S6A14_HUMAN
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 03-AUG-2022, entry version 168.
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, 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 [5]
RP POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO OBESITY.
RX PubMed=14660737; DOI=10.1172/jci200320448;
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 [6]
RP POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO OBESITY.
RX PubMed=14660752; DOI=10.1172/jci200317491;
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 and propionylcarnitine coupled to the
CC transmembrane gradients of Na(+) and Cl(-) (By similarity).
CC {ECO:0000250|UniProtKB:Q9JMA9, ECO:0000269|PubMed:10446133,
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};
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:0000250|UniProtKB:Q9JMA9};
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 -!- 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) (TC
CC 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; 2.
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 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; Q9UN76; -.
DR PeptideAtlas; Q9UN76; -.
DR PRIDE; Q9UN76; -.
DR ProteomicsDB; 85268; -.
DR Antibodypedia; 73032; 122 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 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; AQHNGVQ; -.
DR OrthoDB; 250396at2759; -.
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; 17 hits in 695 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 108 other tissues.
DR Genevisible; Q9UN76; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA: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:0015293; F:symporter activity; IEA:UniProtKB-KW.
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:0003333; P:amino acid transmembrane transport; TAS:GO_Central.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
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 2: Evidence at transcript 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
