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Protein

Sodium-dependent neutral amino acid transporter B(0)AT1

Gene

Slc6a19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transporter that mediates epithelial resorption of neutral amino acids across the apical membrane of epithelial cells in the kidney and intestine. It appears that leucine is the preferred substrate, but all large neutral non-aromatic L-amino acids bind to this transporter. Uptake of leucine is sodium-dependent. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent.1 Publication

Kineticsi

Vmax for leucine is about twice the value of Vmax for glutamine, and three times the value of Vmax for phenylalanine. KM and Vmax values are complex functions of the concentration of substrate (L-amino acid) and cosubstrate (Na+) and the membrane potential.

  1. KM=630 µM for leucine1 Publication
  2. KM=522 µM for glutamine1 Publication
  3. KM=589 µM for phenylalanine1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • neutral amino acid transport Source: MGI
    • response to nutrient Source: Ensembl
    Complete GO annotation...

    Keywords - Biological processi

    Amino-acid transport, Symport, Transport

    Enzyme and pathway databases

    ReactomeiR-MMU-352230. Amino acid transport across the plasma membrane.
    R-MMU-442660. Na+/Cl- dependent neurotransmitter transporters.

    Protein family/group databases

    TCDBi2.A.22.6.3. the neurotransmitter:sodium symporter (nss) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium-dependent neutral amino acid transporter B(0)AT1
    Alternative name(s):
    Solute carrier family 6 member 19
    System B(0) neutral amino acid transporter AT1
    Gene namesi
    Name:Slc6a19
    Synonyms:B0at1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 13

    Organism-specific databases

    MGIiMGI:1921588. Slc6a19.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4141CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei42 – 6221Helical; Name=1Sequence analysisAdd
    BLAST
    Topological domaini63 – 675ExtracellularSequence analysis
    Transmembranei68 – 8821Helical; Name=2Sequence analysisAdd
    BLAST
    Topological domaini89 – 11931CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei120 – 14021Helical; Name=3Sequence analysisAdd
    BLAST
    Topological domaini141 – 19252ExtracellularSequence analysisAdd
    BLAST
    Transmembranei193 – 21321Helical; Name=4Sequence analysisAdd
    BLAST
    Topological domaini214 – 2218CytoplasmicSequence analysis
    Transmembranei222 – 24221Helical; Name=5Sequence analysisAdd
    BLAST
    Topological domaini243 – 26826ExtracellularSequence analysisAdd
    BLAST
    Transmembranei269 – 28921Helical; Name=6Sequence analysisAdd
    BLAST
    Topological domaini290 – 30415CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei305 – 32521Helical; Name=7Sequence analysisAdd
    BLAST
    Topological domaini326 – 41388ExtracellularSequence analysisAdd
    BLAST
    Transmembranei414 – 43421Helical; Name=8Sequence analysisAdd
    BLAST
    Topological domaini435 – 45622CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei457 – 47721Helical; Name=9Sequence analysisAdd
    BLAST
    Topological domaini478 – 48710ExtracellularSequence analysis
    Transmembranei488 – 50821Helical; Name=10Sequence analysisAdd
    BLAST
    Topological domaini509 – 53123CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei532 – 55221Helical; Name=11Sequence analysisAdd
    BLAST
    Topological domaini553 – 58129ExtracellularSequence analysisAdd
    BLAST
    Transmembranei582 – 60221Helical; Name=12Sequence analysisAdd
    BLAST
    Topological domaini603 – 63432CytoplasmicSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • brush border membrane Source: MGI
    • extracellular exosome Source: MGI
    • integral component of plasma membrane Source: GO_Central
    • plasma membrane Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 634634Sodium-dependent neutral amino acid transporter B(0)AT1PRO_0000214810Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171PhosphoserineCombined sources
    Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence analysis
    Modified residuei627 – 6271PhosphoserineCombined sources

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9D687.
    PaxDbiQ9D687.
    PRIDEiQ9D687.

