ID   S38A4_HUMAN             Reviewed;         547 AA.
AC   Q969I6; A8K553;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 160.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 4 {ECO:0000305};
DE   AltName: Full=Amino acid transporter A3;
DE   AltName: Full=Na(+)-coupled neutral amino acid transporter 4;
DE   AltName: Full=Solute carrier family 38 member 4;
DE   AltName: Full=System A amino acid transporter 3;
DE   AltName: Full=System N amino acid transporter 3;
GN   Name=SLC38A4 {ECO:0000312|HGNC:HGNC:14679};
GN   Synonyms=ATA3 {ECO:0000303|PubMed:11342143}, NAT3
GN   {ECO:0000303|PubMed:11414754}, SNAT4 {ECO:0000303|PubMed:16148032};
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], FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Hepatoma;
RX   PubMed=11342143; DOI=10.1016/s0005-2736(00)00390-4;
RA   Hatanaka T., Huang W., Ling R., Prasad P.D., Sugawara M., Leibach F.H.,
RA   Ganapathy V.;
RT   "Evidence for the transport of neutral as well as cationic amino acids by
RT   ATA3, a novel and liver-specific subtype of amino acid transport system
RT   A.";
RL   Biochim. Biophys. Acta 1510:10-17(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11414754; DOI=10.1006/geno.2001.6567;
RA   Gu S., Adan-Rice D., Leach R.J., Jiang J.X.;
RT   "A novel human amino acid transporter, hNAT3: cDNA cloning, chromosomal
RT   mapping, genomic structure, expression, and functional characterization.";
RL   Genomics 74:262-272(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Matsuo H., Kanai Y., Kim D.K., Cha S.H., Chairoungdua A., Fukuda J.,
RA   Endou H.;
RT   "Molecular cloning and characterization of a novel system A amino acid
RT   transporter from human liver.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   REVIEW, AND GENE NOMENCLATURE.
RX   PubMed=12845534; DOI=10.1007/s00424-003-1117-9;
RA   Mackenzie B., Erickson J.D.;
RT   "Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38
RT   gene family.";
RL   Pflugers Arch. 447:784-795(2004).
RN   [8]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16148032; DOI=10.1152/ajpcell.00258.2005;
RA   Desforges M., Lacey H.A., Glazier J.D., Greenwood S.L., Mynett K.J.,
RA   Speake P.F., Sibley C.P.;
RT   "SNAT4 isoform of system A amino acid transporter is expressed in human
RT   placenta.";
RL   Am. J. Physiol. 290:C305-C312(2006).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19015196; DOI=10.1113/jphysiol.2008.161331;
RA   Desforges M., Mynett K.J., Jones R.L., Greenwood S.L., Westwood M.,
RA   Sibley C.P., Glazier J.D.;
RT   "The SNAT4 isoform of the system A amino acid transporter is functional in
RT   human placental microvillous plasma membrane.";
RL   J. Physiol. (Lond.) 587:61-72(2009).
RN   [10]
RP   TOPOLOGY, AND GLYCOSYLATION AT ASN-260 AND ASN-264.
RX   PubMed=21917917; DOI=10.1074/jbc.m111.220277;
RA   Shi Q., Padmanabhan R., Villegas C.J., Gu S., Jiang J.X.;
RT   "Membrane topological structure of neutral system N/A amino acid
RT   transporter 4 (SNAT4) protein.";
RL   J. Biol. Chem. 286:38086-38094(2011).
RN   [11]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=33928121; DOI=10.3389/fmolb.2021.646574;
RA   Fairweather S.J., Okada S., Gauthier-Coles G., Javed K., Broeer A.,
RA   Broeer S.;
RT   "A GC-MS/Single-Cell Method to Evaluate Membrane Transporter Substrate
RT   Specificity and Signaling.";
RL   Front. Mol. Biosci. 8:646574-646574(2021).
RN   [12]
RP   VARIANT 446-ARG--HIS-547 DEL.
RX   PubMed=29961568; DOI=10.1016/j.ajhg.2018.06.001;
RG   NIHR BioResource;
RG   Care4Rare Canada Consortium;
RA   Ito Y., Carss K.J., Duarte S.T., Hartley T., Keren B., Kurian M.A.,
RA   Marey I., Charles P., Mendonca C., Nava C., Pfundt R., Sanchis-Juan A.,
RA   van Bokhoven H., van Essen A., van Ravenswaaij-Arts C., Boycott K.M.,
RA   Kernohan K.D., Dyack S., Raymond F.L.;
RT   "De Novo Truncating Mutations in WASF1 Cause Intellectual Disability with
RT   Seizures.";
RL   Am. J. Hum. Genet. 103:144-153(2018).
