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 02-SEP-2026, entry version 164. DE RecName: Full=Sodium-coupled neutral amino acid transporter 3 {ECO:0000305}; 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 {ECO:0000303|PubMed:10716701}; 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, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain {ECO:0000269|PubMed:10716701}, Kidney RC {ECO:0000269|PubMed:10716701}, and Liver RC {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 Retina RC {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 FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=16249471; DOI=10.1167/iovs.05-0488; RA Umapathy N.S., Li W., Mysona B.A., Smith S.B., Ganapathy V.; RT "Expression and function of glutamine transporters SN1 (SNAT3) and SN2 RT (SNAT5) in retinal Mueller cells."; RL Invest. Ophthalmol. Vis. Sci. 46:3980-3987(2005). RN [5] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=15899884; DOI=10.1074/jbc.m504401200; RA Gu S., Villegas C.J., Jiang J.X.; RT "Differential regulation of amino acid transporter SNAT3 by insulin in RT hepatocytes."; RL J. Biol. Chem. 280:26055-26062(2005). RN [6] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RX PubMed=18689705; DOI=10.1167/iovs.08-2245; RA Umapathy N.S., Dun Y., Martin P.M., Duplantier J.N., Roon P., Prasad P., RA Smith S.B., Ganapathy V.; RT "Expression and function of system N glutamine transporters (SN1/SN2 or RT SNAT3/SNAT5) in retinal ganglion cells."; RL Invest. Ophthalmol. Vis. Sci. 49:5151-5160(2008). RN [7] RP INDUCTION. RX PubMed=19458124; DOI=10.1152/ajprenal.90318.2008; RA Busque S.M., Wagner C.A.; RT "Potassium restriction, high protein intake, and metabolic acidosis RT increase expression of the glutamine transporter SNAT3 (Slc38a3) in mouse RT kidney."; RL Am. J. Physiol. 297:F440-F450(2009). RN [8] 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). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=21364602; DOI=10.1038/jcbfm.2011.21; RA Ruderisch N., Virgintino D., Makrides V., Verrey F.; RT "Differential axial localization along the mouse brain vascular tree of RT luminal sodium-dependent glutamine transporters Snat1 and Snat3."; RL J. Cereb. Blood Flow Metab. 31:1637-1647(2011). RN [10] RP INDUCTION. RX PubMed=24854847; DOI=10.1159/000358722; RA Balkrishna S., Broeer A., Welford S.M., Hatzoglou M., Broeer S.; RT "Expression of glutamine transporter Slc38a3 (SNAT3) during acidosis is RT mediated by a different mechanism than tissue-specific expression."; RL Cell. Physiol. Biochem. 33:1591-1606(2014). RN [11] RP FUNCTION, AND MUTAGENESIS OF 264-LEU--HIS-505. RX PubMed=26490457; DOI=10.1007/s00424-015-1742-0; RA Chan K., Busque S.M., Sailer M., Stoeger C., Broeer S., Daniel H., RA Rubio-Aliaga I., Wagner C.A.; RT "Loss of function mutation of the Slc38a3 glutamine transporter reveals its RT critical role for amino acid metabolism in the liver, brain, and kidney."; RL Pflugers Arch. 468:213-227(2016). RN [12] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=29561757; DOI=10.3390/ijms19040924; RA Dong W., Todd A.C., Broeer A., Hulme S.R., Broeer S., Billups B.; RT "PKC-Mediated Modulation of Astrocyte SNAT3 Glutamine Transporter Function RT at Synapses in Situ."; RL Int. J. Mol. Sci. 19:0-0(2018). RN [13] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=30017230; DOI=10.1016/j.neuint.2018.07.001; RA Dabrowska K., Albrecht J., Zielinska M.; RT "Protein kinase C-mediated impairment of glutamine outward transport and RT SN1 transporter distribution by ammonia in mouse cortical astrocytes."; RL Neurochem. Int. 118:225-232(2018). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=32046769; DOI=10.1186/s12987-020-0178-x; RA Dolgodilina E., Camargo S.M., Roth E., Herzog B., Nunes V., Palacin M., RA Verrey F.; RT "Choroid plexus LAT2 and SNAT3 as partners in CSF amino acid homeostasis RT maintenance."; RL Fluids Barriers CNS 17:17-17(2020). CC -!- FUNCTION: Symporter that cotransports specific neutral amino acids and CC sodium ions, coupled to an H(+) antiporter activity (PubMed:10716701, CC PubMed:15899884, PubMed:16249471, PubMed:18689705, PubMed:29561757, CC PubMed:30017230). Mainly participates in the glutamate-GABA-glutamine CC cycle in brain where it transports L-glutamine from astrocytes in the CC intercellular space for the replenishment of both neurotransmitters CC glutamate and gamma-aminobutyric acid (GABA) in neurons and also CC functions as the major influx transporter in ganglion cells mediating CC the uptake of glutamine (PubMed:18689705, PubMed:29561757, CC PubMed:30017230). The transport activity is specific for L-glutamine, CC L-histidine and L-asparagine (PubMed:10716701, PubMed:15899884, CC PubMed:16249471, PubMed:18689705, PubMed:29561757, PubMed:30017230). CC The transport