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Y L amino acid transporter 2 (Cationic amino acid transporter, y system) (Solute carrier family 7 member 6) (y( )L-type amino acid transporter 2) (Y LAT2) (y LAT-2)

 YLAT2_HUMAN             Reviewed;         515 AA.
Q92536; Q68DS4; Q7L1N3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 3.
23-MAY-2018, entry version 142.
RecName: Full=Y+L amino acid transporter 2;
AltName: Full=Cationic amino acid transporter, y+ system;
AltName: Full=Solute carrier family 7 member 6;
AltName: Full=y(+)L-type amino acid transporter 2;
Short=Y+LAT2;
Short=y+LAT-2;
Name=SLC7A6 {ECO:0000312|HGNC:HGNC:11064};
Synonyms=KIAA0245 {ECO:0000312|EMBL:BAA13376.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Myoblast {ECO:0000269|PubMed:9829974};
PubMed=9829974; DOI=10.1074/jbc.273.49.32437;
Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J.,
Shi Y.-B., Zorzano A., Palacin M.;
"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.";
J. Biol. Chem. 273:32437-32445(1998).
[2] {ECO:0000312|EMBL:BAA13376.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow {ECO:0000312|EMBL:BAA13376.2};
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"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.";
DNA Res. 3:321-329(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Salivary gland;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4] {ECO:0000312|EMBL:CAH18146.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000312|EMBL:AAH28216.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukocyte {ECO:0000312|EMBL:AAH28216.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=11078698;
Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G.,
Sperandeo M.P., Andria G., Gazzola G.C.;
"Arginine transport through system y(+)L in cultured human
fibroblasts: normal phenotype of cells from LPI subjects.";
Am. J. Physiol. 279:C1829-C1837(2000).
[7] {ECO:0000305}
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION.
PubMed=10903140; DOI=10.1042/bj3490787;
Broeer A., Wagner C.A., Lang F., Broeer S.;
"The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates
arginine efflux in exchange with glutamine.";
Biochem. J. 349:787-795(2000).
[8] {ECO:0000305}
FUNCTION, AND SUBUNIT.
PubMed=11311135;
Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V.,
Lang F., Broeer S.;
"Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires
different domains.";
Biochem. J. 355:725-731(2001).
[9] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=11742806;
Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A.,
Bussolati O., Gazzola G.C., Dall'Asta V.;
"Two-way arginine transport in human endothelial cells: TNF-alpha
stimulation is restricted to system y(+).";
Am. J. Physiol. 282:C134-C143(2002).
[10] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14603368; DOI=10.1113/eph8802647;
Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.;
"Nitric oxide synthesis requires activity of the cationic and neutral
amino acid transport system y+L in human umbilical vein endothelium.";
Exp. Physiol. 88:699-710(2003).
[11] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15280038; DOI=10.1016/j.febslet.2004.06.086;
Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E.,
Gazzola G.C., Dall'Asta V.;
"INFgamma stimulates arginine transport through system y+L in human
monocytes.";
FEBS Lett. 571:177-181(2004).
[12] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=15756301; DOI=10.1038/sj.ejhg.5201376;
Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C.,
Taglialatela M., Andria G., Sebastio G.;
"A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity:
implications for the molecular pathogenesis of lysinuric protein
intolerance.";
Eur. J. Hum. Genet. 13:628-634(2005).
[13] {ECO:0000305}
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INHIBITION.
PubMed=16785209; DOI=10.1080/09687860600652968;
Chubb S., Kingsland A.L., Broeer A., Broeer S.;
"Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2
light-chain dysfunction.";
Mol. Membr. Biol. 23:255-267(2006).
[14] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND INHIBITION.
PubMed=17329401; DOI=10.1152/ajpcell.00323.2006;
Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.;
"Activation of classical protein kinase C decreases transport via
systems y+ and y+L.";
Am. J. Physiol. 292:C2259-C2268(2007).
[15] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17197568; DOI=10.1167/iovs.06-0398;
Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M.,
Matsumura M., Ito S.;
"Ornithine transport via cationic amino acid transporter-1 is involved
in ornithine cytotoxicity in retinal pigment epithelial cells.";
Invest. Ophthalmol. Vis. Sci. 48:464-471(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10903140,
ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:14603368,
ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:16785209,
ECO:0000269|PubMed:17197568, ECO:0000269|PubMed:17329401,
ECO:0000269|PubMed:9829974}.
-!- ENZYME REGULATION: 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.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=295 uM for glutamine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=236 uM for leucine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=120 uM for arginine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=138 uM for arginine (in the absence of NaCl)
{ECO:0000269|PubMed:10903140};
-!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
transport protein SLC3A2/4F2hc. {ECO:0000269|PubMed:11311135,
ECO:0000269|PubMed:16785209}.
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:15756301, ECO:0000269|PubMed:16785209}; Multi-
pass membrane protein {ECO:0000269|PubMed:15756301,
ECO:0000269|PubMed:16785209}.
-!- TISSUE SPECIFICITY: Expressed in normal fibroblasts and those from
LPI patients. Also expressed in HUVECs, monocytes, RPE cells, and
various carcinoma cell lines. {ECO:0000269|PubMed:11078698,
ECO:0000269|PubMed:11742806, ECO:0000269|PubMed:14603368,
ECO:0000269|PubMed:15280038, ECO:0000269|PubMed:17197568,
ECO:0000269|PubMed:17329401}.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=BAA13376.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D87432; BAA13376.2; ALT_INIT; mRNA.
EMBL; CR749291; CAH18146.1; -; mRNA.
EMBL; CH471092; EAW83219.1; -; Genomic_DNA.
EMBL; BC028216; AAH28216.1; -; mRNA.
