S38A2_HUMAN
ID S38A2_HUMAN Reviewed; 506 AA.
AC Q96QD8; Q6IA88; Q6ZMG2; Q9HAV3; Q9NVA8; Q9P2G5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 2;
DE AltName: Full=Amino acid transporter A2;
DE AltName: Full=Protein 40-9-1;
DE AltName: Full=Solute carrier family 38 member 2;
DE AltName: Full=System A amino acid transporter 2;
DE AltName: Full=System A transporter 1;
DE AltName: Full=System N amino acid transporter 2;
GN Name=SLC38A2; Synonyms=ATA2, KIAA1382, SAT2, SNAT2;
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] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=10930503; DOI=10.1016/s0005-2736(00)00252-2;
RA Hatanaka T., Huang W., Wang H., Sugawara M., Prasad P.D., Leibach F.H.,
RA Ganapathy V.;
RT "Primary structure, functional characteristics and tissue expression
RT pattern of human ATA2, a subtype of amino acid transport system A.";
RL Biochim. Biophys. Acta 1467:1-6(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Powell J., Brock A.P., Hart I.R.;
RT "Expression studies of the human amino acid transporter, hATA2.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hepatoma, 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [10]
RP INDUCTION.
RX PubMed=14623874; DOI=10.1074/jbc.m310483200;
RA Palii S.S., Chen H., Kilberg M.S.;
RT "Transcriptional control of the human sodium-coupled neutral amino acid
RT transporter system A gene by amino acid availability is mediated by an
RT intronic element.";
RL J. Biol. Chem. 279:3463-3471(2004).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=15922329; DOI=10.1016/j.febslet.2005.05.002;
RA Bevilacqua E., Bussolati O., Dall'Asta V., Gaccioli F., Sala R.,
RA Gazzola G.C., Franchi-Gazzola R.;
RT "SNAT2 silencing prevents the osmotic induction of transport system A and
RT hinders cell recovery from hypertonic stress.";
RL FEBS Lett. 579:3376-3380(2005).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15561425; DOI=10.1016/j.neuroscience.2004.09.023;
RA Gonzalez-Gonzalez I.M., Cubelos B., Gimenez C., Zafra F.;
RT "Immunohistochemical localization of the amino acid transporter SNAT2 in
RT the rat brain.";
RL Neuroscience 130:61-73(2005).
RN [13]
RP INDUCTION.
RX PubMed=16621798; DOI=10.1074/jbc.m600341200;
RA Gaccioli F., Huang C.C., Wang C., Bevilacqua E., Franchi-Gazzola R.,
RA Gazzola G.C., Bussolati O., Snider M.D., Hatzoglou M.;
RT "Amino acid starvation induces the SNAT2 neutral amino acid transporter by
RT a mechanism that involves eukaryotic initiation factor 2alpha
RT phosphorylation and cap-independent translation.";
RL J. Biol. Chem. 281:17929-17940(2006).
RN [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16616430; DOI=10.1016/j.neuroscience.2006.02.042;
RA Melone M., Varoqui H., Erickson J.D., Conti F.;
RT "Localization of the Na(+)-coupled neutral amino acid transporter 2 in the
RT cerebral cortex.";
RL Neuroscience 140:281-292(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-12, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP 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 neutral amino acids and sodium ions with a stoichiometry of 1:1. May
CC function in the transport of amino acids at the blood-brain barrier and
CC in the supply of maternal nutrients to the fetus through the placenta.
CC {ECO:0000269|PubMed:10930503, ECO:0000269|PubMed:15922329}.
CC -!- ACTIVITY REGULATION: Inhibited by N-methyl-D-glucamine and probably
CC choline. {ECO:0000269|PubMed:10930503}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.0);
CC -!- INTERACTION:
CC Q96QD8; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-723083, EBI-10303987;
CC Q96QD8; Q99942: RNF5; NbExp=3; IntAct=EBI-723083, EBI-348482;
CC Q96QD8; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-723083, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15561425,
CC ECO:0000269|PubMed:16616430}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430}.
