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Large neutral amino acids transporter small subunit 1 (4F2 light chain) (4F2 LC) (4F2LC) (CD98 light chain) (Integral membrane protein E16) (L-type amino acid transporter 1) (hLAT1) (Solute carrier family 7 member 5) (y system cationic amino acid transporter)

 LAT1_HUMAN              Reviewed;         507 AA.
Q01650; Q8IV97; Q9UBN8; Q9UP15; Q9UQC0;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Large neutral amino acids transporter small subunit 1;
AltName: Full=4F2 light chain;
Short=4F2 LC;
Short=4F2LC;
AltName: Full=CD98 light chain;
AltName: Full=Integral membrane protein E16;
AltName: Full=L-type amino acid transporter 1;
Short=hLAT1;
AltName: Full=Solute carrier family 7 member 5;
AltName: Full=y+ system cationic amino acid transporter;
Name=SLC7A5; Synonyms=CD98LC, LAT1, MPE16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND VARIANT LYS-230.
PubMed=9751058; DOI=10.1038/26246;
Mastroberardino L., Spindler B., Pfeiffer R., Skelly P.J., Loffing J.,
Shoemaker C.B., Verrey F.;
"Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a
permease family.";
Nature 395:288-291(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=10049700; DOI=10.1006/bbrc.1999.0206;
Prasad P.D., Wang H., Huang W., Kekuda R., Rajan D.P., Leibach F.H.,
Ganapathy V.;
"Human LAT1, a subunit of system L amino acid transporter: molecular
cloning and transport function.";
Biochem. Biophys. Res. Commun. 255:283-288(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
SPECIFICITY.
PubMed=10072483;
Tsurudome M., Ito M., Takebayashi S., Okumura K., Nishio M.,
Kawano M., Kusagawa S., Komada H., Ito Y.;
"Primary structure of the light chain of fusion regulatory protein-
1/CD98/4F2 predicts a protein with multiple transmembrane domains that
is almost identical to the amino acid transporter E16.";
J. Immunol. 162:2462-2466(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Ovary;
PubMed=11557028; DOI=10.1016/S0005-2736(01)00384-4;
Yanagida O., Kanai Y., Chairoungdua A., Kim D.K., Segawa H., Nii T.,
Cha S.H., Matsuo H., Fukushima J., Fukasawa Y., Tani Y., Taketani Y.,
Uchino H., Kim J.Y., Inatomi J., Okayasu I., Miyamoto K., Takeda E.,
Goya T., Endou H.;
"Human L-type amino acid transporter 1 (LAT1): characterization of
function and expression in tumor cell lines.";
Biochim. Biophys. Acta 1514:291-302(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Minato N., Iwai K., Takizawa C., Nakamura E.;
"Human 4F2 light chain: amino acid transporter.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-223.
TISSUE=Liver, and Lymph;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 181-507, TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Peripheral blood lymphocyte;
PubMed=1597461;
Gaugitsch H.W., Prieschl E.E., Kalthoff F., Huber N.E., Baumruker T.;
"A novel transiently expressed, integral membrane protein linked to
cell activation. Molecular cloning via the rapid degradation signal
AUUUA.";
J. Biol. Chem. 267:11267-11273(1992).
[8]
FUNCTION, AND INHIBITION.
PubMed=10391915; DOI=10.1074/jbc.274.28.19738;
Pineda M., Fernandez E., Torrents D., Estevez R., Lopez C., Camps M.,
Lloberas J., Zorzano A., Palacin M.;
"Identification of a membrane protein, LAT-2, that co-expresses with
4F2 heavy chain, an L-type amino acid transport activity with broad
specificity for small and large zwitterionic amino acids.";
J. Biol. Chem. 274:19738-19744(1999).
[9]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10574970; DOI=10.1074/jbc.274.49.34948;
Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F.,
Kuehn L.C.;
"LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter
of kidney and intestine.";
J. Biol. Chem. 274:34948-34954(1999).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
[11]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
INHIBITION.
PubMed=11389679; DOI=10.1042/0264-6021:3560719;
Ritchie J.W.A., Taylor P.M.;
"Role of the System L permease LAT1 in amino acid and iodothyronine
transport in placenta.";
Biochem. J. 356:719-725(2001).
[12]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INHIBITION.
PubMed=11564694; DOI=10.1210/endo.142.10.8418;
Friesema E.C.H., Docter R., Moerings E.P.C.M., Verrey F.,
Krenning E.P., Hennemann G., Visser T.J.;
"Thyroid hormone transport by the heterodimeric human system L amino
acid transporter.";
Endocrinology 142:4339-4348(2001).
[13]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11742812;
Okamoto Y., Sakata M., Ogura K., Yamamoto T., Yamaguchi M., Tasaka K.,
Kurachi H., Tsurudome M., Murata Y.;
"Expression and regulation of 4F2hc and hLAT1 in human trophoblasts.";
Am. J. Physiol. 282:C196-C204(2002).
[14]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION.
