S6A15_HUMAN
ID S6A15_HUMAN Reviewed; 730 AA.
AC Q9H2J7; A8K592; B7Z2P7; E7ESJ5; Q9H9F5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT2;
DE AltName: Full=Sodium- and chloride-dependent neurotransmitter transporter NTT73;
DE AltName: Full=Sodium-coupled branched-chain amino-acid transporter 1;
DE AltName: Full=Solute carrier family 6 member 15;
DE AltName: Full=Transporter v7-3;
GN Name=SLC6A15; Synonyms=B0AT2, NTT73, SBAT1;
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).
RC TISSUE=Cerebellum;
RX PubMed=11112352; DOI=10.1006/geno.2000.6387;
RA Farmer M.K., Robbins M.J., Medhurst A.D., Campbell D.A., Ellington K.,
RA Duckworth M., Brown A.M., Middlemiss D.N., Price G.W., Pangalos M.N.;
RT "Cloning and characterization of human NTT5 and v7-3: two orphan
RT transporters of the Na(+)/Cl(-)-dependent neurotransmitter transporter gene
RT family.";
RL Genomics 70:241-252(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP VAL-400.
RC TISSUE=Brain;
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].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 TISSUE SPECIFICITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16226721; DOI=10.1016/j.bbrc.2005.09.128;
RA Takanaga H., Mackenzie B., Peng J.B., Hediger M.A.;
RT "Characterization of a branched-chain amino-acid transporter SBAT1
RT (SLC6A15) that is expressed in human brain.";
RL Biochem. Biophys. Res. Commun. 337:892-900(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-55; SER-687; SER-699
RP AND SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Functions as a sodium-dependent neutral amino acid
CC transporter. Exhibits preference for the branched-chain amino acids,
CC particularly leucine, valine and isoleucine and methionine. Mediates
CC the saturable, pH-sensitive and electrogenic cotransport of proline and
CC sodium ions with a stoichiometry of 1:1. May have a role as transporter
CC for neurotransmitter precursors into neurons. In contrast to other
CC members of the neurotransmitter transporter family, does not appear to
CC be chloride-dependent. {ECO:0000269|PubMed:16226721}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for L-leucine (at pH 7.5, 100 mM NaCL, -70 mV)
CC {ECO:0000269|PubMed:16226721};
CC KM=0.16 mM for L-valine (at pH 7.5, 100 mM NaCL, -70 mV))
CC {ECO:0000269|PubMed:16226721};
CC KM=0.08 mM for L-isoleucine (at pH 7.5, 100 mM NaCL, -70 mV)
CC {ECO:0000269|PubMed:16226721};
CC KM=0.11 mM for L-methionine (at pH 7.5, 100 mM NaCL, -70 mV)
CC {ECO:0000269|PubMed:16226721};
CC KM=0.38 mM for L-proline (at pH 7.5, 100 mM NaCL, -70 mV)
CC {ECO:0000269|PubMed:16226721};
CC pH dependence:
CC Optimum pH is 7.5-8.5. Strongly inhibited at acidic PH.
CC {ECO:0000269|PubMed:16226721};
CC -!- INTERACTION:
CC Q9H2J7; O75084: FZD7; NbExp=3; IntAct=EBI-11343466, EBI-746917;
CC Q9H2J7; Q8IXM6: NRM; NbExp=3; IntAct=EBI-11343466, EBI-10262547;
CC Q9H2J7; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-11343466, EBI-10314552;
CC Q9H2J7; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-11343466, EBI-10290130;
CC Q9H2J7; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-11343466, EBI-2852148;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H2J7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2J7-2; Sequence=VSP_043030, VSP_043031;
CC Name=3;
CC IsoId=Q9H2J7-3; Sequence=VSP_045192;
CC -!- TISSUE SPECIFICITY: Almost exclusively expressed in the brain.
CC {ECO:0000269|PubMed:16226721}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A15 subfamily. {ECO:0000305}.
