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Protein

Sodium-coupled neutral amino acid transporter 2

Gene

Slc38a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier and in the supply of maternal nutrients to the fetus through the placenta.6 Publications

Enzyme regulationi

Inhibited by N-methyl-D-glucamine and choline.3 Publications

Kineticsi

  1. KM=0.53 mM for alanine (at pH 7.4)4 Publications
  2. KM=1.65 mM for glutamine (at pH 7.4)4 Publications
  3. KM=0.94 mM for serine (at pH 8.0)4 Publications
  4. KM=0.23 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.0 according to PubMed:10747860)4 Publications
  5. KM=0.14 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.0 according to PubMed:10859363)4 Publications
  6. KM=0.53 mM for 2-methylamino-isobutyric acid (MeAIB) (at pH 7.4)4 Publications

    GO - Molecular functioni

    GO - Biological processi

    • alanine transport Source: RGD
    • cellular response to amino acid starvation Source: RGD
    • cellular response to mechanical stimulus Source: RGD
    • cerebral cortex development Source: RGD
    • female pregnancy Source: RGD
    • glycine betaine transport Source: RGD
    • sodium ion transport Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Biological processi

    Amino-acid transport, Ion transport, Sodium transport, Symport, Transport

    Keywords - Ligandi

    Sodium

    Enzyme and pathway databases

    ReactomeiR-RNO-210500. Glutamate Neurotransmitter Release Cycle.
    R-RNO-352230. Amino acid transport across the plasma membrane.

    Protein family/group databases

    TCDBi2.A.18.6.4. the amino acid/auxin permease (aaap) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium-coupled neutral amino acid transporter 2
    Alternative name(s):
    Amino acid transporter A2
    Solute carrier family 38 member 2
    System A amino acid transporter 2
    System A transporter 1
    System N amino acid transporter 2
    Gene namesi
    Name:Slc38a2
    Synonyms:Ata2, Sa1, Sat2, Snat2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 7

    Organism-specific databases

    RGDi69420. Slc38a2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7676CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei77 – 9721HelicalSequence analysisAdd
    BLAST
    Topological domaini98 – 1025ExtracellularSequence analysis
    Transmembranei103 – 12321HelicalSequence analysisAdd
    BLAST
    Topological domaini124 – 15835CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei159 – 17921HelicalSequence analysisAdd
    BLAST
    Topological domaini180 – 1889ExtracellularSequence analysis
    Transmembranei189 – 20921HelicalSequence analysisAdd
    BLAST
    Topological domaini210 – 2178CytoplasmicSequence analysis
    Transmembranei218 – 23821HelicalSequence analysisAdd
    BLAST
    Topological domaini239 – 29052ExtracellularSequence analysisAdd
    BLAST
    Transmembranei291 – 31121HelicalSequence analysisAdd
    BLAST
    Topological domaini312 – 32716CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei328 – 34821HelicalSequence analysisAdd
    BLAST
    Topological domaini349 – 36921ExtracellularSequence analysisAdd
    BLAST
    Transmembranei370 – 39021HelicalSequence analysisAdd
    BLAST
    Topological domaini391 – 41121CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei412 – 43221HelicalSequence analysisAdd
    BLAST
    Topological domaini433 – 4342ExtracellularSequence analysis
    Transmembranei435 – 45521HelicalSequence analysisAdd
    BLAST
    Topological domaini456 – 47217CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei473 – 49321HelicalSequence analysisAdd
    BLAST
    Topological domaini494 – 50411ExtracellularSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • axon Source: RGD
    • brush border Source: RGD
    • dendrite Source: RGD
    • integral component of membrane Source: UniProtKB-KW
    • neuronal cell body Source: RGD
    • plasma membrane Source: RGD
    • sarcolemma Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi504 – 5041H → A: Modifies the transporter pH-sensitivity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 504504Sodium-coupled neutral amino acid transporter 2PRO_0000311372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei22 – 221PhosphoserineBy similarity
    Modified residuei55 – 551PhosphoserineBy similarity
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis

    Post-translational modificationi

    Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9JHE5.