CC Note=Insulin promotes recruitment to the plasma membrane from a pool
CC localized in the trans-Golgi network or endosomes (By similarity).
CC Enriched in the somatodendritic compartment of neurons, it is also
CC detected at the axonal shaft but excluded from the nerve terminal.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96QD8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96QD8-2; Sequence=VSP_029553, VSP_029554;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Widely expressed in the
CC central nervous system with higher concentrations in caudal regions.
CC Expressed by glutamatergic and GABAergic neurons together with
CC astrocytes and other non-neuronal cells in the cerebral cortex (at
CC protein level). {ECO:0000269|PubMed:10930503,
CC ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430}.
CC -!- INDUCTION: Up-regulated upon hypertonic conditions and amino acid
CC deprivation. {ECO:0000269|PubMed:14623874, ECO:0000269|PubMed:15922329,
CC ECO:0000269|PubMed:16621798}.
CC -!- PTM: Polyubiquitination by NEDD4L regulates the degradation and the
CC activity of SLC38A2. {ECO:0000250}.
CC -!- MISCELLANEOUS: Depletion of SCL38A2 by siRNA prevents the recovery of
CC cells from hypertonic stress.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF259799; AAK38510.1; -; mRNA.
DR EMBL; AF298897; AAG24618.1; -; mRNA.
DR EMBL; AJ344099; CAC51434.1; -; mRNA.
DR EMBL; AB037803; BAA92620.2; -; mRNA.
DR EMBL; AK001700; BAA91846.1; -; mRNA.
DR EMBL; AK172784; BAD18765.1; ALT_INIT; mRNA.
DR EMBL; CR457267; CAG33548.1; -; mRNA.
DR EMBL; CH471111; EAW57900.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW57901.1; -; Genomic_DNA.
DR EMBL; BC040342; AAH40342.1; -; mRNA.
DR CCDS; CCDS76551.1; -. [Q96QD8-2]
DR CCDS; CCDS8749.1; -. [Q96QD8-1]
DR RefSeq; NP_001294865.1; NM_001307936.1. [Q96QD8-2]
DR RefSeq; NP_061849.2; NM_018976.4. [Q96QD8-1]
DR AlphaFoldDB; Q96QD8; -.
DR SMR; Q96QD8; -.
DR BioGRID; 119943; 131.
DR IntAct; Q96QD8; 40.
DR MINT; Q96QD8; -.
DR STRING; 9606.ENSP00000256689; -.
DR DrugBank; DB00174; Asparagine.
DR DrugBank; DB00130; L-Glutamine.
DR TCDB; 2.A.18.6.5; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q96QD8; 2 sites.
DR iPTMnet; Q96QD8; -.
DR MetOSite; Q96QD8; -.
DR PhosphoSitePlus; Q96QD8; -.
DR SwissPalm; Q96QD8; -.
DR BioMuta; SLC38A2; -.
DR DMDM; 162416227; -.
DR EPD; Q96QD8; -.
DR jPOST; Q96QD8; -.
DR MassIVE; Q96QD8; -.
DR MaxQB; Q96QD8; -.
DR PaxDb; Q96QD8; -.
DR PeptideAtlas; Q96QD8; -.
DR PRIDE; Q96QD8; -.
DR ProteomicsDB; 77855; -. [Q96QD8-1]
DR ProteomicsDB; 77856; -. [Q96QD8-2]
DR Antibodypedia; 13370; 139 antibodies from 23 providers.
DR DNASU; 54407; -.
DR Ensembl; ENST00000256689.10; ENSP00000256689.5; ENSG00000134294.14. [Q96QD8-1]
DR Ensembl; ENST00000612232.1; ENSP00000482873.1; ENSG00000134294.14. [Q96QD8-2]
DR GeneID; 54407; -.
DR KEGG; hsa:54407; -.
