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Q92536

- YLAT2_HUMAN

UniProt

Q92536 - YLAT2_HUMAN

Protein

Y+L amino acid transporter 2

Gene

SLC7A6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Also acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L-arginine in monocytes. Reduces uptake of ornithine in retinal pigment epithelial (RPE) cells.8 Publications

    Enzyme regulationi

    Arginine transport is strongly inhibited by lysine, glutamate, leucine, glutamine, methionine and histidine, in the presence of Na+. Also inhibited by protein kinase C (PKC) and treatment with phorbol-12-myristate-13-acetate (PMA). Mutual inhibition is observed when leucine or glutamine is used as substrate. Inhibition of arginine and leucine uptake also occurs when SLC3A2/4F2hc is either truncated at its C-terminus or mutated at critical residues within the terminal 15 amino acids.

    Kineticsi

    1. KM=295 µM for glutamine (in the presence of NaCl)1 Publication
    2. KM=236 µM for leucine (in the presence of NaCl)1 Publication
    3. KM=120 µM for arginine (in the presence of NaCl)1 Publication
    4. KM=138 µM for arginine (in the absence of NaCl)1 Publication

    GO - Molecular functioni

    1. amino acid transmembrane transporter activity Source: ProtInc
    2. antiporter activity Source: UniProtKB-KW

    GO - Biological processi

    1. amino acid transport Source: Reactome
    2. blood coagulation Source: Reactome
    3. cellular amino acid metabolic process Source: ProtInc
    4. ion transport Source: Reactome
    5. leukocyte migration Source: Reactome
    6. protein complex assembly Source: ProtInc
    7. transmembrane transport Source: Reactome
    8. transport Source: ProtInc

    Keywords - Biological processi

    Amino-acid transport, Antiport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000103064-MONOMER.
    ReactomeiREACT_12560. Basigin interactions.
    REACT_13796. Amino acid transport across the plasma membrane.
    SABIO-RKQ92536.

    Protein family/group databases

    TCDBi2.A.3.8.23. the amino acid-polyamine-organocation (apc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Y+L amino acid transporter 2
    Alternative name(s):
    Cationic amino acid transporter, y+ system
    Solute carrier family 7 member 6
    y(+)L-type amino acid transporter 2
    Short name:
    Y+LAT2
    Short name:
    y+LAT-2
    Gene namesi
    Name:SLC7A6Imported
    Synonyms:KIAA0245Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11064. SLC7A6.

    Subcellular locationi

    Basolateral cell membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35924.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515Y+L amino acid transporter 2PRO_0000341477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301PhosphoserineBy similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ92536.
    PaxDbiQ92536.
    PRIDEiQ92536.

    PTM databases

    PhosphoSiteiQ92536.

    Expressioni

    Tissue specificityi

    Expressed in normal fibroblasts and those from LPI patients. Also expressed in HUVECs, monocytes, RPE cells, and various carcinoma cell lines.6 Publications

    Gene expression databases

    ArrayExpressiQ92536.
    BgeeiQ92536.
    CleanExiHS_SLC7A6.
    GenevestigatoriQ92536.

    Organism-specific databases

    HPAiHPA050713.

    Interactioni

    Subunit structurei

    Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc.2 Publications

    Protein-protein interaction databases

    IntActiQ92536. 1 interaction.
    STRINGi9606.ENSP00000219343.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92536.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini66 – 7813ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini100 – 11415CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini136 – 16732ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini189 – 1946CytoplasmicSequence Analysis
    Topological domaini216 – 23520ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini257 – 26610CytoplasmicSequence Analysis
    Topological domaini288 – 31124ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini333 – 36331CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini385 – 3851ExtracellularSequence Analysis
    Topological domaini407 – 42519CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini447 – 4515ExtracellularSequence Analysis
    Topological domaini473 – 51543CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei45 – 6521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei79 – 9921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei115 – 13521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei195 – 21521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei236 – 25621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei267 – 28721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei312 – 33221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei364 – 38421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei386 – 40621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei426 – 44621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei452 – 47221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0531.
    HOGENOMiHOG000098892.
    HOVERGENiHBG000476.
    InParanoidiQ92536.
    KOiK13872.
    OMAiLEELIMR.
    OrthoDBiEOG73BVCR.
    PhylomeDBiQ92536.
    TreeFamiTF313355.