    PTM databases

    iPTMnetiQ9JHE5.
    PhosphoSiteiQ9JHE5.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in skeletal muscle and adipose tissue (at protein level). Expressed by glutamatergic and GABAergic neurons together with astrocytes and other non-neuronal cells in the cerebral cortex (at protein level).5 Publications

    Inductioni

    Up-regulation upon amino acid deprivation results from both increased transcription and protein stabilization. Up-regulated by TGFB1.3 Publications

    Gene expression databases

    GenevisibleiQ9JHE5. RN.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000031532.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9696Regulates protein turnover upon amino acid deprivationAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1305. Eukaryota.
    COG0814. LUCA.
    GeneTreeiENSGT00760000119147.
    HOGENOMiHOG000013088.
    HOVERGENiHBG059571.
    InParanoidiQ9JHE5.
    KOiK14207.
    OMAiITHLLCA.
    OrthoDBiEOG7WHH9J.
    PhylomeDBiQ9JHE5.
    TreeFamiTF328787.

    Family and domain databases

    InterProiIPR013057. AA_transpt_TM.
    [Graphical view]
    PfamiPF01490. Aa_trans. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JHE5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKTEMGRFN ISPDEDSSSY SSNGDFNYSY PTKQAALKSH YVDVDPENQN
    60 70 80 90 100
    FLLESNLGKK KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG
    110 120 130 140 150
    IALFIILLTF VSIFSLYSVH LLLKTANEGG SLLYEQLGHK AYGLAGKLAA
    160 170 180 190 200
    SGSITMQNIG AMSSYLFIVK YELPLVIKAL MNIEDTNGLW YLNGDYLVLL
    210 220 230 240 250
    VSFVLILPLS LLRNLGYLGY TSGLSLLCMI FFLIVVICKK FQIPCPVEVA
    260 270 280 290 300
    LMANETVNGT FTQVALAALA SNSTAADTCR PRYFIFNSQT VYAVPILTFS
    310 320 330 340 350
    FVCHPAVLPI YEELKSRSRR RMMNVSKISF FAMFLMYLLA ALFGYLTFYE
    360 370 380 390 400
    HVESELLHTY SAIVGTDILL LVVRLAVLVA VTLTVPVVIF PIRSSVTHLL
    410 420 430 440 450
    CPTKEFSWFR HSVITVTILA FTNLLVIFVP TIRDIFGFIG ASAAAMLIFI
    460 470 480 490 500
    LPSAFYIKLV KKEPMRSVQK IGALCFLLSG VVVMIGSMGL IVLDWVHDAS

    AGGH
    Length:504
    Mass (Da):55,554
    Last modified:October 1, 2000 - v1
    Checksum:iF53022C07152648C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691G → S in AAF74195 (PubMed:10747860).Curated
    Sequence conflicti81 – 811S → T in AAF74195 (PubMed:10747860).Curated
    Sequence conflicti87 – 871S → N in AAF74195 (PubMed:10747860).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF249673 mRNA. Translation: AAF74195.1.
    AF173682 mRNA. Translation: AAF75589.2.
    AF273024 mRNA. Translation: AAF81796.1.
    RefSeqiNP_851604.1. NM_181090.2.
    UniGeneiRn.16393.

    Genome annotation databases

    EnsembliENSRNOT00000039002; ENSRNOP00000031532; ENSRNOG00000006305.
    GeneIDi29642.
    KEGGirno:29642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF249673 mRNA. Translation: AAF74195.1.
    AF173682 mRNA. Translation: AAF75589.2.
    AF273024 mRNA. Translation: AAF81796.1.
    RefSeqiNP_851604.1. NM_181090.2.
    UniGeneiRn.16393.

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000031532.

    Protein family/group databases

    TCDBi2.A.18.6.4. the amino acid/auxin permease (aaap) family.

    PTM databases

    iPTMnetiQ9JHE5.
    PhosphoSiteiQ9JHE5.

    Proteomic databases

    PaxDbiQ9JHE5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000039002; ENSRNOP00000031532; ENSRNOG00000006305.
    GeneIDi29642.
    KEGGirno:29642.

    Organism-specific databases

    CTDi54407.
    RGDi69420. Slc38a2.