CC   -!- FUNCTION: Symporter that cotransports neutral amino acids and sodium
CC       ions from the extraccellular to the intracellular side of the cell
CC       membrane (PubMed:11342143, PubMed:19015196, PubMed:33928121). The
CC       transport is electrogenic, pH dependent and partially tolerates
CC       substitution of Na(+) by Li(+) (PubMed:11414754). Preferentially
CC       transports smaller amino acids, such as glycine, L-alanine, L-serine,
CC       L-asparagine and L-threonine, followed by L-cysteine, L-histidine, L-
CC       proline and L-glutamine and L-methionine (PubMed:11414754,
CC       PubMed:33928121). {ECO:0000269|PubMed:11342143,
CC       ECO:0000269|PubMed:11414754, ECO:0000269|PubMed:19015196,
CC       ECO:0000269|PubMed:33928121}.
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:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68242;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71385;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC         Evidence={ECO:0000305|PubMed:33928121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:11342143, ECO:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68230;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:0000269|PubMed:11414754, ECO:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:0000269|PubMed:11414754, ECO:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68238;
CC         Evidence={ECO:0000305|PubMed:33928121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine(in) + Na(+)(in) = L-histidine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:71583, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595;
CC         Evidence={ECO:0000269|PubMed:11414754, ECO:0000269|PubMed:33928121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71585;
CC         Evidence={ECO:0000305|PubMed:33928121};
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:Q9EQ25};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68234;
CC         Evidence={ECO:0000250|UniProtKB:Q9EQ25};
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:Q9EQ25};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28969;
CC         Evidence={ECO:0000250|UniProtKB:Q9EQ25};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.6 mM for glycine {ECO:0000269|PubMed:11342143};
CC         KM=0.3 mM for L-arginine {ECO:0000269|PubMed:11342143};
CC         KM=3.52 mM for L-alanine {ECO:0000269|PubMed:11414754};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:11342143};
CC   -!- INTERACTION:
CC       Q969I6; P48165: GJA8; NbExp=3; IntAct=EBI-17459810, EBI-17458373;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11414754,
CC       ECO:0000269|PubMed:16148032}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11414754}. Cell projection, microvillus membrane
CC       {ECO:0000269|PubMed:19015196}; Multi-pass membrane protein.
CC       Note=Microvillus membrane localization in placenta.
CC       {ECO:0000269|PubMed:19015196}.
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in embryonic and adult
CC       liver, and at lower levels in the kidney (PubMed:11342143,
CC       PubMed:11414754). Expressed at lower levels in adult muscle and
CC       pancreas (PubMed:11414754). Detected in fetal blood vessels
CC       (PubMed:16148032). Expressed in syncytiotrophoblas of placenta during
CC       first trimester and at term (PubMed:19015196, PubMed:16148032). Highly
CC       expressed in first trimester placenta compared to term placenta
CC       (PubMed:19015196). {ECO:0000269|PubMed:11342143,
CC       ECO:0000269|PubMed:11414754, ECO:0000269|PubMed:16148032,
CC       ECO:0000269|PubMed:19015196}.
CC   -!- PTM: The disulfide bond plays an important role in substrate transport,
CC       but has no effect on trafficking to the cell surface.
CC       {ECO:0000250|UniProtKB:Q8R1S9}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: There is a disagreement about sodium-independent transport of
CC       cationic amino acids, such as L-arginine and L-lysine. While Hatanaka
CC       et al (PubMed:11342143) shown that SLC38A4 may mediate sodium-
CC       independent transport of cationic amino acids, such as L-arginine and
CC       L-lysine (PubMed:11342143). Recent studies by Fairweather et al
CC       (PubMed:33928121), using quantitative LC-MS analysis, shown any
CC       transport activity of cationic amino acids, such as L-arginine and L-
CC       lysine (PubMed:33928121). {ECO:0000269|PubMed:11342143,
CC       ECO:0000269|PubMed:33928121, ECO:0000305|PubMed:11342143,
CC       ECO:0000305|PubMed:33928121}.
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DR   EMBL; AF305814; AAK43528.1; -; mRNA.
DR   EMBL; AF193836; AAK71508.1; -; mRNA.
DR   EMBL; AB055003; BAB84090.1; -; mRNA.
DR   EMBL; AK291168; BAF83857.1; -; mRNA.
DR   EMBL; CH471111; EAW57919.1; -; Genomic_DNA.
DR   EMBL; BC069819; AAH69819.1; -; mRNA.
DR   EMBL; BC101827; AAI01828.1; -; mRNA.
DR   EMBL; BC104913; AAI04914.1; -; mRNA.
DR   CCDS; CCDS8750.1; -.
DR   RefSeq; NP_001137296.1; NM_001143824.1.
DR   RefSeq; NP_060488.2; NM_018018.4.
DR   RefSeq; XP_005269054.1; XM_005268997.2.
DR   AlphaFoldDB; Q969I6; -.
DR   SMR; Q969I6; -.
DR   BioGRID; 120402; 2.
DR   IntAct; Q969I6; 1.
DR   STRING; 9606.ENSP00000266579; -.
DR   DrugBank; DB00174; Asparagine.
DR   TCDB; 2.A.18.6.17; the amino acid/auxin permease (aaap) family.
DR   GlyCosmos; Q969I6; 3 sites, No reported glycans.
DR   GlyGen; Q969I6; 3 sites.
DR   iPTMnet; Q969I6; -.
DR   PhosphoSitePlus; Q969I6; -.