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DR EMBL; AF265577; AAG41361.1; -; mRNA.
DR EMBL; AK022853; BAB14274.1; -; mRNA.
DR EMBL; AK291207; BAF83896.1; -; mRNA.
DR EMBL; AK294945; BAH11933.1; -; mRNA.
DR EMBL; AC018922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97389.1; -; Genomic_DNA.
DR EMBL; BC070040; AAH70040.1; -; mRNA.
DR CCDS; CCDS53816.1; -. [Q9H2J7-3]
DR CCDS; CCDS9026.1; -. [Q9H2J7-1]
DR CCDS; CCDS9027.1; -. [Q9H2J7-2]
DR RefSeq; NP_001139807.1; NM_001146335.2. [Q9H2J7-3]
DR RefSeq; NP_060527.2; NM_018057.6. [Q9H2J7-2]
DR RefSeq; NP_877499.1; NM_182767.5. [Q9H2J7-1]
DR AlphaFoldDB; Q9H2J7; -.
DR SMR; Q9H2J7; -.
DR BioGRID; 120426; 125.
DR IntAct; Q9H2J7; 49.
DR MINT; Q9H2J7; -.
DR STRING; 9606.ENSP00000266682; -.
DR BindingDB; Q9H2J7; -.
DR ChEMBL; CHEMBL3351189; -.
DR DrugCentral; Q9H2J7; -.
DR GuidetoPHARMACOLOGY; 940; -.
DR TCDB; 2.A.22.6.7; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9H2J7; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2J7; -.
DR PhosphoSitePlus; Q9H2J7; -.
DR BioMuta; SLC6A15; -.
DR DMDM; 18202939; -.
DR EPD; Q9H2J7; -.
DR jPOST; Q9H2J7; -.
DR MassIVE; Q9H2J7; -.
DR MaxQB; Q9H2J7; -.
DR PaxDb; Q9H2J7; -.
DR PeptideAtlas; Q9H2J7; -.
DR PRIDE; Q9H2J7; -.
DR ProteomicsDB; 6449; -.
DR ProteomicsDB; 80556; -. [Q9H2J7-1]
DR ProteomicsDB; 80557; -. [Q9H2J7-2]
DR Antibodypedia; 1932; 158 antibodies from 23 providers.
DR DNASU; 55117; -.
DR Ensembl; ENST00000266682.10; ENSP00000266682.5; ENSG00000072041.18. [Q9H2J7-1]
DR Ensembl; ENST00000450363.4; ENSP00000390706.2; ENSG00000072041.18. [Q9H2J7-2]
DR Ensembl; ENST00000552192.5; ENSP00000450145.1; ENSG00000072041.18. [Q9H2J7-3]
DR Ensembl; ENST00000680963.1; ENSP00000505485.1; ENSG00000072041.18. [Q9H2J7-1]
DR Ensembl; ENST00000681106.1; ENSP00000505789.1; ENSG00000072041.18. [Q9H2J7-1]
DR Ensembl; ENST00000681688.1; ENSP00000505731.1; ENSG00000072041.18. [Q9H2J7-2]
DR Ensembl; ENST00000681721.1; ENSP00000505286.1; ENSG00000072041.18. [Q9H2J7-1]
DR GeneID; 55117; -.
DR KEGG; hsa:55117; -.
DR MANE-Select; ENST00000266682.10; ENSP00000266682.5; NM_182767.6; NP_877499.1.
DR UCSC; uc001szv.5; human. [Q9H2J7-1]
DR CTD; 55117; -.
DR DisGeNET; 55117; -.
DR GeneCards; SLC6A15; -.
DR HGNC; HGNC:13621; SLC6A15.
DR HPA; ENSG00000072041; Tissue enhanced (brain, retina).
DR MIM; 607971; gene.
DR neXtProt; NX_Q9H2J7; -.
DR OpenTargets; ENSG00000072041; -.
DR PharmGKB; PA37799; -.
DR VEuPathDB; HostDB:ENSG00000072041; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000157277; -.
