S28A1_HUMAN
ID S28A1_HUMAN Reviewed; 649 AA.
AC O00337; A0AV42; A8K7I2; O00335; O00336; Q5U5S6; Q5U648; Q9UEZ9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sodium/nucleoside cotransporter 1;
DE AltName: Full=Concentrative nucleoside transporter 1 {ECO:0000303|PubMed:9124315};
DE Short=CNT 1 {ECO:0000303|PubMed:9124315};
DE Short=hCNT1 {ECO:0000303|PubMed:9124315};
DE AltName: Full=Na(+)/nucleoside cotransporter 1;
DE AltName: Full=Sodium-coupled nucleoside transporter 1;
DE AltName: Full=Solute carrier family 28 member 1;
GN Name=SLC28A1; Synonyms=CNT1 {ECO:0000303|PubMed:9124315};
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), FUNCTION, TRANSPORTER ACTIVITY,
RP TISSUE SPECIFICITY, POLYMORPHISM, VARIANTS A GLY-34; VAL-140 INS AND
RP ILE-189, VARIANTS B SER-409 AND ASN-521, AND VARIANT C ASN-521.
RC TISSUE=Kidney;
RX PubMed=9124315; DOI=10.1152/ajpcell.1997.272.2.c707;
RA Ritzel M.W.L., Yao S.Y.M., Huang M.-Y., Elliott J.F., Cass C.E.,
RA Young J.D.;
RT "Molecular cloning and functional expression of cDNAs encoding a human Na+-
RT nucleoside cotransporter (hCNT1).";
RL Am. J. Physiol. 272:C707-C714(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT A GLY-34.
RA Ritzel M.W.L., Ritzel R.G., Cass C.E., Young J.D.;
RT "Genomic organization and sequence of the gene encoding the human sodium-
RT dependent, pyrimidine-selective nucleoside transporter (CNT1).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT A ILE-189, VARIANT B
RP ASN-521, AND VARIANT C ASN-521.
RC TISSUE=Small intestine;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS A
RP VAL-140 INS AND CYS-510.
RC TISSUE=Colon;
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 [6]
RP FUNCTION, AND MUTAGENESIS OF SER-318; GLN-319 AND SER-352.
RX PubMed=10455109; DOI=10.1074/jbc.274.35.24475;
RA Loewen S.K., Ng A.M.L., Yao S.Y.M., Cass C.E., Baldwin S.A., Young J.D.;
RT "Identification of amino acid residues responsible for the pyrimidine and
RT purine nucleoside specificities of human concentrative Na(+) nucleoside
RT cotransporters hCNT1 and hCNT2.";
RL J. Biol. Chem. 274:24475-24484(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT URCTU PRO-546,
RP AND MUTAGENESIS OF SER-546.
RX PubMed=21998139; DOI=10.1152/ajpcell.00198.2011;
RA Cano-Soldado P., Gorraitz E., Errasti-Murugarren E., Casado F.J.,
RA Lostao M.P., Pastor-Anglada M.;
RT "Functional analysis of the human concentrative nucleoside transporter-1
RT variant hCNT1S546P provides insight into the sodium-binding pocket.";
RL Am. J. Physiol. 302:C257-C266(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP INVOLVEMENT IN URCTU, FUNCTION, VARIANTS URCTU CYS-510 AND GLN-561, AND
RP CHARACTERIZATION OF VARIANTS URCTU CYS-510 AND GLN-561.
RX PubMed=30658162; DOI=10.1016/j.bbadis.2019.01.013;
RA Perez-Torras S., Mata-Ventosa A., Droegemoeller B., Tarailo-Graovac M.,
RA Meijer J., Meinsma R., van Cruchten A.G., Kulik W., Viel-Oliva A.,
RA Bidon-Chanal A., Ross C.J., Wassermann W.W., van Karnebeek C.D.M.,
RA Pastor-Anglada M., van Kuilenburg A.B.P.;
RT "Deficiency of perforin and hCNT1, a novel inborn error of pyrimidine
RT metabolism, associated with a rapidly developing lethal phenotype due to
RT multi-organ failure.";
RL Biochim. Biophys. Acta 1865:1182-1191(2019).
RN [10]
RP INVOLVEMENT IN URCTU, AND VARIANT URCTU PRO-546.