    Family and domain databases

    InterProiIPR002293. AA/rel_permease1.
    [Graphical view]
    PANTHERiPTHR11785. PTHR11785. 1 hit.
    PfamiPF13520. AA_permease_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006060. AA_transporter. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q92536-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAREPGRPT PTYHLVPNTS QSQVEEDVSS PPQRSSETMQ LKKEISLLNG    50
    VSLVVGNMIG SGIFVSPKGV LVHTASYGMS LIVWAIGGLF SVVGALCYAE 100
    LGTTITKSGA SYAYILEAFG GFIAFIRLWV SLLVVEPTGQ AIIAITFANY 150
    IIQPSFPSCD PPYLACRLLA AACICLLTFV NCAYVKWGTR VQDTFTYAKV 200
    VALIAIIVMG LVKLCQGHSE HFQDAFEGSS WDMGNLSLAL YSALFSYSGW 250
    DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNISDVLS 300
    SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG 350
    HLPDLLSMIH IERFTPIPAL LFNCTMALIY LIVEDVFQLI NYFSFSYWFF 400
    VGLSVVGQLY LRWKEPKRPR PLKLSVFFPI VFCICSVFLV IVPLFTDTIN 450
    SLIGIGIALS GVPFYFMGVY LPESRRPLFI RNVLAAITRG TQQLCFCVLT 500
    ELDVAEEKKD ERKTD 515
    Length:515
    Mass (Da):56,828
    Last modified:June 10, 2008 - v3
    Checksum:i4E92F6E1972351A9
    GO

    Sequence cautioni

    The sequence BAA13376.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81R → G in CAH18146. (PubMed:17974005)Curated
    Sequence conflicti388 – 3881Q → R in CAH18146. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87432 mRNA. Translation: BAA13376.2. Different initiation.
    CR749291 mRNA. Translation: CAH18146.1.
    CH471092 Genomic DNA. Translation: EAW83219.1.
    BC028216 mRNA. Translation: AAH28216.1.
    CCDSiCCDS32470.1.
    RefSeqiNP_001070253.1. NM_001076785.2.
    NP_003974.3. NM_003983.5.
    UniGeneiHs.679580.

    Genome annotation databases

    EnsembliENST00000219343; ENSP00000219343; ENSG00000103064.
    ENST00000566454; ENSP00000455064; ENSG00000103064.
    GeneIDi9057.
    KEGGihsa:9057.
    UCSCiuc002evt.2. human.

    Polymorphism databases

    DMDMi190462822.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87432 mRNA. Translation: BAA13376.2 . Different initiation.
    CR749291 mRNA. Translation: CAH18146.1 .
    CH471092 Genomic DNA. Translation: EAW83219.1 .
    BC028216 mRNA. Translation: AAH28216.1 .
    CCDSi CCDS32470.1.
    RefSeqi NP_001070253.1. NM_001076785.2.
    NP_003974.3. NM_003983.5.
    UniGenei Hs.679580.

    3D structure databases

    ProteinModelPortali Q92536.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q92536. 1 interaction.
    STRINGi 9606.ENSP00000219343.

    Protein family/group databases

    TCDBi 2.A.3.8.23. the amino acid-polyamine-organocation (apc) family.

    PTM databases

    PhosphoSitei Q92536.

    Polymorphism databases

    DMDMi 190462822.

    Proteomic databases

    MaxQBi Q92536.
    PaxDbi Q92536.
    PRIDEi Q92536.