is electroneutral coupled to the cotransport of 1 Na(+) CC and the antiport of 1 H(+) (By similarity). The transport is pH CC dependent, saturable, Li(+) tolerant and functions in both direction CC depending on the concentration gradients of its substrates and CC cotransported ions (PubMed:10716701, PubMed:16249471, PubMed:18689705). CC Also mediates an amino acid-gated H(+) conductance that is not CC stoichiometrically coupled to the amino acid transport but which CC influences the ionic gradients that drive the amino acid transport (By CC similarity). In addition, may play a role in nitrogen metabolism, amino CC acid homeostasis, glucose metabolism and renal ammoniagenesis CC (PubMed:26490457). {ECO:0000250|UniProtKB:Q9JHZ9, CC ECO:0000269|PubMed:10716701, ECO:0000269|PubMed:15899884, CC ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:18689705, CC ECO:0000269|PubMed:26490457, ECO:0000269|PubMed:29561757, CC ECO:0000269|PubMed:30017230}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine(out) + Na(+)(out) + H(+)(in) = L-histidine(in) + CC Na(+)(in) + H(+)(out); Xref=Rhea:RHEA:71135, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57595; CC Evidence={ECO:0000269|PubMed:15899884, ECO:0000269|PubMed:18689705, CC ECO:0000269|PubMed:29561757}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71136; CC Evidence={ECO:0000269|PubMed:15899884, ECO:0000269|PubMed:18689705, CC ECO:0000269|PubMed:29561757}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71137; CC Evidence={ECO:0000250|UniProtKB:Q9JHZ9}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamine(out) + Na(+)(out) + H(+)(in) = L-glutamine(in) + CC Na(+)(in) + H(+)(out); Xref=Rhea:RHEA:71127, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58359; CC Evidence={ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:30017230}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71128; CC Evidence={ECO:0000269|PubMed:16249471}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71129; CC Evidence={ECO:0000269|PubMed:30017230}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-asparagine(out) + Na(+)(out) + H(+)(in) = L-asparagine(in) + CC Na(+)(in) + H(+)(out); Xref=Rhea:RHEA:71131, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58048; CC Evidence={ECO:0000269|PubMed:16249471}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71132; CC Evidence={ECO:0000269|PubMed:16249471}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71133; CC Evidence={ECO:0000250|UniProtKB:Q9JHZ9}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.1 mM for L-histidine (in Na(+)-buffer at pH 7.5) CC {ECO:0000269|PubMed:10716701}; CC KM=1.55 mM for L-glutamine (in Na(+)-buffer at pH 7.5) CC {ECO:0000269|PubMed:10716701}; CC KM=0.41 mM for L-glutamine {ECO:0000269|PubMed:10716701}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18689705, CC ECO:0000269|PubMed:30017230, ECO:0000269|PubMed:32046769}; Multi-pass CC membrane protein {ECO:0000255}. Basolateral cell membrane CC {ECO:0000269|PubMed:10716701}. Note=The localization appears to be CC basolateral in the plasma membrane of hepatocytes surrounding the CC central vein (PubMed:10716701). Localized at the cerebrospinal fluid CC (CSF)-facing membrane of the choroid plexus epithelial cells CC (PubMed:32046769). In astrocytes, the localization at cell membrane is CC decreased by ammonia through the PKC signaling (PubMed:30017230). CC Expressed in both luminal and abluminal plasma membranes of larger CC microvessels and blood brain barrier (BBB) capillaries CC (PubMed:21364602). Restricted to the basolateral membranes of S3 CC segment cells of the proximal tubules (By similarity). CC {ECO:0000250|UniProtKB:Q9JHZ9, ECO:0000269|PubMed:10716701, CC ECO:0000269|PubMed:21364602, ECO:0000269|PubMed:30017230, CC ECO:0000269|PubMed:32046769}. CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver, moderately CC expressed in kidney and brain, and barely detectable in heart and CC muscle (PubMed:10716701). Within liver, expressed in hepatocytes CC (PubMed:10716701). Not detected in testis (PubMed:10716701). Expressed CC in cells of the ganglion cell layer, in soma of some cells of the inner CC nuclear layer (at protein level) (PubMed:18689705). Expressed in the CC inner segments of photoreceptor cells (PubMed:18689705). CC {ECO:0000269|PubMed:10716701, ECO:0000269|PubMed:18689705}. CC -!- INDUCTION: Up-regulated during renal ammoniagenesis and urinary CC ammonium excretion (PubMed:19458124). Up-regulated during acute CC acidosis (PubMed:24854847). Down-regulated by chronic treatment by CC insulin in hepatocytes (PubMed:15899884). Up-regulated by acute CC treatment by insulin (PubMed:15899884). {ECO:0000269|PubMed:15899884, CC ECO:0000269|PubMed:19458124, ECO:0000269|PubMed:24854847}. CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. CC {ECO:0000305}. CC -!