PF01733; Nucleoside_tran; 1.
PIRSF; PIRSF016379; ENT; 1.
PRINTS; PR01130; DERENTRNSPRT.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation; Endosome;
Glycoprotein; Lysosome; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 475 Equilibrative nucleoside transporter 3.
/FTId=PRO_0000209343.
TOPO_DOM 1 53 Cytoplasmic. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255}.
TOPO_DOM 75 105 Extracellular. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TOPO_DOM 127 134 Cytoplasmic. {ECO:0000255}.
TRANSMEM 135 155 Helical. {ECO:0000255}.
TOPO_DOM 156 162 Extracellular. {ECO:0000255}.
TRANSMEM 163 183 Helical. {ECO:0000255}.
TOPO_DOM 184 199 Cytoplasmic. {ECO:0000255}.
TRANSMEM 200 220 Helical. {ECO:0000255}.
TOPO_DOM 221 230 Extracellular. {ECO:0000255}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
TOPO_DOM 252 305 Cytoplasmic. {ECO:0000255}.
TRANSMEM 306 326 Helical. {ECO:0000255}.
TOPO_DOM 327 337 Extracellular. {ECO:0000255}.
TRANSMEM 338 358 Helical. {ECO:0000255}.
TOPO_DOM 359 377 Cytoplasmic. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TOPO_DOM 399 415 Extracellular. {ECO:0000255}.
TRANSMEM 416 436 Helical. {ECO:0000255}.
TOPO_DOM 437 454 Cytoplasmic. {ECO:0000255}.
TRANSMEM 455 475 Helical. {ECO:0000255}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:Q99P65}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 146 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037436.
VARIANT 18 18 R -> G (in dbSNP:rs2277257).
{ECO:0000269|PubMed:12975309}.
/FTId=VAR_018662.
VARIANT 116 116 M -> R (in HLAS; partially retained in
the endoplasmic reticulum; results in
reduced nucleoside transport;
dbSNP:rs267607057).
{ECO:0000269|PubMed:19336477,
ECO:0000269|PubMed:20595384}.
/FTId=VAR_067801.
VARIANT 134 134 R -> C (in HLAS).
{ECO:0000269|PubMed:20199539}.
/FTId=VAR_067802.
VARIANT 158 158 S -> F (in dbSNP:rs780668).
{ECO:0000269|PubMed:11396612,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_018663.
VARIANT 163 163 G -> V (in dbSNP:rs143557881).
{ECO:0000269|PubMed:20140240}.
/FTId=VAR_067803.
VARIANT 184 184 S -> R (in HLAS; dbSNP:rs1023257012).
{ECO:0000269|PubMed:20399510}.
/FTId=VAR_067804.
VARIANT 239 239 V -> I (in dbSNP:rs2252996).
{ECO:0000269|PubMed:11396612,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_018664.
VARIANT 281 281 L -> P (in dbSNP:rs79737301).
{ECO:0000269|PubMed:20140240}.
/FTId=VAR_067805.
VARIANT 326 326 I -> V (in dbSNP:rs2487068).
{ECO:0000269|PubMed:11396612,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_018665.
VARIANT 363 363 R -> Q (in HLAS; dbSNP:rs387907066).
{ECO:0000269|PubMed:19889517,
ECO:0000269|PubMed:21888995}.
/FTId=VAR_067806.
VARIANT 363 363 R -> W (in HLAS; dbSNP:rs387907067).
{ECO:0000269|PubMed:19889517}.
/FTId=VAR_067807.
VARIANT 407 407 V -> M (in dbSNP:rs144517514).
{ECO:0000269|PubMed:20140240}.
/FTId=VAR_067808.
VARIANT 427 427 G -> S (in HLAS; almost total loss of
nucleoside transport; dbSNP:rs121912583).
{ECO:0000269|PubMed:18940313,
ECO:0000269|PubMed:20595384,
ECO:0000269|PubMed:20619369}.
/FTId=VAR_057884.
VARIANT 437 437 G -> R (in HLAS; results in reduced
nucleoside transport; dbSNP:rs121912584).
{ECO:0000269|PubMed:18940313,
ECO:0000269|PubMed:19336477,
ECO:0000269|PubMed:20140240,
ECO:0000269|PubMed:20199539,
ECO:0000269|PubMed:20399510,
ECO:0000269|PubMed:20595384,
ECO:0000269|PubMed:20619369}.
/FTId=VAR_057885.
VARIANT 449 449 T -> R (in HLAS; results in reduced
nucleoside transport; dbSNP:rs267607058).
{ECO:0000269|PubMed:19336477,
ECO:0000269|PubMed:20595384}.
/FTId=VAR_067809.
VARIANT 452 452 V -> E (in dbSNP:rs999940).
/FTId=VAR_018666.
MUTAGEN 31 31 L->A: Localization at the cell surface;
when associated with A-32.
{ECO:0000269|PubMed:15701636}.
MUTAGEN 32 32 L->A: Localization at the cell surface;
when associated with A-31.
{ECO:0000269|PubMed:15701636}.
MUTAGEN 427 427 G->A,F,Y,T: Results in impaired
nucleoside transport.
{ECO:0000269|PubMed:20595384}.
CONFLICT 32 32 L -> P (in Ref. 5; BAG37097).
{ECO:0000305}.
CONFLICT 112 112 T -> A (in Ref. 5; BAA92041).
{ECO:0000305}.
CONFLICT 306 306 A -> S (in Ref. 5; BAG65311).
{ECO:0000305}.
CONFLICT 370 370 Q -> R (in Ref. 5; BAA92041).
{ECO:0000305}.
CONFLICT 453 453 M -> I (in Ref. 5; BAG65311).
{ECO:0000305}.
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


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