ID   S6A14_HUMAN             Reviewed;         642 AA.
AC   Q9UN76; Q5H942;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) {ECO:0000305};
DE   AltName: Full=Amino acid transporter ATB0+;
DE   AltName: Full=Solute carrier family 6 member 14;
GN   Name=SLC6A14 {ECO:0000312|HGNC:HGNC:11047};
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], FUNCTION, TISSUE SPECIFICITY, AND TRASNPORTER
RP   ACTIVITY.
RC   TISSUE=Mammary gland;
RX   PubMed=10446133; DOI=10.1074/jbc.274.34.23740;
RA   Sloan J.L., Mager S.;
RT   "Cloning and functional expression of a human Na(+) and Cl(-)-dependent
RT   neutral and cationic amino acid transporter B(0+).";
RL   J. Biol. Chem. 274:23740-23745(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17855766; DOI=10.1152/ajpgi.00233.2007;
RA   Srinivas S.R., Prasad P.D., Umapathy N.S., Ganapathy V., Shekhawat P.S.;
RT   "Transport of butyryl-L-carnitine, a potential prodrug, via the carnitine
RT   transporter OCTN2 and the amino acid transporter ATB(0,+).";
RL   Am. J. Physiol. 293:G1046-G1053(2007).
RN   [5]
RP   FUNCTION, AND TRANSPORTER ACITVITY.
RX   PubMed=18599538; DOI=10.1113/jphysiol.2008.154500;
RA   Anderson C.M., Ganapathy V., Thwaites D.T.;
RT   "Human solute carrier SLC6A14 is the beta-alanine carrier.";
RL   J. Physiol. (Lond.) 586:4061-4067(2008).
RN   [6]
RP   POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO OBESITY.
RX   PubMed=14660737; DOI=10.1172/jci20448;
RA   Tiwari H.K., Allison D.B.;
RT   "Do allelic variants of SLC6A14 predispose to obesity?";
RL   J. Clin. Invest. 112:1633-1636(2003).
RN   [7]
RP   POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO OBESITY.
RX   PubMed=14660752; DOI=10.1172/jci17491;
RA   Suviolahti E., Oksanen L.J., Oehman M., Cantor R.M., Ridderstrale M.,
RA   Tuomi T., Kaprio J., Rissanen A., Mustajoki P., Jousilahti P.,
RA   Vartiainen E., Silander K., Kilpikari R., Salomaa V., Groop L., Kontula K.,
RA   Peltonen L., Pajukanta P.;
RT   "The SLC6A14 gene shows evidence of association with obesity.";
RL   J. Clin. Invest. 112:1762-1772(2003).
CC   -!- FUNCTION: Amino acid transporter that plays an important role in the
CC       absorption of amino acids in the intestinal tract. Mediates the uptake
CC       of a broad range of neutral and cationic amino acids (with the
CC       exception of proline) in a Na(+)/Cl(-)-dependent manner
CC       (PubMed:10446133). Transports non-alpha-amino acids such as beta-
CC       alanine with low affinity, and has a higher affinity for dipolar and
CC       cationic amino acids such as leucine and lysine (PubMed:18599538). Can
CC       also transport carnitine, butirylcarnitine and propionylcarnitine
CC       coupled to the transmembrane gradients of Na(+) and Cl(-)
CC       (PubMed:17855766). {ECO:0000250|UniProtKB:Q9JMA9,
CC       ECO:0000269|PubMed:10446133, ECO:0000269|PubMed:17855766,
CC       ECO:0000269|PubMed:18599538}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) +
CC         glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:10446133, ECO:0000269|PubMed:17855766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-leucine(out) + 2 Na(+)(out) = chloride(in) +
CC         L-leucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71279, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000269|PubMed:10446133, ECO:0000269|PubMed:18599538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-glutamine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-glutamine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71283,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-arginine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-arginine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71287,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:32682;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine(out) + chloride(out) + 2 Na(+)(out) = (R)-
CC         carnitine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71291,
CC         ChEBI:CHEBI:16347, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:17855766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + 2 Na(+)(out) + O-butanoyl-(R)-carnitine(out) =
CC         chloride(in) + 2 Na(+)(in) + O-butanoyl-(R)-carnitine(in);
CC         Xref=Rhea:RHEA:72163, ChEBI:CHEBI:17996, ChEBI:CHEBI:21949,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000305|PubMed:17855766};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + 2 Na(+)(out) + O-propanoyl-(R)-carnitine(out)
CC         = chloride(in) + 2 Na(+)(in) + O-propanoyl-(R)-carnitine(in);
CC         Xref=Rhea:RHEA:71295, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:53210; Evidence={ECO:0000250|UniProtKB:Q9JMA9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-isoleucine(out) + 2 Na(+)(out) =
CC         chloride(in) + L-isoleucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71299,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-methionine(out) + 2 Na(+)(out) =
CC         chloride(in) + L-methionine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71303,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-valine(out) + 2 Na(+)(out) = chloride(in) +