DR MANE-Select; ENST00000256689.10; ENSP00000256689.5; NM_018976.5; NP_061849.2.
DR UCSC; uc001rpg.4; human. [Q96QD8-1]
DR CTD; 54407; -.
DR DisGeNET; 54407; -.
DR GeneCards; SLC38A2; -.
DR HGNC; HGNC:13448; SLC38A2.
DR HPA; ENSG00000134294; Low tissue specificity.
DR MIM; 605180; gene.
DR neXtProt; NX_Q96QD8; -.
DR OpenTargets; ENSG00000134294; -.
DR PharmGKB; PA37773; -.
DR VEuPathDB; HostDB:ENSG00000134294; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000155486; -.
DR HOGENOM; CLU_009020_0_1_1; -.
DR InParanoid; Q96QD8; -.
DR OMA; QFWITAF; -.
DR PhylomeDB; Q96QD8; -.
DR TreeFam; TF328787; -.
DR PathwayCommons; Q96QD8; -.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q96QD8; -.
DR SIGNOR; Q96QD8; -.
DR BioGRID-ORCS; 54407; 107 hits in 1086 CRISPR screens.
DR ChiTaRS; SLC38A2; human.
DR GeneWiki; SLC38A2; -.
DR GenomeRNAi; 54407; -.
DR Pharos; Q96QD8; Tbio.
DR PRO; PR:Q96QD8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96QD8; protein.
DR Bgee; ENSG00000134294; Expressed in tibia and 215 other tissues.
DR ExpressionAtlas; Q96QD8; baseline and differential.
DR Genevisible; Q96QD8; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; IDA:ARUK-UCL.
DR GO; GO:0032328; P:alanine transport; IEA:Ensembl.
DR GO; GO:0003333; P:amino acid transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
DR GO; GO:1903841; P:cellular response to arsenite(3-); IMP:ARUK-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0006868; P:glutamine transport; ISS:ARUK-UCL.
DR GO; GO:0031460; P:glycine betaine transport; IEA:Ensembl.
DR GO; GO:0015825; P:L-serine transport; ISS:ARUK-UCL.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IPI:ARUK-UCL.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IPI:ARUK-UCL.
DR GO; GO:0080135; P:regulation of cellular response to stress; IMP:ARUK-UCL.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
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 Alternative splicing; Amino-acid transport; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..506
FT /note="Sodium-coupled neutral amino acid transporter 2"
FT /id="PRO_0000311369"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..96
FT /note="Regulates protein turnover upon amino acid
FT deprivation"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CFE6"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_029553"
FT VAR_SEQ 101..105
FT /note="IALFI -> MKQNL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_029554"
FT VARIANT 48
FT /note="N -> K (in dbSNP:rs11183450)"
FT /id="VAR_037235"
FT CONFLICT 156
FT /note="M -> V (in Ref. 3; CAC51434)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="H -> R (in Ref. 6; BAA91846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56026 MW; 125C70875793D031 CRC64;
MKKAEMGRFS ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN FLLESNLGKK
KYETEFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH
LLLKTANEGG SLLYEQLGYK AFGLVGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIQAL
TNIEDKTGLW YLNGNYLVLL VSLVVILPLS LFRNLGYLGY TSGLSLLCMV FFLIVVICKK
FQVPCPVEAA LIINETINTT LTQPTALVPA LSHNVTENDS CRPHYFIFNS QTVYAVPILI
FSFVCHPAVL PIYEELKDRS RRRMMNVSKI SFFAMFLMYL LAALFGYLTF YEHVESELLH
TYSSILGTDI LLLIVRLAVL MAVTLTVPVV IFPIRSSVTH LLCASKDFSW WRHSLITVSI
LAFTNLLVIF VPTIRDIFGF IGASAASMLI FILPSAFYIK LVKKEPMKSV QKIGALFFLL
SGVLVMTGSM ALIVLDWVHN APGGGH