RX PubMed=30847922; DOI=10.1002/jimd.12081;
RA Wevers R.A., Christensen M., Engelke U.F.H., Geuer S., Coene K.L.M.,
RA Kwast J.T., Lund A.M., Vissers L.E.L.M.;
RT "Functional disruption of pyrimidine nucleoside transporter CNT1 results in
RT a novel inborn error of metabolism with high excretion of uridine and
RT cytidine.";
RL J. Inherit. Metab. Dis. 42:494-500(2019).
CC -!- FUNCTION: Sodium-dependent and pyrimidine-selective transporter
CC (PubMed:9124315, PubMed:21998139, PubMed:10455109, PubMed:30658162).
CC Exhibits the transport characteristics of the nucleoside transport
CC system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides
CC and adenosine) (PubMed:21998139). Transports uridine, cytidine,
CC thymidine, and nucleoside-derived drugs (PubMed:21998139). Transports
CC the antiviral pyrimidine nucleoside analogs 3'-azido-3'-deoxythymidine
CC (AZT) and 2',3'-dideoxycytidine (ddC) (PubMed:9124315). It may be
CC involved in the intestinal absorption and renal handling of pyrimidine
CC nucleoside analogs used to treat acquired immunodeficiency syndrome
CC (AIDS) (PubMed:9124315). It has the following selective inhibition:
CC adenosine, thymidine, cytidine, uridine >> guanosine, inosine
CC (PubMed:9124315). {ECO:0000269|PubMed:10455109,
CC ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:30658162,
CC ECO:0000269|PubMed:9124315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in);
CC Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:9124315};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(out) + thymidine(out) = Na(+)(in) + thymidine(in);
CC Xref=Rhea:RHEA:69891, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:9124315};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(out) + Na(+)(out) = cytidine(in) + Na(+)(in);
CC Xref=Rhea:RHEA:69895, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:9124315};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21998139};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00337-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00337-2; Sequence=VSP_037221, VSP_037222;
CC -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:9124315}.
CC -!- POLYMORPHISM: Three variant forms of isoform 1 (A, B and C) are
CC expressed in the kidney. All three variant forms have similar
CC nucleoside transport activity. {ECO:0000269|PubMed:9124315}.
CC -!- DISEASE: Uridine-cytidineuria (URCTU) [MIM:618477]: An autosomal
CC recessive inborn error of metabolism characterized by increased urinary
CC uridine and cytidine excretion. It is a likely benign metabolic trait
CC without clinical manifestations. {ECO:0000269|PubMed:21998139,
CC ECO:0000269|PubMed:30658162, ECO:0000269|PubMed:30847922}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; U62966; AAB53837.1; -; mRNA.
DR EMBL; U62967; AAB53838.1; -; mRNA.
DR EMBL; U62968; AAB53839.1; -; mRNA.
DR EMBL; AF187978; AAF15353.1; -; Genomic_DNA.
DR EMBL; AF187969; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187970; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187971; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187972; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187973; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187974; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187975; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187976; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AF187977; AAF15353.1; JOINED; Genomic_DNA.
DR EMBL; AK291997; BAF84686.1; -; mRNA.
DR EMBL; AC087468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029788; AAH29788.1; -; mRNA.
DR EMBL; BC039898; AAH39898.1; -; mRNA.
DR EMBL; BC126204; AAI26205.1; -; mRNA.
DR EMBL; BC126206; AAI26207.1; -; mRNA.
DR CCDS; CCDS10334.1; -. [O00337-1]
DR CCDS; CCDS10335.1; -. [O00337-2]
DR RefSeq; NP_001274691.1; NM_001287762.1. [O00337-1]
DR RefSeq; NP_004204.3; NM_004213.4. [O00337-1]
DR RefSeq; NP_964014.1; NM_201651.2. [O00337-2]
DR AlphaFoldDB; O00337; -.
DR SMR; O00337; -.
DR IntAct; O00337; 1.
DR STRING; 9606.ENSP00000378074; -.
DR BindingDB; O00337; -.
DR ChEMBL; CHEMBL5551; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB01262; Decitabine.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB00649; Stavudine.
DR DrugBank; DB09327; Tegafur-uracil.
DR DrugBank; DB00432; Trifluridine.
DR DrugBank; DB00495; Zidovudine.
DR DrugCentral; O00337; -.
DR TCDB; 2.A.41.2.3; the concentrative nucleoside transporter (cnt) family.
DR GlyGen; O00337; 2 sites.
DR iPTMnet; O00337; -.
DR PhosphoSitePlus; O00337; -.
DR BioMuta; SLC28A1; -.
DR EPD; O00337; -.
DR jPOST; O00337; -.
DR MassIVE; O00337; -.
