S29A4_HUMAN
ID S29A4_HUMAN Reviewed; 530 AA.
AC Q7RTT9; Q6PJ08; Q86WY8; Q8NAR3; Q8NBM2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Equilibrative nucleoside transporter 4;
DE Short=hENT4;
DE AltName: Full=Plasma membrane monoamine transporter;
DE AltName: Full=Solute carrier family 29 member 4;
GN Name=SLC29A4; Synonyms=ENT4, PMAT; ORFNames=PSEC0113;
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, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=15448143; DOI=10.1074/jbc.m407913200;
RA Engel K., Zhou M., Wang J.;
RT "Identification and characterization of a novel monoamine transporter in
RT the human brain.";
RL J. Biol. Chem. 279:50042-50049(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP GLU-79; LYS-124 AND THR-429.
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION.
RX PubMed=12446811; DOI=10.1093/oxfordjournals.molbev.a004044;
RA Acimovic Y., Coe I.R.;
RT "Molecular evolution of the equilibrative nucleoside transporter family:
RT identification of novel family members in prokaryotes and eukaryotes.";
RL Mol. Biol. Evol. 19:2199-2210(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT
RP ASN-523, AND MUTAGENESIS OF GLU-206 AND GLU-375.
RX PubMed=16873718; DOI=10.1161/01.res.0000238359.18495.42;
RA Barnes K., Dobrzynski H., Foppolo S., Beal P.R., Ismat F., Scullion E.R.,
RA Sun L., Tellez J., Ritzel M.W., Claycomb W.C., Cass C.E., Young J.D.,
RA Billeter-Clark R., Boyett M.R., Baldwin S.A.;
RT "Distribution and functional characterization of equilibrative nucleoside
RT transporter-4, a novel cardiac adenosine transporter activated at acidic
RT pH.";
RL Circ. Res. 99:510-519(2006).
RN [7]
RP FUNCTION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=17018840; DOI=10.1152/ajprenal.00302.2006;
RA Xia L., Engel K., Zhou M., Wang J.;
RT "Membrane localization and pH-dependent transport of a newly cloned organic
RT cation transporter (PMAT) in kidney cells.";
RL Am. J. Physiol. 292:F682-F690(2007).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-91; ASP-107; GLU-128; ASP-154; ASP-163;
RP GLU-206; THR-220; GLU-227; GLU-242; TRP-336 AND GLU-375.
RX PubMed=17121826; DOI=10.1074/jbc.m609421200;
RA Zhou M., Xia L., Engel K., Wang J.;
RT "Molecular determinants of substrate selectivity of a novel organic cation
RT transporter (PMAT) in the SLC29 family.";
RL J. Biol. Chem. 282:3188-3195(2007).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17393420; DOI=10.1002/mrd.20697;
RA Bottalico B., Noskova V., Pilka R., Larsson I., Domanski H., Casslen B.,
RA Hansson S.R.;
RT "The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane
RT monoamine transporter (PMAT) show differential distribution and cyclic
RT expression pattern in human endometrium and early pregnancy decidua.";
RL Mol. Reprod. Dev. 74:1303-1311(2007).
CC -!- FUNCTION: Functions as a polyspecific organic cation transporter,
CC efficiently transporting many organic cations such as monoamine
CC neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines
CC including serotonin, dopamine, norepinephrine and epinephrine. May play
CC a role in regulating central nervous system homeostasis of monoamine
CC neurotransmitters. May be involved in luminal transport of organic
CC cations in the kidney and seems to use luminal proton gradient to drive
CC organic cation reabsorption. Does not seem to transport nucleoside and
CC nucleoside analogs such as uridine, cytidine, thymidine, adenosine,
CC inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine
CC is efficiently transported but in a fashion highly sensitive to
CC extracellular pH, with maximal activity in the pH range 5.5 to 6.5.
CC Glu-206 is essential for the cation selectivity and may function as the
CC charge sensor for cationic substrates. Transport is chloride and
CC sodium-independent but appears to be sensitive to changes in membrane
CC potential. Weakly inhibited by the classical inhibitors of
CC equilibrative nucleoside transport, dipyridamole, dilazep, and
CC nitrobenzylthioinosine. May play a role in the regulation of
CC extracellular adenosine concentrations in cardiac tissues, in
CC particular during ischemia. {ECO:0000269|PubMed:15448143,
CC ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17018840,
CC ECO:0000269|PubMed:17121826}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Apical cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Located to the plasma membranes of
CC ventricular myocytes and vascular endothelial cells. Targeted to the
CC apical membranes of differentiated kidney epithelial cells.
CC {ECO:0000269|PubMed:15448143, ECO:0000269|PubMed:16873718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7RTT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7RTT9-2; Sequence=VSP_032647;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the heart, in both
CC cardiomyocytes and vascular endothelial cells (at protein level).
