SC6A6_HUMAN
ID SC6A6_HUMAN Reviewed; 620 AA.
AC P31641; B2RNU7; Q9BRI2; Q9BXB0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Sodium- and chloride-dependent taurine transporter;
DE AltName: Full=Solute carrier family 6 member 6;
GN Name=SLC6A6;
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, TISSUE SPECIFICITY,
RP TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RC TISSUE=Thyroid;
RX PubMed=8382624; DOI=10.1016/0014-5793(93)80008-i;
RA Jhiang S.M., Fithian L., Smanik P., McGill J., Tong Q., Mazzaferri E.L.;
RT "Cloning of the human taurine transporter and characterization of taurine
RT uptake in thyroid cells.";
RL FEBS Lett. 318:139-144(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RC TISSUE=Placenta;
RX PubMed=8010975; DOI=10.1042/bj3000893;
RA Ramamoorthy S., Leibach F.H., Mahesh V.B., Han H., Yang-Feng T.,
RA Blakely R.D., Ganapathy V.;
RT "Functional characterization and chromosomal localization of a cloned
RT taurine transporter from human placenta.";
RL Biochem. J. 300:893-900(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Retinal pigment epithelium;
RX PubMed=8654117; DOI=10.3109/02713689609007631;
RA Miyamoto Y., Liou G.I., Sprinkle T.J.;
RT "Isolation of a cDNA encoding a taurine transporter in the human retinal
RT pigment epithelium.";
RL Curr. Eye Res. 15:345-349(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Brain, and Ovary;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-324.
RA Kim H.W., An H.S., Park T.S., Park K.K.;
RT "Taurine transporter expression in various organs.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190.
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 [9]
RP INVOLVEMENT IN HTRDC, FUNCTION, VARIANT HTRDC GLU-78, CHARACTERIZATION OF
RP VARIANT HTRDC GLU-78, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=31345061; DOI=10.1096/fj.201900914rr;
RA Preising M.N., Goerg B., Friedburg C., Qvartskhava N., Budde B.S.,
RA Bonus M., Toliat M.R., Pfleger C., Altmueller J., Herebian D., Beyer M.,
RA Zoellner H.J., Wittsack H.J., Schaper J., Klee D., Zechner U.,
RA Nuernberg P., Schipper J., Schnitzler A., Gohlke H., Lorenz B.,
RA Haeussinger D., Bolz H.J.;
RT "Biallelic mutation of human SLC6A6 encoding the taurine transporter TAUT
RT is linked to early retinal degeneration.";
RL FASEB J. 33:11507-11527(2019).
RN [10]
RP INVOLVEMENT IN HTRDC, FUNCTION, SUBCELLULAR LOCATION, VARIANT HTRDC
RP VAL-399, CHARACTERIZATION OF VARIANT HTRDC VAL-399, TRANSPORTER ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31903486; DOI=10.1093/hmg/ddz303;
RA Ansar M., Ranza E., Shetty M., Paracha S.A., Azam M., Kern I.,
RA Iwaszkiewicz J., Farooq O., Pournaras C.J., Malcles A., Kecik M.,
RA Rivolta C., Muzaffar W., Qurban A., Ali L., Aggoun Y., Santoni F.A.,
RA Makrythanasis P., Ahmed J., Qamar R., Sarwar M.T., Henry L.K.,
RA Antonarakis S.E.;
RT "Taurine treatment of retinal degeneration and cardiomyopathy in a
RT consanguineous family with SLC6A6 taurine transporter deficiency.";
RL Hum. Mol. Genet. 29:618-623(2020).
CC -!- FUNCTION: Mediates sodium- and chloride-dependent transport of taurine
CC (PubMed:8382624, PubMed:8010975, PubMed:8654117, PubMed:31345061,
CC PubMed:31903486). Mediates transport of beta-alanine (PubMed:8010975).
CC Can also mediate transport of hypotaurine and gamma-aminobutyric acid
CC (GABA) (By similarity). {ECO:0000250|UniProtKB:O35316,
CC ECO:0000269|PubMed:31345061, ECO:0000269|PubMed:31903486,
CC ECO:0000269|PubMed:8010975, ECO:0000269|PubMed:8382624,
CC ECO:0000269|PubMed:8654117}.
CC -!- FUNCTION: Sodium-dependent taurine and beta-alanine transporter.
CC Chloride ions are necessary for optimal uptake.