DR PaxDb; O00337; -.
DR PeptideAtlas; O00337; -.
DR PRIDE; O00337; -.
DR ProteomicsDB; 47852; -. [O00337-1]
DR ProteomicsDB; 47853; -. [O00337-2]
DR Antibodypedia; 65918; 71 antibodies from 19 providers.
DR DNASU; 9154; -.
DR Ensembl; ENST00000286749.3; ENSP00000286749.3; ENSG00000156222.12. [O00337-1]
DR Ensembl; ENST00000338602.6; ENSP00000341629.2; ENSG00000156222.12. [O00337-2]
DR Ensembl; ENST00000394573.6; ENSP00000378074.1; ENSG00000156222.12. [O00337-1]
DR GeneID; 9154; -.
DR KEGG; hsa:9154; -.
DR MANE-Select; ENST00000394573.6; ENSP00000378074.1; NM_004213.5; NP_004204.3.
DR UCSC; uc002blf.5; human. [O00337-1]
DR CTD; 9154; -.
DR DisGeNET; 9154; -.
DR GeneCards; SLC28A1; -.
DR HGNC; HGNC:11001; SLC28A1.
DR HPA; ENSG00000156222; Group enriched (intestine, kidney, liver).
DR MalaCards; SLC28A1; -.
DR MIM; 606207; gene.
DR MIM; 618477; phenotype.
DR neXtProt; NX_O00337; -.
DR OpenTargets; ENSG00000156222; -.
DR PharmGKB; PA387; -.
DR VEuPathDB; HostDB:ENSG00000156222; -.
DR eggNOG; KOG3747; Eukaryota.
DR GeneTree; ENSGT00390000016025; -.
DR HOGENOM; CLU_1532017_0_0_1; -.
DR InParanoid; O00337; -.
DR OMA; IVWHTVI; -.
DR OrthoDB; 471043at2759; -.
DR PhylomeDB; O00337; -.
DR TreeFam; TF314131; -.
DR PathwayCommons; O00337; -.
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR SignaLink; O00337; -.
DR BioGRID-ORCS; 9154; 15 hits in 1061 CRISPR screens.
DR ChiTaRS; SLC28A1; human.
DR GeneWiki; Concentrative_nucleoside_transporter_1; -.
DR GenomeRNAi; 9154; -.
DR Pharos; O00337; Tbio.
DR PRO; PR:O00337; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O00337; protein.
DR Bgee; ENSG00000156222; Expressed in right lobe of liver and 73 other tissues.
DR ExpressionAtlas; O00337; baseline and differential.
DR Genevisible; O00337; HS.
DR GO; GO:0031526; C:brush border membrane; ISS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:1901474; F:azole transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005415; F:nucleoside:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; NAS:ARUK-UCL.
DR GO; GO:0015389; F:pyrimidine- and adenine-specific:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0045117; P:azole transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015861; P:cytidine transport; IDA:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:1901642; P:nucleoside transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015858; P:nucleoside transport; TAS:ProtInc.
DR GO; GO:1904823; P:purine nucleobase transmembrane transport; NAS:ARUK-UCL.
DR GO; GO:0015855; P:pyrimidine nucleobase transport; IBA:GO_Central.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015862; P:uridine transport; IDA:UniProtKB.
DR InterPro; IPR008276; C_nuclsd_transpt.
DR InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR InterPro; IPR030212; CNT1/CNT2.
DR InterPro; IPR011657; CNT_C_dom.
DR InterPro; IPR002668; CNT_N_dom.
DR InterPro; IPR011642; Gate_dom.
DR PANTHER; PTHR10590; PTHR10590; 1.
DR PANTHER; PTHR10590:SF16; PTHR10590:SF16; 1.
DR Pfam; PF07670; Gate; 1.
DR Pfam; PF07662; Nucleos_tra2_C; 1.
DR Pfam; PF01773; Nucleos_tra2_N; 1.