DR   BioMuta; SLC38A4; -.
DR   DMDM; 74731046; -.
DR   MassIVE; Q969I6; -.
DR   PaxDb; 9606-ENSP00000389843; -.
DR   PeptideAtlas; Q969I6; -.
DR   ProteomicsDB; 75771; -.
DR   Antibodypedia; 13384; 70 antibodies from 22 providers.
DR   DNASU; 55089; -.
DR   Ensembl; ENST00000266579.9; ENSP00000266579.4; ENSG00000139209.16.
DR   Ensembl; ENST00000447411.5; ENSP00000389843.1; ENSG00000139209.16.
DR   GeneID; 55089; -.
DR   KEGG; hsa:55089; -.
DR   MANE-Select; ENST00000266579.9; ENSP00000266579.4; NM_018018.5; NP_060488.2.
DR   UCSC; uc001rpi.3; human.
DR   AGR; HGNC:14679; -.
DR   CTD; 55089; -.
DR   DisGeNET; 55089; -.
DR   GeneCards; SLC38A4; -.
DR   HGNC; HGNC:14679; SLC38A4.
DR   HPA; ENSG00000139209; Tissue enriched (liver).
DR   MIM; 608065; gene.
DR   neXtProt; NX_Q969I6; -.
DR   OpenTargets; ENSG00000139209; -.
DR   PharmGKB; PA37908; -.
DR   VEuPathDB; HostDB:ENSG00000139209; -.
DR   eggNOG; KOG1305; Eukaryota.
DR   GeneTree; ENSGT00940000158917; -.
DR   HOGENOM; CLU_009020_0_1_1; -.
DR   InParanoid; Q969I6; -.
DR   OMA; HNVHPIE; -.
DR   OrthoDB; 935269at2759; -.
DR   PhylomeDB; Q969I6; -.
DR   TreeFam; TF328787; -.
DR   PathwayCommons; Q969I6; -.
DR   Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR   SignaLink; Q969I6; -.
DR   BioGRID-ORCS; 55089; 17 hits in 1149 CRISPR screens.
DR   ChiTaRS; SLC38A4; human.
DR   GenomeRNAi; 55089; -.
DR   Pharos; Q969I6; Tbio.
DR   PRO; PR:Q969I6; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q969I6; Protein.
DR   Bgee; ENSG00000139209; Expressed in right lobe of liver and 106 other cell types or tissues.
DR   ExpressionAtlas; Q969I6; baseline and differential.
DR   GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0015655; F:alanine:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0005295; F:neutral L-amino acid:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR   GO; GO:1904273; P:L-alanine import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF222; SODIUM-COUPLED NEUTRAL AMINO ACID TRANSPORTER 4; 1.
DR   Pfam; PF01490; Aa_trans; 2.
DR   Genevisible; Q969I6; HS.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Cell projection; Disulfide bond;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..547
FT                   /note="Sodium-coupled neutral amino acid transporter 4"
FT                   /id="PRO_0000247860"
FT   TOPO_DOM        1..104
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..220
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..411
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        433..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        475..476
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        498..514
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   TRANSMEM        515..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        536..547
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:21917917"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            232
FT                   /note="Influences on amino acid transport capacity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1S9"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQ25"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21917917"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21917917"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        249..321
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1S9"
FT   VARIANT         29
FT                   /note="G -> R (in dbSNP:rs2429467)"
FT                   /id="VAR_048123"
FT   VARIANT         366
FT                   /note="T -> M (in dbSNP:rs11183610)"
FT                   /id="VAR_048124"
FT   VARIANT         446..547
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:29961568"
FT                   /id="VAR_083479"
SQ   SEQUENCE   547 AA;  60764 MW;  D47289AA386F3373 CRC64;
     MDPMELRNVN IEPDDESSSG ESAPDSYIGI GNSEKAAMSS QFANEDTESQ KFLTNGFLGK
     KKLADYADEH HPGTTSFGMS SFNLSNAIMG SGILGLSYAM ANTGIILFII MLLAVAILSL
     YSVHLLLKTA KEGGSLIYEK LGEKAFGWPG KIGAFVSITM QNIGAMSSYL FIIKYELPEV
     IRAFMGLEEN TGEWYLNGNY LIIFVSVGII LPLSLLKNLG YLGYTSGFSL TCMVFFVSVV
     IYKKFQIPCP LPVLDHSVGN LSFNNTLPMH VVMLPNNSES SDVNFMMDYT HRNPAGLDEN
     QAKGSLHDSG VEYEAHSDDK CEPKYFVFNS RTAYAIPILV FAFVCHPEVL PIYSELKDRS
     RRKMQTVSNI SITGMLVMYL LAALFGYLTF YGEVEDELLH AYSKVYTLDI PLLMVRLAVL
     VAVTLTVPIV LFPIRTSVIT LLFPKRPFSW IRHFLIAAVL IALNNVLVIL VPTIKYIFGF
     IGASSATMLI FILPAVFYLK LVKKETFRSP QKVGALIFLV VGIFFMIGSM ALIIIDWIYD
     PPNSKHH
//