    PTM databases

    iPTMnetiQ9D687.
    PhosphoSiteiQ9D687.

    Expressioni

    Tissue specificityi

    Expression observed in kidney, small intestine, and skin. Expression not observed in other organs, such as lung, skeletal muscle, brain, liver and pancreas. In kidney, expression is localized in the renal cortex but not in the medulla. Substantial amounts of expression in the proximal tubules. The distal nephron segments and the glomeruli are consistently negative. In the small intestine, expression is exclusively localized in villus enterocytes. High resolution of the hybridization-positive villi reveals a gradient of expression with the highest levels in apical cells. Not detected in crypt cells or in any other cell types of the small intestine.1 Publication

    Gene expression databases

    BgeeiQ9D687.
    ExpressionAtlasiQ9D687. baseline and differential.
    GenevisibleiQ9D687. MM.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-38102N.
    IntActiQ9D687. 2 interactions.
    MINTiMINT-4127196.
    STRINGi10090.ENSMUSP00000022048.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D687.
    SMRiQ9D687. Positions 32-329, 392-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3659. Eukaryota.
    COG0733. LUCA.
    GeneTreeiENSGT00760000119044.
    HOGENOMiHOG000116406.
    HOVERGENiHBG071421.
    InParanoidiQ9D687.
    KOiK05334.
    OMAiGYVDECA.
    OrthoDBiEOG793B71.
    PhylomeDBiQ9D687.
    TreeFamiTF343812.

    Family and domain databases

    InterProiIPR000175. Na/ntran_symport.
    IPR002438. Na/ntran_symport_orphan.
    [Graphical view]
    PANTHERiPTHR11616. PTHR11616. 2 hits.
    PfamiPF00209. SNF. 1 hit.
    [Graphical view]
    PRINTSiPR00176. NANEUSMPORT.
    PR01206. ORPHTRNSPORT.
    PROSITEiPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
    PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9D687-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVRLVLPNPG LEERIPSLDE LEVIEKEEAG SRPKWDNKAQ YMLTCVGFCV
    60 70 80 90 100
    GLGNVWRFPY LCQSHGGGAF MIPFLILLVF EGIPLLYLEF AIGQRLRKGS
    110 120 130 140 150
    MGVWSSIHPA LKGIGIASMF VSFMVGLYYN TIIAWVMWYF FNSFQEPLPW
    160 170 180 190 200
    SECPLNQNQT GYVEECAKSS SVDYFWYRET LNISTSISDS GSIQWWILLC
    210 220 230 240 250
    LTCAWSVLYV CIIRGIETTG KAVYITSTLP YVVLTIFLIR GLTLKGATNG
    260 270 280 290 300
    IVFLFTPNIT ELSNPNTWLD AGAQVFYSFS LAFGGLISFS SYNSVHNNCE
    310 320 330 340 350
    MDSVIVSVIN GFTSVYAATV VYSIIGFRAT ERFDDCVNTN ILTLINGFDL
    360 370 380 390 400
    PEGNVTSENF EAYQQWCNAT NPQAYAQLKF QTCDINSFLS EGVEGTGLAF
    410 420 430 440 450
    IVFTEAITKM PVSPLWSVLF FIMLFCLGLS SMFGNMEGVV VPLQDLNITP
    460 470 480 490 500
    KKWPKELLTG LICLGTYLIA FIFTLNSGQY WLSLLDSFAG SIPLLIIAFC
    510 520 530 540 550
    EMFAVVYVYG VDRFNKDIEF MIGHKPNIFW QVTWRVVSPL IMLVIFLFFF
    560 570 580 590 600
    VIEVNKTLMY SIWDPNYEEF PKSQKIPYPN WVYAVVVTVA GVPCLSIPCF
    610 620 630
    AIYKFIRNCC QKSDDHHGLV NTLSTASVNG DLKN
    Length:634
    Mass (Da):71,367
    Last modified:June 1, 2001 - v1
    Checksum:i433EB23C97E9FE5B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ633679 mRNA. Translation: CAG17898.1.
    AK014544 mRNA. Translation: BAB29422.1.
    AK028784 mRNA. Translation: BAC26119.1.
    CCDSiCCDS26634.1.
    RefSeqiNP_083154.1. NM_028878.3.
    UniGeneiMm.271635.

