S38A3_MOUSE
ID S38A3_MOUSE Reviewed; 505 AA.
AC Q9DCP2; Q8BS53; Q9JLL8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 3;
DE AltName: Full=N-system amino acid transporter 1;
DE AltName: Full=Na(+)-coupled neutral amino acid transporter 3;
DE AltName: Full=Solute carrier family 38 member 3;
DE Short=mNAT;
DE AltName: Full=System N amino acid transporter 1;
GN Name=Slc38a3 {ECO:0000312|MGI:MGI:1923507}; Synonyms=Sn1, Snat3;
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] {ECO:0000305, ECO:0000312|EMBL:AAF61849.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:10716701},
RC Kidney {ECO:0000269|PubMed:10716701}, and
RC Liver {ECO:0000312|EMBL:AAF61849.1};
RX PubMed=10716701; DOI=10.1073/pnas.97.7.3230;
RA Gu S., Roderick H.L., Camacho P., Jiang J.X.;
RT "Identification and characterization of an amino acid transporter expressed
RT differentially in liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3230-3235(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 [3] {ECO:0000312|EMBL:AAH54846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH55339.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH55339.1}, and
RC Retina {ECO:0000312|EMBL:AAH54846.1};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Pancreas;
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: Sodium-dependent amino acid/proton antiporter. Mediates
CC electrogenic cotransport of glutamine and sodium ions in exchange for
CC protons. Also recognizes histidine, asparagine and alanine. May mediate
CC amino acid transport in either direction under physiological
CC conditions. May play a role in nitrogen metabolism and synaptic
CC transmission. {ECO:0000250|UniProtKB:Q9JHZ9,
CC ECO:0000269|PubMed:10716701}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10716701};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10716701}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver, moderately
CC expressed in kidney and brain, and barely detectable in heart and
CC muscle. Within liver, expressed in hepatocytes. Not detected in testis.
CC {ECO:0000269|PubMed:10716701}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF159856; AAF61849.1; -; mRNA.
DR EMBL; AK002607; BAB22226.1; -; mRNA.
DR EMBL; AK035155; BAC28963.1; -; mRNA.
DR EMBL; BC054846; AAH54846.1; -; mRNA.
DR EMBL; BC055339; AAH55339.1; -; mRNA.
DR CCDS; CCDS23503.1; -.
DR RefSeq; NP_001186146.1; NM_001199217.1.
DR RefSeq; NP_001186147.1; NM_001199218.1.
DR RefSeq; NP_076294.2; NM_023805.3.
DR RefSeq; XP_017169171.1; XM_017313682.1.
DR AlphaFoldDB; Q9DCP2; -.
DR SMR; Q9DCP2; -.
DR BioGRID; 218051; 1.
DR STRING; 10090.ENSMUSP00000130414; -.
DR TCDB; 2.A.18.6.2; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q9DCP2; 4 sites.
DR iPTMnet; Q9DCP2; -.
DR PhosphoSitePlus; Q9DCP2; -.
DR SwissPalm; Q9DCP2; -.
DR jPOST; Q9DCP2; -.
DR MaxQB; Q9DCP2; -.
DR PaxDb; Q9DCP2; -.
DR PeptideAtlas; Q9DCP2; -.
DR PRIDE; Q9DCP2; -.
DR ProteomicsDB; 260777; -.
DR Antibodypedia; 73268; 94 antibodies from 24 providers.
DR DNASU; 76257; -.
DR Ensembl; ENSMUST00000010208; ENSMUSP00000010208; ENSMUSG00000010064.
DR Ensembl; ENSMUST00000167868; ENSMUSP00000130414; ENSMUSG00000010064.
DR Ensembl; ENSMUST00000177567; ENSMUSP00000137561; ENSMUSG00000010064.
DR Ensembl; ENSMUST00000193932; ENSMUSP00000142087; ENSMUSG00000010064.
DR GeneID; 76257; -.
DR KEGG; mmu:76257; -.
DR UCSC; uc009rmn.1; mouse.
DR CTD; 10991; -.
DR MGI; MGI:1923507; Slc38a3.
DR VEuPathDB; HostDB:ENSMUSG00000010064; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000157127; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q9DCP2; -.
DR OMA; CWGVAVM; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q9DCP2; -.
DR TreeFam; TF328787; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 76257; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Slc38a3; mouse.
DR PRO; PR:Q9DCP2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCP2; protein.
DR Bgee; ENSMUSG00000010064; Expressed in retinal neural layer and 155 other tissues.
DR ExpressionAtlas; Q9DCP2; baseline and differential.
DR Genevisible; Q9DCP2; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006867; P:asparagine transport; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IDA:MGI.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0006868; P:glutamine transport; IDA:MGI.
DR GO; GO:0015817; P:histidine transport; IDA:MGI.
DR GO; GO:0015808; P:L-alanine transport; ISO:MGI.
DR GO; GO:2000487; P:positive regulation of glutamine transport; ISO:MGI.
DR GO; GO:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; IDA:MGI.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Antiport; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..505
FT /note="Sodium-coupled neutral amino acid transporter 3"
FT /id="PRO_0000093829"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 239..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 110
FT /note="S -> N (in Ref. 2; BAC28963)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Q -> R (in Ref. 2; BAC28963)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="T -> A (in Ref. 1; AAF61849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 55592 MW; 368DBB87F1BB248A CRC64;
MEIPRQTEMV ELVPNGKHLE GLLPVGVPTT DTQRTEDTQH CGEGKGFLQK SPSKEPHFTD
FEGKTSFGMS VFNLSNAIMG SGILGLAYAM ANTGIILFLF LLTAVALLSS YSIHLLLKSS
GIVGIRAYEQ LGYRAFGTPG KLAAALAITL QNIGAMSSYL YIIKSELPLV IQTFLNLEKP
ASVWYMDGNY LVILVSVTII LPLALMRQLG YLGYSSGFSL SCMVFFLIAV IYKKFQVPCP
LAHNLANATG NFSHMVVAEE KAQLQGEPDT AAEAFCTPSY FTLNSQTAYT IPIMAFAFVC
HPEVLPIYTE LKDPSKRKMQ HISNLSIAVM YVMYFLAALF GYLTFYDGVE SELLHTYSKV
DPFDVLILCV RVAVLIAVTL TVPIVLFPVR RAIQQMLFQN QEFSWLRHVL IATGLLTCIN
LLVIFAPNIL GIFGIIGATS APCLIFIFPA IFYFRIMPTD KEPARSTPKI LALCFAAVGF
LLMTMSLSFI IIDWVSGTSQ HGGNH
