S38A1_HUMAN
ID S38A1_HUMAN Reviewed; 487 AA.
AC Q9H2H9; Q8NC61; Q8NCF8; Q96JX2; Q9H2Q2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 1;
DE AltName: Full=Amino acid transporter A1;
DE AltName: Full=N-system amino acid transporter 2;
DE AltName: Full=Solute carrier family 38 member 1;
DE AltName: Full=System A amino acid transporter 1;
DE AltName: Full=System N amino acid transporter 1;
GN Name=SLC38A1; Synonyms=ATA1, NAT2, SAT1, SNAT1;
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, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10891391; DOI=10.1006/bbrc.2000.3061;
RA Wang H., Huang W., Sugawara M., Devoe L.D., Leibach F.H., Prasad P.D.,
RA Ganapathy V.;
RT "Cloning and functional expression of ATA1, a subtype of amino acid
RT transporter A, from human placenta.";
RL Biochem. Biophys. Res. Commun. 273:1175-1179(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
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=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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12388062; DOI=10.1152/ajpcell.00253.2002;
RA Nelson D.M., Smith S.D., Furesz T.C., Sadovsky Y., Ganapathy V.,
RA Parvin C.A., Smith C.H.;
RT "Hypoxia reduces expression and function of system A amino acid
RT transporters in cultured term human trophoblasts.";
RL Am. J. Physiol. 284:C310-C315(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15054072; DOI=10.1093/cercor/bhh018;
RA Melone M., Quagliano F., Barbaresi P., Varoqui H., Erickson J.D., Conti F.;
RT "Localization of the glutamine transporter SNAT1 in rat cerebral cortex and
RT neighboring structures, with a note on its localization in human cortex.";
RL Cereb. Cortex 14:562-574(2004).
RN [9]
RP TISSUE SPECIFICITY.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INDUCTION BY LPS.
RX PubMed=16583402; DOI=10.1002/jnr.20855;
RA Ogura M., Nakamichi N., Takano K., Oikawa H., Kambe Y., Ohno Y.,
RA Taniura H., Yoneda Y.;
RT "Functional expression of a glutamine transporter responsive to down-
RT regulation by lipopolysaccharide through reduced promoter activity in
RT cultured rat neocortical astrocytes.";
RL J. Neurosci. Res. 83:1447-1460(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28; SER-52; THR-54
RP AND SER-56, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-54 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND THR-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
CC Mediates the saturable, pH-sensitive and electrogenic cotransport of
CC glutamine and sodium ions with a stoichiometry of 1:1. May also
CC transport small zwitterionic and aliphatic amino acids with a lower
CC affinity. May supply glutamatergic and GABAergic neurons with glutamine
CC which is required for the synthesis of the neurotransmitters glutamate
CC and GABA. {ECO:0000269|PubMed:10891391}.
CC -!- ACTIVITY REGULATION: Inhibited by potassium, choline ions and 2-
CC methylamino-isobutyric acid (MeAIB) (By similarity). Inhibited by
CC lithium and N-methyl-D-glucamine. {ECO:0000250,
CC ECO:0000269|PubMed:10891391}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=890 uM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.5)
CC {ECO:0000269|PubMed:10891391};
CC -!- INTERACTION:
CC Q9H2H9; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-9978441, EBI-19125216;
CC Q9H2H9; Q13520: AQP6; NbExp=3; IntAct=EBI-9978441, EBI-13059134;
CC Q9H2H9; O95393: BMP10; NbExp=3; IntAct=EBI-9978441, EBI-3922513;
CC Q9H2H9; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-9978441, EBI-12062109;
CC Q9H2H9; P11912: CD79A; NbExp=6; IntAct=EBI-9978441, EBI-7797864;
CC Q9H2H9; Q969F0: FATE1; NbExp=6; IntAct=EBI-9978441, EBI-743099;
CC Q9H2H9; O15552: FFAR2; NbExp=3; IntAct=EBI-9978441, EBI-2833872;