    Genome annotation databases

    EnsembliENSMUST00000022048; ENSMUSP00000022048; ENSMUSG00000021565.
    GeneIDi74338.
    KEGGimmu:74338.
    UCSCiuc007rdy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ633679 mRNA. Translation: CAG17898.1.
    AK014544 mRNA. Translation: BAB29422.1.
    AK028784 mRNA. Translation: BAC26119.1.
    CCDSiCCDS26634.1.
    RefSeqiNP_083154.1. NM_028878.3.
    UniGeneiMm.271635.

    3D structure databases

    ProteinModelPortaliQ9D687.
    SMRiQ9D687. Positions 32-329, 392-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-38102N.
    IntActiQ9D687. 2 interactions.
    MINTiMINT-4127196.
    STRINGi10090.ENSMUSP00000022048.

    Protein family/group databases

    TCDBi2.A.22.6.3. the neurotransmitter:sodium symporter (nss) family.

    PTM databases

    iPTMnetiQ9D687.
    PhosphoSiteiQ9D687.

    Proteomic databases

    MaxQBiQ9D687.
    PaxDbiQ9D687.
    PRIDEiQ9D687.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000022048; ENSMUSP00000022048; ENSMUSG00000021565.
    GeneIDi74338.
    KEGGimmu:74338.
    UCSCiuc007rdy.1. mouse.

    Organism-specific databases

    CTDi340024.
    MGIiMGI:1921588. Slc6a19.

    Phylogenomic databases

    eggNOGiKOG3659. Eukaryota.
    COG0733. LUCA.
    GeneTreeiENSGT00760000119044.
    HOGENOMiHOG000116406.
    HOVERGENiHBG071421.
    InParanoidiQ9D687.
    KOiK05334.
    OMAiGYVDECA.
    OrthoDBiEOG793B71.
    PhylomeDBiQ9D687.
    TreeFamiTF343812.

    Enzyme and pathway databases

    ReactomeiR-MMU-352230. Amino acid transport across the plasma membrane.
    R-MMU-442660. Na+/Cl- dependent neurotransmitter transporters.

    Miscellaneous databases

    PROiQ9D687.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9D687.
    ExpressionAtlasiQ9D687. baseline and differential.
    GenevisibleiQ9D687. MM.

    Family and domain databases

    InterProiIPR000175. Na/ntran_symport.
    IPR002438. Na/ntran_symport_orphan.
    [Graphical view]
    PANTHERiPTHR11616. PTHR11616. 2 hits.
    PfamiPF00209. SNF. 1 hit.
    [Graphical view]
    PRINTSiPR00176. NANEUSMPORT.
    PR01206. ORPHTRNSPORT.
    PROSITEiPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
    PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of mouse amino acid transport system B(0), a neutral amino acid transporter related to Hartnup disorder."
      Broeer A., Klingel K., Kowalczuk S., Rasko J.E.J., Cavanaugh J.A., Broeer S.
      J. Biol. Chem. 279:24467-24476(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NMRI.
      Tissue: Kidney.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Skin.
    3. "Characterization of mouse amino acid transporter B(0)AT1 (Slc6a19)."
      Boehmer C., Broeer A., Munzinger M., Kowalczuk S., Rasko J.E.J., Lang F., Broeer S.
      Biochem. J. 389:745-751(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Kidney.

    Entry informationi

    Entry nameiS6A19_MOUSE
    AccessioniPrimary (citable) accession number: Q9D687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 1, 2001
    Last modified: July 6, 2016
    This is version 108 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. 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.