CCDS; CCDS32470.1; -.
RefSeq; NP_001070253.1; NM_001076785.2.
RefSeq; NP_003974.3; NM_003983.5.
RefSeq; XP_011521735.1; XM_011523433.1.
RefSeq; XP_011521736.1; XM_011523434.1.
RefSeq; XP_011521740.1; XM_011523438.1.
UniGene; Hs.679580; -.
ProteinModelPortal; Q92536; -.
BioGrid; 114519; 6.
IntAct; Q92536; 2.
STRING; 9606.ENSP00000219343; -.
TCDB; 2.A.3.8.23; the amino acid-polyamine-organocation (apc) family.
iPTMnet; Q92536; -.
PhosphoSitePlus; Q92536; -.
BioMuta; SLC7A6; -.
DMDM; 190462822; -.
EPD; Q92536; -.
MaxQB; Q92536; -.
PaxDb; Q92536; -.
PeptideAtlas; Q92536; -.
PRIDE; Q92536; -.
DNASU; 9057; -.
Ensembl; ENST00000219343; ENSP00000219343; ENSG00000103064.
Ensembl; ENST00000566454; ENSP00000455064; ENSG00000103064.
GeneID; 9057; -.
KEGG; hsa:9057; -.
UCSC; uc002evt.3; human.
CTD; 9057; -.
DisGeNET; 9057; -.
EuPathDB; HostDB:ENSG00000103064.13; -.
GeneCards; SLC7A6; -.
H-InvDB; HIX0013172; -.
HGNC; HGNC:11064; SLC7A6.
HPA; HPA050713; -.
MIM; 605641; gene.
neXtProt; NX_Q92536; -.
OpenTargets; ENSG00000103064; -.
PharmGKB; PA35924; -.
eggNOG; KOG1287; Eukaryota.
eggNOG; COG0531; LUCA.
GeneTree; ENSGT00760000119037; -.
HOGENOM; HOG000098892; -.
HOVERGEN; HBG000476; -.
InParanoid; Q92536; -.
KO; K13872; -.
OMA; PFKAWLP; -.
OrthoDB; EOG091G07EM; -.
PhylomeDB; Q92536; -.
TreeFam; TF313355; -.
BioCyc; MetaCyc:ENSG00000103064-MONOMER; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
SABIO-RK; Q92536; -.
ChiTaRS; SLC7A6; human.
GeneWiki; SLC7A6; -.
GenomeRNAi; 9057; -.
PRO; PR:Q92536; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103064; -.
CleanEx; HS_SLC7A6; -.
ExpressionAtlas; Q92536; baseline and differential.
Genevisible; Q92536; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:ProtInc.
GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
InterPro; IPR002293; AA/rel_permease1.
Pfam; PF13520; AA_permease_2; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
1: Evidence at protein level;
Amino-acid transport; Antiport; Cell membrane; Complete proteome;
Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 515 Y+L amino acid transporter 2.
/FTId=PRO_0000341477.
TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.
TRANSMEM 45 65 Helical. {ECO:0000255}.
TOPO_DOM 66 78 Extracellular. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
TOPO_DOM 100 114 Cytoplasmic. {ECO:0000255}.
TRANSMEM 115 135 Helical. {ECO:0000255}.
TOPO_DOM 136 167 Extracellular. {ECO:0000255}.
TRANSMEM 168 188 Helical. {ECO:0000255}.
TOPO_DOM 189 194 Cytoplasmic. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TOPO_DOM 216 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TOPO_DOM 257 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical. {ECO:0000255}.
TOPO_DOM 288 311 Extracellular. {ECO:0000255}.
TRANSMEM 312 332 Helical. {ECO:0000255}.
TOPO_DOM 333 363 Cytoplasmic. {ECO:0000255}.
TRANSMEM 364 384 Helical. {ECO:0000255}.
TOPO_DOM 385 385 Extracellular. {ECO:0000255}.
TRANSMEM 386 406 Helical. {ECO:0000255}.
TOPO_DOM 407 425 Cytoplasmic. {ECO:0000255}.
TRANSMEM 426 446 Helical. {ECO:0000255}.
TOPO_DOM 447 451 Extracellular. {ECO:0000255}.
TRANSMEM 452 472 Helical. {ECO:0000255}.
TOPO_DOM 473 515 Cytoplasmic. {ECO:0000255}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BGK6}.
CONFLICT 8 8 R -> G (in Ref. 3; CAH18146).
{ECO:0000305}.
CONFLICT 388 388 Q -> R (in Ref. 3; CAH18146).
{ECO:0000305}.
SEQUENCE 515 AA; 56828 MW; 4E92F6E1972351A9 CRC64;
MEAREPGRPT PTYHLVPNTS QSQVEEDVSS PPQRSSETMQ LKKEISLLNG VSLVVGNMIG
SGIFVSPKGV LVHTASYGMS LIVWAIGGLF SVVGALCYAE LGTTITKSGA SYAYILEAFG
GFIAFIRLWV SLLVVEPTGQ AIIAITFANY IIQPSFPSCD PPYLACRLLA AACICLLTFV
NCAYVKWGTR VQDTFTYAKV VALIAIIVMG LVKLCQGHSE HFQDAFEGSS WDMGNLSLAL
YSALFSYSGW DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNISDVLS
SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG HLPDLLSMIH
IERFTPIPAL LFNCTMALIY LIVEDVFQLI NYFSFSYWFF VGLSVVGQLY LRWKEPKRPR
PLKLSVFFPI VFCICSVFLV IVPLFTDTIN SLIGIGIALS GVPFYFMGVY LPESRRPLFI
RNVLAAITRG TQQLCFCVLT ELDVAEEKKD ERKTD


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