DR HOGENOM; CLU_006855_7_1_1; -.
DR InParanoid; Q9H2J7; -.
DR OMA; VVFCLRY; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q9H2J7; -.
DR TreeFam; TF352709; -.
DR PathwayCommons; Q9H2J7; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR SignaLink; Q9H2J7; -.
DR SIGNOR; Q9H2J7; -.
DR BioGRID-ORCS; 55117; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; SLC6A15; human.
DR GeneWiki; SLC6A15; -.
DR GenomeRNAi; 55117; -.
DR Pharos; Q9H2J7; Tchem.
DR PRO; PR:Q9H2J7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H2J7; protein.
DR Bgee; ENSG00000072041; Expressed in cortical plate and 146 other tissues.
DR ExpressionAtlas; Q9H2J7; baseline and differential.
DR Genevisible; Q9H2J7; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0005298; F:proline:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0015820; P:leucine transport; ISS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; NAS:UniProtKB.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR GO; GO:0015824; P:proline transport; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd11522; SLC6sbd_SBAT1; 1.
DR InterPro; IPR042934; B(0)AT2.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002438; Neutral_aa_SLC6.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01206; ORPHTRNSPORT.
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; Amino-acid transport; Glycoprotein; Ion transport;
KW Membrane; Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..730
FT /note="Sodium-dependent neutral amino acid transporter
FT B(0)AT2"
FT /id="PRO_0000214798"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..244
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..270
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..323
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..356
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..472
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..514
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..592
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..642
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045192"
FT VAR_SEQ 253..289
FT /note="IIYFSSLFPYVVLICFLIRAFLLNGSIDGIRHMFTPK -> VSMLEPFLILL
FT ITISGFIPLSNSVTDFCGQITHNTSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043030"
FT VAR_SEQ 290..730
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043031"
FT VARIANT 400
FT /note="A -> V (in dbSNP:rs12424429)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_052065"
FT VARIANT 603
FT /note="I -> M (in dbSNP:rs3782369)"
FT /id="VAR_052066"
SQ SEQUENCE 730 AA; 81836 MW; 45963118E06CFFE6 CRC64;
MPKNSKVVKR ELDDDVTESV KDLLSNEDAA DDAFKTSELI VDGQEEKDTD VEEGSEVEDE
RPAWNSKLQY ILAQVGFSVG LGNVWRFPYL CQKNGGGAYL LPYLILLMVI GIPLFFLELS
VGQRIRRGSI GVWNYISPKL GGIGFASCVV CYFVALYYNV IIGWSLFYFS QSFQQPLPWD
QCPLVKNASH TFVEPECEQS SATTYYWYRE ALNISSSISE SGGLNWKMTI CLLAAWVMVC
LAMIKGIQSS GKIIYFSSLF PYVVLICFLI RAFLLNGSID GIRHMFTPKL EIMLEPKVWR
EAATQVFFAL GLGFGGVIAF SSYNKRDNNC HFDAVLVSFI NFFTSVLATL VVFAVLGFKA
NVINEKCITQ NSETIMKFLK MGNISQDIIP HHINLSTVTA EDYHLVYDII QKVKEEEFPA
LHLNSCKIEE ELNKAVQGTG LAFIAFTEAM THFPASPFWS VMFFLMLVNL GLGSMFGTIE
GIVTPIVDTF KVRKEILTVI CCLLAFCIGL IFVQRSGNYF VTMFDDYSAT LPLLIVVILE
NIAVCFVYGI DKFMEDLKDM LGFAPSRYYY YMWKYISPLM LLSLLIASVV NMGLSPPGYN
AWIEDKASEE FLSYPTWGLV VCVSLVVFAI LPVPVVFIVR RFNLIDDSSG NLASVTYKRG
RVLKEPVNLE GDDTSLIHGK IPSEMPSPNF GKNIYRKQSG SPTLDTAPNG RYGIGYLMAD
IMPDMPESDL
