ID   S6A15_RAT               Reviewed;         729 AA.
AC   Q08469; Q63838;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT2;
DE   AltName: Full=Solute carrier family 6 member 15;
DE   AltName: Full=Transporter v7-3;
DE   AltName: Full=sodium- and chloride-dependent neurotransmitter transporter NTT73;
GN   Name=Slc6a15; Synonyms=Ntt73;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1363329; DOI=10.1016/0169-328x(92)90246-8;
RA   Uhl G.R., Kitayama S., Gregor P., Nanthakumar E., Persico A.M., Shimada S.;
RT   "Neurotransmitter transporter family cDNAs in a rat midbrain library:
RT   'orphan transporters' suggest sizable structural variations.";
RL   Brain Res. Mol. Brain Res. 16:353-359(1992).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=8738154; DOI=10.1016/0169-328x(95)00298-7;
RA   Inoue K., Sato K., Tohyama M., Shimada S., Uhl G.R.;
RT   "Widespread brain distribution of mRNA encoding the orphan neurotransmitter
RT   transporter v7-3.";
RL   Brain Res. Mol. Brain Res. 37:217-223(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699 AND SER-701, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. Can also
CC       transport low-affinity substrates such as alanine, phenylalanine,
CC       glutamine and pipecolic acid. Mediates the saturable, pH-sensitive and
CC       electrogenic cotransport of proline and sodium ions with a
CC       stoichiometry of 1:1. May have a role as transporter for
CC       neurotransmitter precursors into neurons. In contrast to other members
CC       of the neurotransmitter transporter family, does not appear to be
CC       chloride-dependent. {ECO:0000250|UniProtKB:Q9H2J7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(in) + Na(+)(in) = L-leucine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29263, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-isoleucine(in) + Na(+)(in) = L-isoleucine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29275, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine(in) + Na(+)(in) = L-methionine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68240, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparagine(in) + Na(+)(in) = L-asparagine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:71383, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-valine(in) + Na(+)(in) = L-valine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29267, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2J7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-pipecolate(in) + Na(+)(in) = L-pipecolate(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:71387, ChEBI:CHEBI:29101, ChEBI:CHEBI:61185;
CC         Evidence={ECO:0000250|UniProtKB:Q8BG16};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine(in) + Na(+)(in) = L-phenylalanine(out) +
CC         Na(+)(out); Xref=Rhea:RHEA:68244, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q8BG16};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9H2J7}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:Q9H2J7}.
CC   -!- TISSUE SPECIFICITY: Widely distributed in the central nervous system,
CC       including the olfactory bulb, the hypothalamus, the cerebral cortex,
CC       the hippocampus, and the cerebellum. In addition, intense expression is
CC       found in the motor nuclei including the oculomotor nucleus, abducens
CC       nucleus, trigeminal motor nucleus, facial nucleus, hypoglossal nucleus
CC       and ventral horn of spinal cord. Intense hybridization signals are also
CC       observed in the nuclei containing monoaminergic neurons, such as locus
CC       coeruleus, the substantia nigra pars compacta, the ventral tegmental
CC       area, the dorsal raphe nucleus and the median raphe nucleus.
CC       {ECO:0000269|PubMed:8738154}.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A15 subfamily. {ECO:0000305}.
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DR   EMBL; L22022; AAA41729.1; -; mRNA.
DR   EMBL; S56968; AAB25532.1; -; mRNA.
DR   PIR; I65413; I65413.
DR   RefSeq; NP_758824.1; NM_172321.1.
DR   AlphaFoldDB; Q08469; -.
DR   SMR; Q08469; -.
DR   STRING; 10116.ENSRNOP00000073005; -.
DR   GlyCosmos; Q08469; 3 sites, No reported glycans.
DR   GlyGen; Q08469; 3 sites.
DR   iPTMnet; Q08469; -.
DR   PhosphoSitePlus; Q08469; -.
DR   PaxDb; 10116-ENSRNOP00000032996; -.
DR   Ensembl; ENSRNOT00000029208.6; ENSRNOP00000032996.4; ENSRNOG00000027468.6.
DR   Ensembl; ENSRNOT00055028317; ENSRNOP00055022798; ENSRNOG00055016667.
