S6A15_MOUSE
ID S6A15_MOUSE Reviewed; 729 AA.
AC Q8BG16; Q333Y0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=Solute carrier family 6 member 15;
DE AltName: Full=Transporter v7-3;
GN Name=Slc6a15; Synonyms=B0at2, Ntt73;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Liu Q.-R., Uhl G.R.;
RT "Mouse sodium-dependent orphan neurotransmitter transporter V73 cDNA.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RA Liu Q.-R., Uhl G.R.;
RT "Characterization of orphan neurotransmitter transporter V73 genomic
RT structure.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16185194; DOI=10.1042/bj20051273;
RA Broer A., Tietze N., Kowalczuk S., Chubb S., Munzinger M., Bak L.K.,
RA Broer S.;
RT "The orphan transporter v7-3 (slc6a15) is a Na+-dependent neutral amino
RT acid transporter (B0AT2).";
RL Biochem. J. 393:421-430(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 DISRUPTION PHENOTYPE.
RX PubMed=17931606; DOI=10.1016/j.brainres.2007.09.001;
RA Drgonova J., Liu Q.R., Hall F.S., Krieger R.M., Uhl G.R.;
RT "Deletion of v7-3 (SLC6A15) transporter allows assessment of its roles in
RT synaptosomal proline uptake, leucine uptake and behaviors.";
RL Brain Res. 1183:10-20(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as a sodium-dependent neutral amino acid
CC transporter. Exhibits preference for methionine and for the branched-
CC chain amino acids, particularly leucine, valine and isoleucine.
CC Mediates the saturable, pH-sensitive and electrogenic cotransport of
CC proline and sodium ions with a stoichiometry of 1:1. May have a role as
CC transporter for neurotransmitter precursors into neurons. In contrast
CC to other members of the neurotransmitter transporter family, does not
CC appear to be chloride-dependent (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16185194}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=195 uM for proline (in the presence of 100 mM NaCL)
CC {ECO:0000269|PubMed:16185194};
CC KM=510 uM for proline (in the presence of 30 mM NaCL)
CC {ECO:0000269|PubMed:16185194};
CC KM=790 uM for proline (in the presence of 3 mM NaCL)
CC {ECO:0000269|PubMed:16185194};
CC KM=81 uM for leucine {ECO:0000269|PubMed:16185194};
CC KM=58 uM for isoleucine {ECO:0000269|PubMed:16185194};
CC KM=40 uM for methionine {ECO:0000269|PubMed:16185194};
CC KM=670 uM for alanine {ECO:0000269|PubMed:16185194};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:16185194};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Significant expressed in brain, lung and kidney.
CC regions, the cortex, the cerebellum and the brain stem.
CC {ECO:0000269|PubMed:16185194}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout development, starting with the
CC pre-implantation embryo. {ECO:0000269|PubMed:16185194}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile and fail to
CC demonstrate any striking abnormality in motor and sensory functions.
CC Other transporters could help to compensate for lost of SLC6A15.
CC {ECO:0000269|PubMed:17931606}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A15 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY149280; AAN75437.1; -; mRNA.
DR EMBL; AY149281; AAN75438.1; -; mRNA.
DR EMBL; AY149282; AAN75439.1; -; Genomic_DNA.
DR EMBL; AM085111; CAJ29896.1; -; mRNA.
DR EMBL; AK036136; BAC29315.1; -; mRNA.
DR EMBL; CH466539; EDL21676.1; -; Genomic_DNA.
DR EMBL; CH466539; EDL21677.1; -; Genomic_DNA.
DR EMBL; BC076593; AAH76593.1; -; mRNA.
DR CCDS; CCDS24156.1; -.
DR RefSeq; NP_001239259.1; NM_001252330.1.
DR RefSeq; NP_780537.1; NM_175328.3.
DR RefSeq; XP_006513045.1; XM_006512982.3.
DR RefSeq; XP_006513046.1; XM_006512983.3.