- CAUTION: Fei et al (PMID:10823827) shows that the transport process is CC electrogenic with a Na(+):L-glutamine stoichiometry of 2:1, contrary to CC the conclusions of Chaudhry et al (PMID:10619430) who finds that the CC transport is electroneutral with a Na(+):L-glutamine stoichiometry of CC 1:1 (By similarity). Chaudhry et al (PMID:11742981) shows that this CC electrogenic transport describes by Fei et al (PMID:10823827) would CC correspond to an amino acid-gated H(+) conductance that is not CC stoichiometrically coupled to the amino acid transport but which CC influences the ionic gradients that drive the amino acid transport (By CC similarity). {ECO:0000250|UniProtKB:Q99624, CC ECO:0000250|UniProtKB:Q9JHZ9}. 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; 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_030100556.1; XM_030244696.2. DR RefSeq; XP_030100557.1; XM_030244697.1. DR RefSeq; XP_036011271.1; XM_036155378.1. DR AlphaFoldDB; Q9DCP2; -. DR SMR; Q9DCP2; -. DR BioGRID; 218051; 2. DR FunCoup; Q9DCP2; 158. DR STRING; 10090.ENSMUSP00000130414; -. DR TCDB; 2.A.18.6.2; the amino acid/auxin permease (aaap) family. DR GlyCosmos; Q9DCP2; 4 sites, No reported glycans. DR GlyGen; Q9DCP2; 6 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; Q9DCP2; -. DR PhosphoSitePlus; Q9DCP2; -. DR SwissPalm; Q9DCP2; -. DR jPOST; Q9DCP2; -. DR PaxDb; 10090-ENSMUSP00000130414; -. DR PeptideAtlas; Q9DCP2; -. DR ProteomicsDB; 260777; -. DR Antibodypedia; 73268; 95 antibodies from 24 providers. DR DNASU; 76257; -. DR Ensembl; ENSMUST00000010208.14; ENSMUSP00000010208.9; ENSMUSG00000010064.16. DR Ensembl; ENSMUST00000167868.8; ENSMUSP00000130414.2; ENSMUSG00000010064.16. DR Ensembl; ENSMUST00000177567.8; ENSMUSP00000137561.2; ENSMUSG00000010064.16. DR Ensembl; ENSMUST00000193932.6; ENSMUSP00000142087.2; ENSMUSG00000010064.16. DR GeneID; 76257; -. DR KEGG; mmu:76257; -. DR UCSC; uc009rmn.1; mouse. DR AGR; MGI:1923507; -. 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; MEVAGEM; -. DR OrthoDB; 655540at2759; -. DR PhylomeDB; Q9DCP2; -. DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane. DR BioGRID-ORCS; 76257; 0 hits in 77 CRISPR screens. DR PRO; PR:Q9DCP2; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q9DCP2; protein. DR Bgee; ENSMUSG00000010064; Expressed in retinal neural layer and 157 other cell types or tissues. DR ExpressionAtlas; Q9DCP2; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL. DR GO; GO:0016323; C:basolateral plasma membrane; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:GO_Central. DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; ISO:GO_Central. DR GO; GO:0140831; F:L-asparagine, sodium:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:MGI. DR GO; GO:0140830; F:L-glutamine, sodium:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:MGI. DR GO; GO:0140832; F:L-histidine, sodium:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0005295; F:neutral L-amino acid:sodium symporter activity; ISS:UniProtKB. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central. DR GO; GO:1903713; P:asparagine transmembrane transport; ISO:GO_Central. DR GO; GO:0006867; P:asparagine transport; ISS:UniProtKB. 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:0015817; P:histidine transport; IDA:MGI. DR GO; GO:0080144; P:intracellular amino acid homeostasis; IMP:UniProtKB. DR GO; GO:0015808; P:L-alanine transport; ISO:GO_Central. DR GO; GO:1903811; P:L-asparagine import across plasma membrane; ISS:UniProtKB. DR GO; GO:1903803; P:L-glutamine import across plasma membrane; IDA:UniProtKB. DR GO; GO:0010585; P:L-glutamine secretion; IDA:UniProtKB. DR GO; GO:0006868; P:L-glutamine transport; IDA:MGI. DR GO; GO:1903810; P:L-histidine import across plasma membrane; IDA:UniProtKB. DR GO; GO:0089709; P:L-histidine transmembrane transport; ISO:GO_Central. DR GO; GO:1902024; P:L-histidine transport; ISS:UniProtKB. DR GO; GO:2000487; P:positive regulation of glutamine transport; ISO:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR InterPro; IPR013057; AA_transpt_TM. DR PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1. DR PANTHER; PTHR22950:SF22; SODIUM-COUPLED NEUTRAL AMINO ACID TRANSPORTER 3; 1. 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 COMPBIAS 33..43 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 76 FT /note="Modulates L-glutamine-induced conductances and Na(+) FT binding" FT /evidence="ECO:0000250|UniProtKB:Q9JHZ9" 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 MUTAGEN 264..505 FT /note="Missing: Homozygous mice are lethal. Mice die FT between 18 and 20 days after birth. Mice are small, FT lethargic and ataxic." FT /evidence="ECO:0000269|PubMed:26490457" 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 //