    Protocols and materials databases

    DNASUi 9057.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219343 ; ENSP00000219343 ; ENSG00000103064 .
    ENST00000566454 ; ENSP00000455064 ; ENSG00000103064 .
    GeneIDi 9057.
    KEGGi hsa:9057.
    UCSCi uc002evt.2. human.

    Organism-specific databases

    CTDi 9057.
    GeneCardsi GC16P068298.
    H-InvDB HIX0013172.
    HGNCi HGNC:11064. SLC7A6.
    HPAi HPA050713.
    MIMi 605641. gene.
    neXtProti NX_Q92536.
    PharmGKBi PA35924.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0531.
    HOGENOMi HOG000098892.
    HOVERGENi HBG000476.
    InParanoidi Q92536.
    KOi K13872.
    OMAi LEELIMR.
    OrthoDBi EOG73BVCR.
    PhylomeDBi Q92536.
    TreeFami TF313355.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000103064-MONOMER.
    Reactomei REACT_12560. Basigin interactions.
    REACT_13796. Amino acid transport across the plasma membrane.
    SABIO-RK Q92536.

    Miscellaneous databases

    GeneWikii SLC7A6.
    GenomeRNAii 9057.
    NextBioi 33939.
    PROi Q92536.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92536.
    Bgeei Q92536.
    CleanExi HS_SLC7A6.
    Genevestigatori Q92536.

    Family and domain databases

    InterProi IPR002293. AA/rel_permease1.
    [Graphical view ]
    PANTHERi PTHR11785. PTHR11785. 1 hit.
    Pfami PF13520. AA_permease_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006060. AA_transporter. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance."
      Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J., Shi Y.-B., Zorzano A., Palacin M.
      J. Biol. Chem. 273:32437-32445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Myoblast1 Publication.
    2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrowImported.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Salivary gland.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: LeukocyteImported.
    6. "Arginine transport through system y(+)L in cultured human fibroblasts: normal phenotype of cells from LPI subjects."
      Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G., Sperandeo M.P., Andria G., Gazzola G.C.
      Am. J. Physiol. 279:C1829-C1837(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine."
      Broeer A., Wagner C.A., Lang F., Broeer S.
      Biochem. J. 349:787-795(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION.
    8. "Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains."
      Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V., Lang F., Broeer S.
      Biochem. J. 355:725-731(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Two-way arginine transport in human endothelial cells: TNF-alpha stimulation is restricted to system y(+)."
      Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A., Bussolati O., Gazzola G.C., Dall'Asta V.
      Am. J. Physiol. 282:C134-C143(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Nitric oxide synthesis requires activity of the cationic and neutral amino acid transport system y+L in human umbilical vein endothelium."
      Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.
      Exp. Physiol. 88:699-710(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "INFgamma stimulates arginine transport through system y+L in human monocytes."
      Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E., Gazzola G.C., Dall'Asta V.
      FEBS Lett. 571:177-181(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. "A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity: implications for the molecular pathogenesis of lysinuric protein intolerance."
      Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C., Taglialatela M., Andria G., Sebastio G.
      Eur. J. Hum. Genet. 13:628-634(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2 light-chain dysfunction."
      Chubb S., Kingsland A.L., Broeer A., Broeer S.
      Mol. Membr. Biol. 23:255-267(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INHIBITION.
    14. "Activation of classical protein kinase C decreases transport via systems y+ and y+L."
      Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.
      Am. J. Physiol. 292:C2259-C2268(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INHIBITION.
    15. "Ornithine transport via cationic amino acid transporter-1 is involved in ornithine cytotoxicity in retinal pigment epithelial cells."
      Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M., Matsumura M., Ito S.
      Invest. Ophthalmol. Vis. Sci. 48:464-471(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiYLAT2_HUMAN
    AccessioniPrimary (citable) accession number: Q92536
    Secondary accession number(s): Q68DS4, Q7L1N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3