DR RefSeq; XP_006513047.1; XM_006512984.3.
DR AlphaFoldDB; Q8BG16; -.
DR SMR; Q8BG16; -.
DR STRING; 10090.ENSMUSP00000073829; -.
DR GlyGen; Q8BG16; 4 sites.
DR iPTMnet; Q8BG16; -.
DR PhosphoSitePlus; Q8BG16; -.
DR SwissPalm; Q8BG16; -.
DR MaxQB; Q8BG16; -.
DR PaxDb; Q8BG16; -.
DR PeptideAtlas; Q8BG16; -.
DR PRIDE; Q8BG16; -.
DR ProteomicsDB; 253391; -.
DR Antibodypedia; 1932; 158 antibodies from 23 providers.
DR DNASU; 103098; -.
DR Ensembl; ENSMUST00000074204; ENSMUSP00000073829; ENSMUSG00000019894.
DR Ensembl; ENSMUST00000179636; ENSMUSP00000136676; ENSMUSG00000019894.
DR GeneID; 103098; -.
DR KEGG; mmu:103098; -.
DR UCSC; uc007gyj.2; mouse.
DR CTD; 55117; -.
DR MGI; MGI:2143484; Slc6a15.
DR VEuPathDB; HostDB:ENSMUSG00000019894; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000157277; -.
DR HOGENOM; CLU_006855_7_1_1; -.
DR InParanoid; Q8BG16; -.
DR OMA; VVFCLRY; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q8BG16; -.
DR TreeFam; TF352709; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 103098; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BG16; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BG16; protein.
DR Bgee; ENSMUSG00000019894; Expressed in saccule of membranous labyrinth and 196 other tissues.
DR ExpressionAtlas; Q8BG16; baseline and differential.
DR Genevisible; Q8BG16; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005298; F:proline:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0015820; P:leucine transport; IDA:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR GO; GO:0015824; P:proline transport; IDA: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 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_0000214799"
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 REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9H2J7"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2J7"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
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"
SQ SEQUENCE 729 AA; 81792 MW; D336735E9D1E9B97 CRC64;
MPKNSKVVKR DLDDDVIESV KDLLSNEDSV EEVSKKSELI VDVQEEKDTD AEDGSEADDE
RPAWNSKLQY ILAQVGFSVG LGNVWRFPYL CQKNGGGAYL LPYLILLLVI GIPLFFLELS
VGQRIRRGSI GVWNYISPKL GGIGFASCVV CYFVALYYNV IIGWTLFYFS QSFQQPLPWD
QCPLVKNASH TYVEPECEQS SATTYYWYRE ALDITSSISD SGGLNWKMTV CLLVAWVMVC
LAMIKGIQSS GKIMYFSSLF PYVVLICFLI RSLLLNGSID GIRHMFTPKL EMMLEPKVWR
EAATQVFFAL GLGFGGVIAF SSYNKRDNNC HFDAVLVSFI NFFTSVLATL VVFAVLGFKA
NIVNEKCISQ NSEMILKLLK MGNISWDVIP HHINLSAVTV EDYRLVYDII QKVKEEEFAV
LHLNACQIED ELNKAVQGTG LAFIAFTEAM THFPASPFWS VMFFLMLINL GLGSMFGTIE
GIITPIVDTF KVRKEILTVI CCLLAFCIGL IFVQRSGNYF VTMFDDYSAT LPLLIVVILE
NIAVSFVYGI DKFIEDLTDM LGFAPSKYYY YMWKYISPLM LLTLLIASIV NMGLSPPGYN
AWIKEKASEE FLSYPMWGMV VCFSLMVLAI LPVPVVFIIR RCNLIDDSSG NLASVTYKRG
RVLKEPVNLE GDDASLIHGK IPSEMSSPNF GKNIYRKQSG SPTLDTAPNG RYGIGYLMAD
MPDMPESDL