CC {ECO:0000269|PubMed:31345061, ECO:0000269|PubMed:31903486,
CC ECO:0000269|PubMed:8382624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:O35316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + 2 Na(+)(out) + taurine(out) = chloride(in) + 2
CC Na(+)(in) + taurine(in); Xref=Rhea:RHEA:71223, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:31345061, ECO:0000269|PubMed:31903486,
CC ECO:0000269|PubMed:8010975, ECO:0000269|PubMed:8382624,
CC ECO:0000269|PubMed:8654117};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71224;
CC Evidence={ECO:0000305|PubMed:8382624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(out) + chloride(out) + 2 Na(+)(out) = beta-
CC alanine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71247,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000269|PubMed:8010975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71248;
CC Evidence={ECO:0000305|PubMed:8010975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC -!- ACTIVITY REGULATION: Taurine transport activity is stimulated by
CC thyrotropin (PubMed:8382624). Taurine transport activity is inhibited
CC by GABA, hypotaurine and beta-alanine (PubMed:8010975, PubMed:8654117).
CC {ECO:0000269|PubMed:8010975, ECO:0000269|PubMed:8382624,
CC ECO:0000269|PubMed:8654117}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for taurine {ECO:0000269|PubMed:8010975};
CC KM=2.0 uM for taurine {ECO:0000269|PubMed:8654117};
CC KM=3.8 uM for taurine {ECO:0000269|PubMed:31903486};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31345061,
CC ECO:0000269|PubMed:31903486}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31641-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31641-2; Sequence=VSP_044961;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in placenta and skeletal
CC muscle, at intermediate levels in heart, brain, lung, kidney and
CC pancreas and at low levels in liver. {ECO:0000269|PubMed:8010975,
CC ECO:0000269|PubMed:8382624}.
CC -!- PTM: Taurine transport activity is down-regulated upon Ser-322
CC phosphorylation. {ECO:0000250|UniProtKB:Q00589}.
CC -!- DISEASE: Hypotaurinemic retinal degeneration and cardiomyopathy (HTRDC)
CC [MIM:145350]: An autosomal recessive disorder characterized by low
CC plasma taurine, childhood-onset progressive retinal degeneration, and
CC cardiomyopathy. {ECO:0000269|PubMed:31345061,
CC ECO:0000269|PubMed:31903486}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A6 subfamily. {ECO:0000305}.
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DR EMBL; Z18956; CAA79481.1; -; mRNA.
DR EMBL; U16120; AAA50842.1; -; mRNA.
DR EMBL; U09220; AAC50443.1; -; mRNA.
DR EMBL; AC090941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64192.1; -; Genomic_DNA.
DR EMBL; BC006252; AAH06252.1; -; mRNA.
DR EMBL; BC111489; AAI11490.1; -; mRNA.
DR EMBL; BC137128; AAI37129.1; -; mRNA.
DR EMBL; BC137129; AAI37130.1; -; mRNA.
DR EMBL; AF346763; AAK30132.1; -; mRNA.
DR CCDS; CCDS33705.1; -. [P31641-1]
DR CCDS; CCDS46765.1; -. [P31641-2]
DR PIR; G01426; G01426.
DR PIR; S29839; S29839.
DR PIR; S46487; S46487.
DR RefSeq; NP_001127839.2; NM_001134367.3.
DR RefSeq; NP_001127840.1; NM_001134368.3. [P31641-2]
DR RefSeq; NP_003034.2; NM_003043.5. [P31641-1]
DR RefSeq; XP_011532332.1; XM_011534030.2. [P31641-1]
DR AlphaFoldDB; P31641; -.
DR SMR; P31641; -.
DR BioGRID; 112424; 42.
DR IntAct; P31641; 12.
DR MINT; P31641; -.
DR STRING; 9606.ENSP00000480890; -.
DR BindingDB; P31641; -.
DR ChEMBL; CHEMBL5762; -.
DR DrugBank; DB01956; Taurine.
DR TCDB; 2.A.22.3.3; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; P31641; 3 sites.
DR iPTMnet; P31641; -.
DR PhosphoSitePlus; P31641; -.
DR SwissPalm; P31641; -.
DR BioMuta; SLC6A6; -.
DR DMDM; 1352535; -.
DR EPD; P31641; -.
DR jPOST; P31641; -.
DR MassIVE; P31641; -.
DR MaxQB; P31641; -.
DR PaxDb; P31641; -.
DR PeptideAtlas; P31641; -.
DR PRIDE; P31641; -.
DR ProteomicsDB; 54796; -. [P31641-1]
DR ProteomicsDB; 78766; -.
DR Antibodypedia; 10999; 169 antibodies from 26 providers.
DR DNASU; 6533; -.
DR Ensembl; ENST00000621751.4; ENSP00000482560.1; ENSG00000131389.18. [P31641-2]
DR Ensembl; ENST00000622186.5; ENSP00000480890.1; ENSG00000131389.18. [P31641-1]
DR GeneID; 6533; -.
DR KEGG; hsa:6533; -.
DR MANE-Select; ENST00000622186.5; ENSP00000480890.1; NM_003043.6; NP_003034.2.
DR UCSC; uc032rfd.2; human. [P31641-1]
DR CTD; 6533; -.