CC Highly expressed in brain, kidney and skeletal muscle. In the brain
CC expressed in cerebellum, cerebral cortex, medulla, occipital pole,
CC frontal and temporal lobes putamen and in the spinal cord. Lower
CC expression in liver, pancreas, and liver. Expressed in endometrial
CC tissue, exclusively in the stroma. Expression is high in the
CC proliferative phase, decreases during the secretory phase, and is no
CC longer detectable in the menstrual phase. {ECO:0000269|PubMed:15448143,
CC ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17018840,
CC ECO:0000269|PubMed:17393420}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16873718}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11612.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY485959; AAS65965.1; -; mRNA.
DR EMBL; AK075422; BAC11612.1; ALT_INIT; mRNA.
DR EMBL; AK092242; BAC03836.1; -; mRNA.
DR EMBL; CH471144; EAW87329.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87330.1; -; Genomic_DNA.
DR EMBL; BC025325; AAH25325.1; -; mRNA.
DR EMBL; BC047592; AAH47592.1; -; mRNA.
DR EMBL; BK000627; DAA00308.1; -; Genomic_DNA.
DR CCDS; CCDS5340.1; -. [Q7RTT9-1]
DR CCDS; CCDS75561.1; -. [Q7RTT9-2]
DR RefSeq; NP_001035751.1; NM_001040661.1. [Q7RTT9-1]
DR RefSeq; NP_001287776.1; NM_001300847.1. [Q7RTT9-2]
DR RefSeq; NP_694979.2; NM_153247.2. [Q7RTT9-1]
DR RefSeq; XP_005249715.1; XM_005249658.4. [Q7RTT9-2]
DR RefSeq; XP_006715730.1; XM_006715667.3. [Q7RTT9-1]
DR RefSeq; XP_011513502.1; XM_011515200.2. [Q7RTT9-1]
DR RefSeq; XP_011513503.1; XM_011515201.2. [Q7RTT9-1]
DR AlphaFoldDB; Q7RTT9; -.
DR SMR; Q7RTT9; -.
DR BioGRID; 128822; 2.
DR IntAct; Q7RTT9; 1.
DR STRING; 9606.ENSP00000380081; -.
DR ChEMBL; CHEMBL3509593; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB00331; Metformin.
DR DrugBank; DB01104; Sertraline.
DR DrugCentral; Q7RTT9; -.
DR GuidetoPHARMACOLOGY; 1120; -.
DR TCDB; 2.A.57.1.5; the equilibrative nucleoside transporter (ent) family.
DR GlyGen; Q7RTT9; 1 site.
DR iPTMnet; Q7RTT9; -.
DR PhosphoSitePlus; Q7RTT9; -.
DR BioMuta; SLC29A4; -.
DR DMDM; 74713147; -.
DR MassIVE; Q7RTT9; -.
DR PaxDb; Q7RTT9; -.
DR PeptideAtlas; Q7RTT9; -.
DR PRIDE; Q7RTT9; -.
DR ProteomicsDB; 68902; -. [Q7RTT9-1]
DR ProteomicsDB; 68903; -. [Q7RTT9-2]
DR Antibodypedia; 24590; 258 antibodies from 25 providers.
DR DNASU; 222962; -.
DR Ensembl; ENST00000297195.8; ENSP00000297195.4; ENSG00000164638.11. [Q7RTT9-1]
DR Ensembl; ENST00000396872.8; ENSP00000380081.2; ENSG00000164638.11. [Q7RTT9-1]
DR Ensembl; ENST00000406453.3; ENSP00000385845.3; ENSG00000164638.11. [Q7RTT9-2]
DR GeneID; 222962; -.
DR KEGG; hsa:222962; -.
DR MANE-Select; ENST00000396872.8; ENSP00000380081.2; NM_153247.4; NP_694979.2.
DR UCSC; uc003soc.4; human. [Q7RTT9-1]
DR CTD; 222962; -.
DR DisGeNET; 222962; -.
DR GeneCards; SLC29A4; -.
DR HGNC; HGNC:23097; SLC29A4.
DR HPA; ENSG00000164638; Tissue enhanced (adipose tissue, choroid plexus).
DR MIM; 609149; gene.
DR neXtProt; NX_Q7RTT9; -.
DR OpenTargets; ENSG00000164638; -.
DR PharmGKB; PA134976472; -.
DR VEuPathDB; HostDB:ENSG00000164638; -.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_4_0_1; -.
DR InParanoid; Q7RTT9; -.
DR OMA; FDMSVVY; -.
DR OrthoDB; 674800at2759; -.
DR PhylomeDB; Q7RTT9; -.
DR TreeFam; TF313950; -.
DR PathwayCommons; Q7RTT9; -.
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR SignaLink; Q7RTT9; -.
DR BioGRID-ORCS; 222962; 26 hits in 1068 CRISPR screens.
DR ChiTaRS; SLC29A4; human.
DR GeneWiki; SLC29A4; -.
DR GenomeRNAi; 222962; -.
DR Pharos; Q7RTT9; Tchem.
DR PRO; PR:Q7RTT9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7RTT9; protein.
DR Bgee; ENSG00000164638; Expressed in buccal mucosa cell and 131 other tissues.