DR TIGRFAMs; TIGR00804; nupC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..649
FT /note="Sodium/nucleoside cotransporter 1"
FT /id="PRO_0000070446"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 155..175
FT /note="GLALAAFLGLVLWLSLDTSQR -> DPRPWSKEGPNQYLPQITWTV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037221"
FT VAR_SEQ 176..649
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037222"
FT VARIANT 34
FT /note="E -> G (in allele A)"
FT /evidence="ECO:0000269|PubMed:9124315, ECO:0000269|Ref.2"
FT /id="VAR_009499"
FT VARIANT 140
FT /note="L -> LV (in allele A)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9124315"
FT /id="VAR_009500"
FT VARIANT 189
FT /note="V -> I (in allele A; dbSNP:rs2290272)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9124315"
FT /id="VAR_009501"
FT VARIANT 190
FT /note="A -> S (in dbSNP:rs45523532)"
FT /id="VAR_057194"
FT VARIANT 237
FT /note="Q -> K (in dbSNP:rs8187758)"
FT /id="VAR_057195"
FT VARIANT 409
FT /note="N -> S (in allele B; dbSNP:rs1174011667)"
FT /evidence="ECO:0000269|PubMed:9124315"
FT /id="VAR_009502"
FT VARIANT 510
FT /note="R -> C (in URCTU; affects urinary excretion of
FT uridine and cytidine; decreased sodium-dependent transport
FT of cytidine; increased protein degradation; decreased
FT localization to the cell membrane; dbSNP:rs2242047)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:30658162"
FT /id="VAR_057196"
FT VARIANT 521
FT /note="D -> N (in alleles B and C; dbSNP:rs2242046)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9124315"
FT /id="VAR_009503"
FT VARIANT 546
FT /note="S -> P (in URCTU; affects urinary excretion of
FT uridine and cytidine; unable to mediate sodium-dependent
FT transport of uridine, cytidine and thymidine; no effect on
FT localization to the cell membrane; dbSNP:rs45584739)"
FT /evidence="ECO:0000269|PubMed:21998139,
FT ECO:0000269|PubMed:30847922"
FT /id="VAR_061802"
FT VARIANT 561
FT /note="R -> Q (in URCTU; affects urinary excretion of
FT uridine and cytidine; decreased sodium-dependent transport
FT of cytidine; increased protein degradation; decreased
FT localization to the cell membrane)"
FT /evidence="ECO:0000269|PubMed:30658162"
FT /id="VAR_082636"
FT MUTAGEN 318
FT /note="S->G: Enables transport of purine nucleosides."
FT /evidence="ECO:0000269|PubMed:10455109"
FT MUTAGEN 319
FT /note="Q->M: Increases transport of purine nucleosides;
FT when associated with Gly-319."
FT /evidence="ECO:0000269|PubMed:10455109"
FT MUTAGEN 352
FT /note="S->T: Produces a full purine-type transporter; when
FT associated with Gly-319 and Met-320."
FT /evidence="ECO:0000269|PubMed:10455109"
FT MUTAGEN 546
FT /note="S->A,C,R,T: Unable to mediate sodium-dependent
FT transport of uridine."
FT /evidence="ECO:0000269|PubMed:21998139"
FT MUTAGEN 546
FT /note="Missing: Unable to mediate sodium-dependent
FT transport of uridine."
FT /evidence="ECO:0000269|PubMed:21998139"
SQ SEQUENCE 649 AA; 71584 MW; 42E952443B46B102 CRC64;
MENDPSRRRE SISLTPVAKG LENMGADFLE SLEEGQLPRS DLSPAEIRSS WSEAAPKPFS
RWRNLQPALR ARSFCREHMQ LFRWIGTGLL CTGLSAFLLV ACLLDFQRAL ALFVLTCVVL
TFLGHRLLKR LLGPKLRRFL KPQGHPRLLL WFKRGLALAA FLGLVLWLSL DTSQRPEQLV
SFAGICVFVA LLFACSKHHC AVSWRAVSWG LGLQFVLGLL VIRTEPGFIA FEWLGEQIRI
FLSYTKAGSS FVFGEALVKD VFAFQVLPII VFFSCVISVL YHVGLMQWVI LKIAWLMQVT
MGTTATETLS VAGNIFVSQT EAPLLIRPYL ADMTLSEVHV VMTGGYATIA GSLLGAYISF
GIDATSLIAA SVMAAPCALA LSKLVYPEVE ESKFRREEGV KLTYGDAQNL IEAASTGAAI
SVKVVANIAA NLIAFLAVLD FINAALSWLG DMVDIQGLSF QLICSYILRP VAFLMGVAWE
DCPVVAELLG IKLFLNEFVA YQDLSKYKQR RLAGAEEWVG DRKQWISVRA EVLTTFALCG
FANFSSIGIM LGGLTSMVPQ RKSDFSQIVL RALFTGACVS LVNACMAGIL YMPRGAEVDC
MSLLNTTLSS SSFEIYQCCR EAFQSVNPEF SPEALDNCCR FYNHTICAQ