CC         L-valine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71307, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57762;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-alanine(out) + 2 Na(+)(out) = chloride(in) +
CC         L-alanine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71311, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-serine(out) + 2 Na(+)(out) = chloride(in) +
CC         L-serine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71315, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-cysteine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-cysteine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71319,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-asparagine(out) + 2 Na(+)(out) =
CC         chloride(in) + L-asparagine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71323,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-threonine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-threonine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71327,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-phenylalanine(out) + 2 Na(+)(out) =
CC         chloride(in) + L-phenylalanine(in) + 2 Na(+)(in);
CC         Xref=Rhea:RHEA:71331, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-tryptophan(out) + 2 Na(+)(out) =
CC         chloride(in) + L-tryptophan(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71335,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57912;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-tyrosine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-tyrosine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71339,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58315;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-histidine(out) + 2 Na(+)(out) = chloride(in)
CC         + L-histidine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71343,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595;
CC         Evidence={ECO:0000269|PubMed:10446133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + L-lysine(out) + 2 Na(+)(out) = chloride(in) +
CC         L-lysine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71347, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:32551;
CC         Evidence={ECO:0000269|PubMed:10446133, ECO:0000269|PubMed:18599538};
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:18599538};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.32 mM for glycine {ECO:0000269|PubMed:17855766};
CC         KM=1.5 mM for Na(+) {ECO:0000269|PubMed:17855766};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10446133}; Multi-
CC       pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q9JMA9}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Levels are highest in adult and fetal lung, in
CC       trachea and salivary gland. Lower levels detected in mammary gland,
CC       stomach and pituitary gland, and very low levels in colon, uterus,
CC       prostate and testis. {ECO:0000269|PubMed:10446133}.
CC   -!- DISEASE: Note=Genetic variations in SLC6A14 may be associated with
CC       obesity in some populations, as shown by significant differences in
CC       allele frequencies between obese and non-obese individuals.
CC       {ECO:0000269|PubMed:14660737, ECO:0000269|PubMed:14660752}.
CC   -!- MISCELLANEOUS: Transport inhibited by BCH (2-aminobicyclo-[2.2.1]-
CC       heptane-2-carboxylic acid).
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A14 subfamily. {ECO:0000305}.
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DR   EMBL; AF151978; AAD49223.1; -; mRNA.
DR   EMBL; Z96810; CAI42799.1; -; Genomic_DNA.
DR   EMBL; AL034411; CAI42799.1; JOINED; Genomic_DNA.
DR   EMBL; AL034411; CAI43081.1; -; Genomic_DNA.
DR   EMBL; Z96810; CAI43081.1; JOINED; Genomic_DNA.
DR   EMBL; BC093710; AAH93710.1; -; mRNA.
DR   EMBL; BC093712; AAH93712.1; -; mRNA.
DR   CCDS; CCDS14570.1; -.
DR   RefSeq; NP_009162.1; NM_007231.4.
DR   AlphaFoldDB; Q9UN76; -.
DR   SMR; Q9UN76; -.
DR   BioGRID; 116415; 3.
DR   STRING; 9606.ENSP00000470801; -.
DR   BindingDB; Q9UN76; -.
DR   ChEMBL; CHEMBL4680044; -.
DR   DrugBank; DB03929; D-Serine.
DR   DrugBank; DB00130; L-Glutamine.
DR   DrugBank; DB00172; Proline.
DR   DrugBank; DB00577; Valaciclovir.
DR   DrugBank; DB01610; Valganciclovir.
DR   GuidetoPHARMACOLOGY; 937; -.
DR   TCDB; 2.A.22.2.3; the neurotransmitter:sodium symporter (nss) family.
DR   GlyConnect; 1751; 3 N-Linked glycans (3 sites).
DR   GlyCosmos; Q9UN76; 8 sites, 3 glycans.
DR   GlyGen; Q9UN76; 8 sites, 3 N-linked glycans (3 sites).
DR   iPTMnet; Q9UN76; -.
DR   PhosphoSitePlus; Q9UN76; -.
DR   BioMuta; SLC6A14; -.
DR   DMDM; 41018156; -.
DR   EPD; Q9UN76; -.
DR   jPOST; Q9UN76; -.
DR   MassIVE; Q9UN76; -.
DR   MaxQB; Q9UN76; -.
DR   PaxDb; 9606-ENSP00000470801; -.
DR   PeptideAtlas; Q9UN76; -.
DR   ProteomicsDB; 85268; -.
DR   Pumba; Q9UN76; -.
DR   Antibodypedia; 73032; 143 antibodies from 23 providers.
DR   DNASU; 11254; -.
DR   Ensembl; ENST00000598581.3; ENSP00000470801.1; ENSG00000268104.3.
DR   GeneID; 11254; -.
DR   KEGG; hsa:11254; -.