DR   Ensembl; ENSRNOT00060007903; ENSRNOP00060005942; ENSRNOG00060004728.
DR   Ensembl; ENSRNOT00065004463; ENSRNOP00065003187; ENSRNOG00065003168.
DR   GeneID; 282712; -.
DR   KEGG; rno:282712; -.
DR   UCSC; RGD:628664; rat.
DR   AGR; RGD:628664; -.
DR   CTD; 55117; -.
DR   RGD; 628664; Slc6a15.
DR   eggNOG; KOG3659; Eukaryota.
DR   GeneTree; ENSGT00940000157277; -.
DR   HOGENOM; CLU_006855_7_1_1; -.
DR   InParanoid; Q08469; -.
DR   OMA; VVFCLRY; -.
DR   OrthoDB; 3084493at2759; -.
DR   PhylomeDB; Q08469; -.
DR   TreeFam; TF352709; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-RNO-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   PRO; PR:Q08469; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000027468; Expressed in Ammon's horn and 9 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0015657; F:branched-chain amino acid:sodium symporter activity; ISS:UniProtKB.
DR   GO; GO:0005295; F:neutral L-amino acid:sodium symporter activity; ISS:UniProtKB.
DR   GO; GO:0005298; F:proline:sodium symporter activity; ISS:UniProtKB.
DR   GO; GO:0015820; P:leucine transport; ISO:RGD.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
DR   GO; GO:0015824; P:proline transport; ISO:RGD.
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   NCBIfam; NF037979; Na_transp; 1.
DR   PANTHER; PTHR11616:SF101; SODIUM-DEPENDENT NEUTRAL AMINO ACID TRANSPORTER B(0)AT2; 1.
DR   PANTHER; PTHR11616; SODIUM/CHLORIDE DEPENDENT TRANSPORTER; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PRINTS; PR01206; ORPHTRNSPORT.
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; Q08469; RN.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Glycoprotein; Ion transport; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Reference proteome; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..729
FT                   /note="Sodium-dependent neutral amino acid transporter
FT                   B(0)AT2"
FT                   /id="PRO_0000214800"
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..729
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J7"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J7"
FT   MOD_RES         687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J7"
FT   MOD_RES         699
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        187
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   CONFLICT        1..3
FT                   /note="MPK -> IP (in Ref. 1; AAB25532)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   729 AA;  81596 MW;  ECDDC6403741B53E CRC64;
     MPKNSKVVKR DLDDDVIESV KDLLSNEDSV EDVSKKSELI VDVQEEKDTD AEDGSEVDDE
     RPAWNSKLQY ILAQVGFSVG LGNVWRFPYL CQKNGGGAYL LPYLILLLVI GIPLFFLELS
     VGQRIRRGSI GVWNYISPKL GGIGFASCVV CYFVALYYNV IIGWTLFYFS QSFQQPLPWD
     QCPLVKNASH TYIEPECEKS SATTYYWYRE ALAISSSISE SGGLNWKMTG CLLAAWVMVC
     LAMIKGIQSS GKIMYFSSLF PYVVLICFLI RSLLLNGSID GIRHMFTPKL EMMLEPKVWR
     EAATQVFFAL GLGFGGVIAF SSYNKRDNNC HFDAVLVSFI NFFTSVLATL VVFAVLGFKA
     NIVNEKCISQ NSEMILKLLK TGNVSWDVIP RHINLSAVTA EDYHVVYDII QKVKEEEFAV
     LHLKACQIED ELNKAVQGTG LAFIAFTEAM THFPASPFWS VMFFLMLINL GLGSMFGTIE
     GIITPVVDTF KVRKEILTVI CCLLAFCIGL MFVQRSGNYF VTMFDDYSAT LPLLIVVILE
     NIAVSFVYGI DKFLEDLTDM LGFAPSKYYY YMWKYISPLM LVTLLIASIV NMGLSPPGYN
     AWIKEKASEE FLSYPMWGMV VCFSLMVLAI LPVPVVFVIR RCNLIDDSSG NLASVTYKRG
     RVLKEPVNLD GDDASLIHGK IPSEMSSPNF GKNIYRKQSG SPTLDTAPNG RYGIGYLMAD
     MPDMPESDL
//