DR ExpressionAtlas; Q7RTT9; baseline and differential.
DR Genevisible; Q7RTT9; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008324; F:cation transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0005342; F:organic acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0098655; P:cation transmembrane transport; ISS:ARUK-UCL.
DR GO; GO:0090494; P:dopamine uptake; IDA:ARUK-UCL.
DR GO; GO:0051625; P:epinephrine uptake; IDA:ARUK-UCL.
DR GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0001692; P:histamine metabolic process; TAS:ARUK-UCL.
DR GO; GO:0051615; P:histamine uptake; IDA:ARUK-UCL.
DR GO; GO:0015844; P:monoamine transport; IMP:ARUK-UCL.
DR GO; GO:0006836; P:neurotransmitter transport; IDA:ARUK-UCL.
DR GO; GO:0051620; P:norepinephrine uptake; IDA:ARUK-UCL.
DR GO; GO:1903825; P:organic acid transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015695; P:organic cation transport; IDA:ARUK-UCL.
DR GO; GO:0051610; P:serotonin uptake; IDA:ARUK-UCL.
DR GO; GO:1901998; P:toxin transport; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0042908; P:xenobiotic transport; IDA:ARUK-UCL.
DR InterPro; IPR030198; ENT4.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR PANTHER; PTHR10332:SF4; PTHR10332:SF4; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Equilibrative nucleoside transporter 4"
FT /id="PRO_0000326251"
FT TOPO_DOM 1..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..450
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 139..182
FT /note="GYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTV -> ASAT
FT CGCSSSLGTRPTPSTWPLWAPWPSAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032647"
FT VARIANT 79
FT /note="V -> E (in dbSNP:rs17854505)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_040044"
FT VARIANT 124
FT /note="N -> K (in dbSNP:rs17855675)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_040045"
FT VARIANT 429
FT /note="P -> T (in dbSNP:rs17857336)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_040046"
FT MUTAGEN 91
FT /note="D->A: No significant change in cationic transport
FT activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 107
FT /note="D->A: Loss of cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 128
FT /note="E->A: No significant change in cationic transport
FT activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 154
FT /note="D->A: Loss of cationic transport activity; increase
FT in uridine uptake."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 163
FT /note="D->A: Loss of cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 206
FT /note="E->A: Loss of cationic transport activity."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT MUTAGEN 206
FT /note="E->D: No loss of cationic transporter activity; no
FT activity towards uridine."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT MUTAGEN 206
FT /note="E->Q: Loss of cationic transporter activity;
FT increase in uridine uptake."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT MUTAGEN 206
FT /note="E->R: Loss of cationic transporter activity."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT MUTAGEN 220
FT /note="T->A: Reduced cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 220
FT /note="T->I: Loss of cationic transporter activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 220
FT /note="T->S: Reduced cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 227
FT /note="E->A: Functional with slight increased cationic
FT transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 242
FT /note="E->A: Reduced cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 336
FT /note="W->A: Loss of cationic transport activity."
FT /evidence="ECO:0000269|PubMed:17121826"
FT MUTAGEN 375
FT /note="E->A: Functional with slight increased cationic
FT transport activity."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT MUTAGEN 375
FT /note="E->Q: No change in cationic activity and pH
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:16873718,
FT ECO:0000269|PubMed:17121826"
FT CONFLICT 25
FT /note="S -> C (in Ref. 2; BAC03836)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> R (in Ref. 2; BAC03836)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="K -> R (in Ref. 2; BAC03836)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="Y -> H (in Ref. 2; BAC11612)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="L -> P (in Ref. 2; BAC03836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 58059 MW; 3FE5D5ED1D248A13 CRC64;
MGSVGSQRLE EPSVAGTPDP GVVMSFTFDS HQLEEAAEAA QGQGLRARGV PAFTDTTLDE
PVPDDRYHAI YFAMLLAGVG FLLPYNSFIT DVDYLHHKYP GTSIVFDMSL TYILVALAAV
LLNNVLVERL TLHTRITAGY LLALGPLLFI SICDVWLQLF SRDQAYAINL AAVGTVAFGC
TVQQSSFYGY TGMLPKRYTQ GVMTGESTAG VMISLSRILT KLLLPDERAS TLIFFLVSVA
LELLCFLLHL LVRRSRFVLF YTTRPRDSHR GRPGLGRGYG YRVHHDVVAG DVHFEHPAPA
LAPNESPKDS PAHEVTGSGG AYMRFDVPRP RVQRSWPTFR ALLLHRYVVA RVIWADMLSI
AVTYFITLCL FPGLESEIRH CILGEWLPIL IMAVFNLSDF VGKILAALPV DWRGTHLLAC
SCLRVVFIPL FILCVYPSGM PALRHPAWPC IFSLLMGISN GYFGSVPMIL AAGKVSPKQR
ELAGNTMTVS YMSGLTLGSA VAYCTYSLTR DAHGSCLHAS TANGSILAGL