DR   MANE-Select; ENST00000598581.3; ENSP00000470801.1; NM_007231.5; NP_009162.1.
DR   UCSC; uc033eru.2; human.
DR   AGR; HGNC:11047; -.
DR   CTD; 11254; -.
DR   DisGeNET; 11254; -.
DR   GeneCards; SLC6A14; -.
DR   HGNC; HGNC:11047; SLC6A14.
DR   HPA; ENSG00000268104; Tissue enhanced (lung, salivary gland).
DR   MalaCards; SLC6A14; -.
DR   MIM; 300444; gene.
DR   neXtProt; NX_Q9UN76; -.
DR   OpenTargets; ENSG00000268104; -.
DR   Orphanet; 586; Cystic fibrosis.
DR   PharmGKB; PA35910; -.
DR   VEuPathDB; HostDB:ENSG00000268104; -.
DR   eggNOG; KOG3660; Eukaryota.
DR   GeneTree; ENSGT00940000154963; -.
DR   HOGENOM; CLU_006855_4_1_1; -.
DR   InParanoid; Q9UN76; -.
DR   OMA; VPSEQYW; -.
DR   OrthoDB; 3084493at2759; -.
DR   PhylomeDB; Q9UN76; -.
DR   TreeFam; TF343812; -.
DR   PathwayCommons; Q9UN76; -.
DR   Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   Reactome; R-HSA-5619094; Variant SLC6A14 may confer susceptibility towards obesity.
DR   BioGRID-ORCS; 11254; 23 hits in 782 CRISPR screens.
DR   ChiTaRS; SLC6A14; human.
DR   GeneWiki; SLC6A14; -.
DR   GenomeRNAi; 11254; -.
DR   Pharos; Q9UN76; Tchem.
DR   PRO; PR:Q9UN76; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UN76; Protein.
DR   Bgee; ENSG00000268104; Expressed in palpebral conjunctiva and 110 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR   GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0022858; F:alanine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0001761; F:beta-alanine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015657; F:branched-chain amino acid:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015193; F:L-proline transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015374; F:neutral, basic amino acid:sodium:chloride symporter activity; IDA:UniProtKB.
DR   GO; GO:1902270; P:(R)-carnitine transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0032328; P:alanine transport; IDA:ARUK-UCL.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; TAS:GO_Central.
DR   GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR   GO; GO:0001762; P:beta-alanine transport; IDA:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   CDD; cd11501; SLC6sbd_ATB0; 1.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR037272; SNS_sf.
DR   PANTHER; PTHR11616:SF286; SODIUM- AND CHLORIDE-DEPENDENT NEUTRAL AND BASIC AMINO ACID TRANSPORTER B(0+); 1.
DR   PANTHER; PTHR11616; SODIUM/CHLORIDE DEPENDENT TRANSPORTER; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   SUPFAM; SSF161070; SNF-like; 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.
DR   Genevisible; Q9UN76; HS.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Glycoprotein; Membrane; Obesity;
KW   Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..642
FT                   /note="Sodium- and chloride-dependent neutral and basic
FT                   amino acid transporter B(0+)"
FT                   /id="PRO_0000214795"
FT   TOPO_DOM        1..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..477
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        584..642
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          622..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   642 AA;  72153 MW;  E0FCDD5F173128C0 CRC64;
     MDKLKCPSFF KCREKEKVSA SSENFHVGEN DENQDRGNWS KKSDYLLSMI GYAVGLGNVW
     RFPYLTYSNG GGAFLIPYAI MLALAGLPLF FLECSLGQFA SLGPVSVWRI LPLFQGVGIT
     MVLISIFVTI YYNVIIAYSL YYMFASFQSE LPWKNCSSWS DKNCSRSPIV THCNVSTVNK
     GIQEIIQMNK SWVDINNFTC INGSEIYQPG QLPSEQYWNK VALQRSSGMN ETGVIVWYLA
     LCLLLAWLIV GAALFKGIKS SGKVVYFTAL FPYVVLLILL VRGATLEGAS KGISYYIGAQ
     SNFTKLKEAE VWKDAATQIF YSLSVAWGGL VALSSYNKFK NNCFSDAIVV CLTNCLTSVF
     AGFAIFSILG HMAHISGKEV SQVVKSGFDL AFIAYPEALA QLPGGPFWSI LFFFMLLTLG
     LDSQFASIET ITTTIQDLFP KVMKKMRVPI TLGCCLVLFL LGLVCVTQAG IYWVHLIDHF
     CAGWGILIAA ILELVGIIWI YGGNRFIEDT EMMIGAKRWI FWLWWRACWF VITPILLIAI
     FIWSLVQFHR PNYGAIPYPD WGVALGWCMI VFCIIWIPIM AIIKIIQAKG NIFQRLISCC
     RPASNWGPYL EQHRGERYKD MVDPKKEADH EIPTVSGSRK PE
//