CC Q9H2H9; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-9978441, EBI-13345167;
CC Q9H2H9; O15529: GPR42; NbExp=3; IntAct=EBI-9978441, EBI-18076404;
CC Q9H2H9; Q14416: GRM2; NbExp=3; IntAct=EBI-9978441, EBI-10232876;
CC Q9H2H9; P24593: IGFBP5; NbExp=4; IntAct=EBI-9978441, EBI-720480;
CC Q9H2H9; Q01638-2: IL1RL1; NbExp=3; IntAct=EBI-9978441, EBI-12838366;
CC Q9H2H9; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-9978441, EBI-16427978;
CC Q9H2H9; O15173: PGRMC2; NbExp=3; IntAct=EBI-9978441, EBI-1050125;
CC Q9H2H9; Q01453: PMP22; NbExp=3; IntAct=EBI-9978441, EBI-2845982;
CC Q9H2H9; Q9NS64: RPRM; NbExp=3; IntAct=EBI-9978441, EBI-1052363;
CC Q9H2H9; O95968: SCGB1D1; NbExp=3; IntAct=EBI-9978441, EBI-12825395;
CC Q9H2H9; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-9978441, EBI-17247926;
CC Q9H2H9; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-9978441, EBI-749270;
CC Q9H2H9; Q14973: SLC10A1; NbExp=3; IntAct=EBI-9978441, EBI-3923031;
CC Q9H2H9; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-9978441, EBI-18159983;
CC Q9H2H9; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-9978441, EBI-12808018;
CC Q9H2H9; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-9978441, EBI-741850;
CC Q9H2H9; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-9978441, EBI-17280858;
CC Q9H2H9; P0DN84: STRIT1; NbExp=3; IntAct=EBI-9978441, EBI-12200293;
CC Q9H2H9; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-9978441, EBI-2852148;
CC Q9H2H9; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-9978441, EBI-11724433;
CC Q9H2H9; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-9978441, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15054072};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15054072}.
CC Note=Restricted to the somatodendritic compartment of neurons. Found in
CC the cellular processes of neurons in the developing brain (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex by pyramidal and
CC GABAergic neurons, astrocytes and other non-neuronal cells (at protein
CC level). Expressed in placenta, heart, lung, skeletal muscle, spleen,
CC stomach and testis. {ECO:0000269|PubMed:10891391,
CC ECO:0000269|PubMed:12388062, ECO:0000269|PubMed:15054072,
CC ECO:0000269|PubMed:16148032}.
CC -!- INDUCTION: Down-regulated by bacterial lipopolysaccharides (LPS) in
CC glial cells. Down-regulated upon hypoxia. {ECO:0000269|PubMed:12388062,
CC ECO:0000269|PubMed:16583402}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44546.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF271070; AAG39354.1; -; mRNA.
DR EMBL; AF247166; AAG44546.1; ALT_FRAME; mRNA.
DR EMBL; AK027825; BAB55394.1; -; mRNA.
DR EMBL; AK074758; BAC11186.1; ALT_INIT; mRNA.
DR EMBL; AK074949; BAC11310.1; -; mRNA.
DR EMBL; CH471111; EAW57895.1; -; Genomic_DNA.
DR EMBL; BC010620; AAH10620.1; -; mRNA.
DR CCDS; CCDS41774.1; -.
DR PIR; JC7328; JC7328.
DR RefSeq; NP_001070952.1; NM_001077484.1.
DR RefSeq; NP_001265316.1; NM_001278387.1.
DR RefSeq; NP_001265317.1; NM_001278388.1.
DR RefSeq; NP_001265318.1; NM_001278389.1.
DR RefSeq; NP_109599.3; NM_030674.3.
DR AlphaFoldDB; Q9H2H9; -.
DR SMR; Q9H2H9; -.
DR BioGRID; 123509; 126.
DR IntAct; Q9H2H9; 93.
DR MINT; Q9H2H9; -.
DR STRING; 9606.ENSP00000449756; -.
DR DrugBank; DB00174; Asparagine.
DR DrugBank; DB00130; L-Glutamine.
DR TCDB; 2.A.18.6.14; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q9H2H9; 2 sites.
DR iPTMnet; Q9H2H9; -.
DR PhosphoSitePlus; Q9H2H9; -.
DR SwissPalm; Q9H2H9; -.
DR BioMuta; SLC38A1; -.
DR DMDM; 74733561; -.
DR EPD; Q9H2H9; -.
DR jPOST; Q9H2H9; -.
DR MassIVE; Q9H2H9; -.
DR MaxQB; Q9H2H9; -.
DR PaxDb; Q9H2H9; -.
DR PeptideAtlas; Q9H2H9; -.