    Phylogenomic databases

    eggNOGiKOG1305. Eukaryota.
    COG0814. LUCA.
    GeneTreeiENSGT00760000119147.
    HOGENOMiHOG000013088.
    HOVERGENiHBG059571.
    InParanoidiQ9JHE5.
    KOiK14207.
    OMAiITHLLCA.
    OrthoDBiEOG7WHH9J.
    PhylomeDBiQ9JHE5.
    TreeFamiTF328787.

    Enzyme and pathway databases

    ReactomeiR-RNO-210500. Glutamate Neurotransmitter Release Cycle.
    R-RNO-352230. Amino acid transport across the plasma membrane.

    Miscellaneous databases

    PROiQ9JHE5.

    Gene expression databases

    GenevisibleiQ9JHE5. RN.

    Family and domain databases

    InterProiIPR013057. AA_transpt_TM.
    [Graphical view]
    PfamiPF01490. Aa_trans. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of an amino acid transporter with functional characteristics and tissue expression pattern identical to that of system A."
      Sugawara M., Nakanishi T., Fei Y.-J., Huang W., Ganapathy M.E., Leibach F.H., Ganapathy V.
      J. Biol. Chem. 275:16473-16477(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Skeletal muscle.
    2. "A novel system A isoform mediating Na+/neutral amino acid cotransport."
      Yao D., Mackenzie B., Ming H., Varoqui H., Zhu H., Hediger M.A., Erickson J.D.
      J. Biol. Chem. 275:22790-22797(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Cerebellum.
    3. "Amino acid transport system A resembles system N in sequence but differs in mechanism."
      Reimer R.J., Chaudhry F.A., Gray A.T., Edwards R.H.
      Proc. Natl. Acad. Sci. U.S.A. 97:7715-7720(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    4. "Subcellular localization and adaptive up-regulation of the system A (SAT2) amino acid transporter in skeletal-muscle cells and adipocytes."
      Hyde R., Christie G.R., Litherland G.J., Hajduch E., Taylor P.M., Hundal H.S.
      Biochem. J. 355:563-568(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    5. "Transforming growth factor-beta 1 stimulates vascular smooth muscle cell L-proline transport by inducing system A amino acid transporter 2 (SAT2) gene expression."
      Ensenat D., Hassan S., Reyna S.V., Schafer A.I., Durante W.
      Biochem. J. 360:507-512(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TGFB1.
    6. "ATA2-mediated amino acid uptake following partial hepatectomy is regulated by redistribution to the plasma membrane."
      Freeman T.L., Thiele G.M., Tuma D.J., Machu T.K., Mailliard M.E.
      Arch. Biochem. Biophys. 400:215-222(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Insulin promotes the cell surface recruitment of the SAT2/ATA2 system A amino acid transporter from an endosomal compartment in skeletal muscle cells."
      Hyde R., Peyrollier K., Hundal H.S.
      J. Biol. Chem. 277:13628-13634(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Glutamine uptake by neurons: interaction of protons with system a transporters."
      Chaudhry F.A., Schmitz D., Reimer R.J., Larsson P., Gray A.T., Nicoll R., Kavanaugh M., Edwards R.H.
      J. Neurosci. 22:62-72(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "ATA2 is predominantly expressed as system A at the blood-brain barrier and acts as brain-to-blood efflux transport for L-proline."
      Takanaga H., Tokuda N., Ohtsuki S., Hosoya K., Terasaki T.
      Mol. Pharmacol. 61:1289-1296(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue."
      Baird F.E., Pinilla-Tenas J.J., Ogilvie W.L.J., Ganapathy V., Hundal H.S., Taylor P.M.
      Biochem. J. 397:369-375(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-504, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Localization of the Na(+)-coupled neutral amino acid transporter 2 in the cerebral cortex."
      Melone M., Varoqui H., Erickson J.D., Conti F.
      Neuroscience 140:281-292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. "Distinct sensor pathways in the hierarchical control of SNAT2, a putative amino acid transceptor, by amino acid availability."
      Hyde R., Cwiklinski E.L., MacAulay K., Taylor P.M., Hundal H.S.
      J. Biol. Chem. 282:19788-19798(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, INDUCTION.
    13. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
      Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
      Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiS38A2_RAT
    AccessioniPrimary (citable) accession number: Q9JHE5
    Secondary accession number(s): Q9JI88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: October 1, 2000
    Last modified: June 8, 2016
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.