DR DisGeNET; 6533; -.
DR GeneCards; SLC6A6; -.
DR HGNC; HGNC:11052; SLC6A6.
DR HPA; ENSG00000131389; Tissue enhanced (bone marrow, retina).
DR MIM; 145350; phenotype.
DR MIM; 186854; gene.
DR neXtProt; NX_P31641; -.
DR OpenTargets; ENSG00000131389; -.
DR PharmGKB; PA35912; -.
DR VEuPathDB; HostDB:ENSG00000131389; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000154583; -.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; P31641; -.
DR OMA; WAHCNHT; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; P31641; -.
DR TreeFam; TF343812; -.
DR PathwayCommons; P31641; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR SignaLink; P31641; -.
DR BioGRID-ORCS; 6533; 15 hits in 1086 CRISPR screens.
DR ChiTaRS; SLC6A6; human.
DR GeneWiki; SLC6A6; -.
DR GenomeRNAi; 6533; -.
DR Pharos; P31641; Tbio.
DR PRO; PR:P31641; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P31641; protein.
DR Bgee; ENSG00000131389; Expressed in mucosa of paranasal sinus and 176 other tissues.
DR ExpressionAtlas; P31641; baseline and differential.
DR Genevisible; P31641; 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:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0031528; C:microvillus membrane; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098797; C:plasma membrane protein complex; ISS:ARUK-UCL.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005368; F:taurine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005369; F:taurine:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0032328; P:alanine transport; IDA:ARUK-UCL.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0051939; P:gamma-aminobutyric acid import; ISS:ARUK-UCL.
DR GO; GO:0098739; P:import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0071705; P:nitrogen compound transport; IDA:ARUK-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IDA:ARUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0015734; P:taurine transport; IDA:UniProtKB.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR CDD; cd11510; SLC6sbd_TauT; 1.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002434; Na/ntran_symport_taurine.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01200; TAUTRANSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cardiomyopathy; Cell membrane; Disease variant;
KW Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Sodium- and chloride-dependent taurine transporter"
FT /id="PRO_0000214767"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..236
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..262
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..315
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..348
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..400
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..448
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..525
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..563
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00589"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 201..620
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044961"
FT VARIANT 17
FT /note="I -> M (in dbSNP:rs1042350)"
FT /id="VAR_011767"
FT VARIANT 18
FT /note="L -> V (in dbSNP:rs1042351)"
FT /id="VAR_011768"
FT VARIANT 78
FT /note="A -> E (in HTRDC; severely decreased taurine
FT transport activity in patient cells; does not affect cell
FT membrane localization)"
FT /evidence="ECO:0000269|PubMed:31345061"
FT /id="VAR_083336"
FT VARIANT 399
FT /note="G -> V (in HTRDC; decreased taurine transport
FT activity; does not affect protein abundance; does not
FT affect cell membrane localization)"
FT /evidence="ECO:0000269|PubMed:31903486"
FT /id="VAR_083337"
FT CONFLICT 28
FT /note="T -> K (in Ref. 2; AAA50842)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> R (in Ref. 1; CAA79481)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="Missing (in Ref. 1; CAA79481)"
FT /evidence="ECO:0000305"
FT CONFLICT 538..540
FT /note="YPN -> SPT (in Ref. 1; CAA79481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 69830 MW; 3CEB22BA46116AD1 CRC64;
MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEAEGKPPQ REKWSSKIDF VLSVAGGFVG
LGNVWRFPYL CYKNGGGAFL IPYFIFLFGS GLPVFFLEII IGQYTSEGGI TCWEKICPLF
SGIGYASVVI VSLLNVYYIV ILAWATYYLF QSFQKELPWA HCNHSWNTPH CMEDTMRKNK
SVWITISSTN FTSPVIEFWE RNVLSLSPGI DHPGSLKWDL ALCLLLVWLV CFFCIWKGVR
STGKVVYFTA TFPFAMLLVL LVRGLTLPGA GAGIKFYLYP DITRLEDPQV WIDAGTQIFF
SYAICLGAMT SLGSYNKYKY NSYRDCMLLG CLNSGTSFVS GFAIFSILGF MAQEQGVDIA
DVAESGPGLA FIAYPKAVTM MPLPTFWSIL FFIMLLLLGL DSQFVEVEGQ ITSLVDLYPS
FLRKGYRREI FIAFVCSISY LLGLTMVTEG GMYVFQLFDY YAASGVCLLW VAFFECFVIA
WIYGGDNLYD GIEDMIGYRP GPWMKYSWAV ITPVLCVGCF IFSLVKYVPL TYNKTYVYPN
WAIGLGWSLA LSSMLCVPLV IVIRLCQTEG PFLVRVKYLL TPREPNRWAV EREGATPYNS
RTVMNGALVK PTHIIVETMM