DR PRIDE; Q9H2H9; -.
DR ProteomicsDB; 80552; -.
DR ABCD; Q9H2H9; 2 sequenced antibodies.
DR Antibodypedia; 7400; 199 antibodies from 29 providers.
DR DNASU; 81539; -.
DR Ensembl; ENST00000398637.10; ENSP00000381634.4; ENSG00000111371.16.
DR Ensembl; ENST00000439706.5; ENSP00000398142.1; ENSG00000111371.16.
DR Ensembl; ENST00000546893.5; ENSP00000447853.1; ENSG00000111371.16.
DR Ensembl; ENST00000549049.5; ENSP00000449607.1; ENSG00000111371.16.
DR GeneID; 81539; -.
DR KEGG; hsa:81539; -.
DR MANE-Select; ENST00000398637.10; ENSP00000381634.4; NM_030674.4; NP_109599.3.
DR UCSC; uc001rpb.5; human.
DR CTD; 81539; -.
DR DisGeNET; 81539; -.
DR GeneCards; SLC38A1; -.
DR HGNC; HGNC:13447; SLC38A1.
DR HPA; ENSG00000111371; Low tissue specificity.
DR MIM; 608490; gene.
DR neXtProt; NX_Q9H2H9; -.
DR OpenTargets; ENSG00000111371; -.
DR PharmGKB; PA37772; -.
DR VEuPathDB; HostDB:ENSG00000111371; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000160716; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q9H2H9; -.
DR OMA; LTQRIWA; -.
DR PhylomeDB; Q9H2H9; -.
DR TreeFam; TF328787; -.
DR PathwayCommons; Q9H2H9; -.
DR Reactome; R-HSA-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q9H2H9; -.
DR SIGNOR; Q9H2H9; -.
DR BioGRID-ORCS; 81539; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; SLC38A1; human.
DR GeneWiki; SLC38A1; -.
DR GenomeRNAi; 81539; -.
DR Pharos; Q9H2H9; Tbio.
DR PRO; PR:Q9H2H9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H2H9; protein.
DR Bgee; ENSG00000111371; Expressed in lateral nuclear group of thalamus and 200 other tissues.
DR ExpressionAtlas; Q9H2H9; baseline and differential.
DR Genevisible; Q9H2H9; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0098591; C:external side of apical plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; NAS:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; ISS:ARUK-UCL.
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:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0006868; P:glutamine transport; IBA:GO_Central.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; ISS:ARUK-UCL.
DR GO; GO:0001504; P:neurotransmitter uptake; TAS:Reactome.
DR GO; GO:0015804; P:neutral amino acid transport; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..487
FT /note="Sodium-coupled neutral amino acid transporter 1"
FT /id="PRO_0000310475"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2P7"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2P7"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 107
FT /note="L -> P (in Ref. 3; BAB55394)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="F -> V (in Ref. 4; BAC11310)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="V -> D (in Ref. 2; AAG44546)"
FT /evidence="ECO:0000305"
FT CONFLICT 483..484
FT /note="SD -> NG (in Ref. 2; AAG44546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 54048 MW; 5CBC96880D7BDE03 CRC64;
MMHFKSGLEL TELQNMTVPE DDNISNDSND FTEVENGQIN SKFISDRESR RSLTNSHLEK
KKCDEYIPGT TSLGMSVFNL SNAIMGSGIL GLAFALANTG ILLFLVLLTS VTLLSIYSIN
LLLICSKETG CMVYEKLGEQ VFGTTGKFVI FGATSLQNTG AMLSYLFIVK NELPSAIKFL
MGKEETFSAW YVDGRVLVVI VTFGIILPLC LLKNLGYLGY TSGFSLSCMV FFLIVVIYKK
FQIPCIVPEL NSTISANSTN ADTCTPKYVT FNSKTVYALP TIAFAFVCHP SVLPIYSELK
DRSQKKMQMV SNISFFAMFV MYFLTAIFGY LTFYDNVQSD LLHKYQSKDD ILILTVRLAV
IVAVILTVPV LFFTVRSSLF ELAKKTKFNL CRHTVVTCIL LVVINLLVIF IPSMKDIFGV
VGVTSANMLI FILPSSLYLK ITDQDGDKGT QRIWAALFLG LGVLFSLVSI PLVIYDWACS
SSSDEGH