PubMed=12117417; DOI=10.1042/BJ20020841;
Simmons-Willis T.A., Koh A.S., Clarkson T.W., Ballatori N.;
"Transport of a neurotoxicant by molecular mimicry: the methylmercury-
L-cysteine complex is a substrate for human L-type large neutral amino
acid transporter (LAT) 1 and LAT2.";
Biochem. J. 367:239-246(2002).
[15]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
LOCATION, AND INHIBITION.
PubMed=12225859; DOI=10.1016/S0005-2736(02)00516-3;
Kim D.K., Kanai Y., Choi H.W., Tangtrongsup S., Chairoungdua A.,
Babu E., Tachampa K., Anzai N., Iribe Y., Endou H.;
"Characterization of the system L amino acid transporter in T24 human
bladder carcinoma cells.";
Biochim. Biophys. Acta 1565:112-121(2002).
[16]
TISSUE SPECIFICITY.
PubMed=12824232; DOI=10.1167/iovs.02-0907;
Jain-Vakkalagadda B., Dey S., Pal D., Mitra A.K.;
"Identification and functional characterization of a Na+-independent
large neutral amino acid transporter, LAT1, in human and rabbit
cornea.";
Invest. Ophthalmol. Vis. Sci. 44:2919-2927(2003).
[17]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16027961; DOI=10.1007/s00726-005-0221-x;
Fraga S., Pinho M.J., Soares-da-Silva P.;
"Expression of LAT1 and LAT2 amino acid transporters in human and rat
intestinal epithelial cells.";
Amino Acids 29:229-233(2005).
[18]
FUNCTION, SUBUNIT, AND INHIBITION.
PubMed=15769744; DOI=10.1074/jbc.M413164200;
Li S., Whorton A.R.;
"Identification of stereoselective transporters for S-nitroso-L-
cysteine: role of LAT1 and LAT2 in biological activity of S-
nitrosothiols.";
J. Biol. Chem. 280:20102-20110(2005).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16496379; DOI=10.1002/ijc.21866;
Nawashiro H., Otani N., Shinomiya N., Fukui S., Ooigawa H., Shima K.,
Matsuo H., Kanai Y., Endou H.;
"L-type amino acid transporter 1 as a potential molecular target in
human astrocytic tumors.";
Int. J. Cancer 119:484-492(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[21]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION.
PubMed=18262359; DOI=10.1016/j.neulet.2008.01.028;
Vumma R., Wiesel F.A., Flyckt L., Bjerkenstedt L., Venizelos N.;
"Functional characterization of tyrosine transport in fibroblast cells
from healthy controls.";
Neurosci. Lett. 434:56-60(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND THR-45, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND THR-45,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
INTERACTION WITH LAPTM4B, AND FUNCTION.
PubMed=25998567; DOI=10.1038/ncomms8250;
Milkereit R., Persaud A., Vanoaica L., Guetg A., Verrey F., Rotin D.;
"LAPTM4b recruits the LAT1-4F2hc Leu transporter to lysosomes and
promotes mTORC1 activation.";
Nat. Commun. 6:7250-7250(2015).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Sodium-independent, high-affinity transport of large
neutral amino acids such as phenylalanine, tyrosine, leucine,
arginine and tryptophan, when associated with SLC3A2/4F2hc.
Involved in cellular amino acid uptake. Acts as an amino acid
exchanger. Involved in the transport of L-DOPA across the blood-
brain barrier, and that of thyroid hormones triiodothyronine (T3)
and thyroxine (T4) across the cell membrane in tissues such as
placenta. Plays a role in neuronal cell proliferation
(neurogenesis) in brain. Involved in the uptake of methylmercury
(MeHg) when administered as the L-cysteine or D,L-homocysteine
complexes, and hence plays a role in metal ion homeostasis and
toxicity. Involved in the cellular activity of small molecular
weight nitrosothiols, via the stereoselective transport of L-
nitrosocysteine (L-CNSO) across the transmembrane. May play an
important role in high-grade gliomas. Mediates blood-to-retina L-
leucine transport across the inner blood-retinal barrier which in
turn may play a key role in maintaining large neutral amino acids
as well as neurotransmitters in the neural retina. Acts as the
major transporter of tyrosine in fibroblasts. When associated with
LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote
leucine uptake into these organelles and is required for mTORC1
activation (PubMed:25998567). {ECO:0000269|PubMed:10049700,
ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679,
ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744,
ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:18262359,
ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:9751058}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.9 uM for T4 (in the presence of choline chloride)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=0.8 uM for T3 (in the presence of choline chloride)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=12.5 uM for reverse triiodothyronine (rT3) (in the presence
of choline chloride) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=7.9 uM for 3,3'-diiodothyronine (in the presence of choline
chloride) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=46 uM for leucine (in the presence of choline chloride)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=19 uM for tryptophan (in the presence of choline chloride)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=32 uM for L-leucine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=10 mM for L-alanine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=2.2 mM for L-glutamine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=35 uM for L-histidine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=740 uM for L-phenylalanine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=98 uM for MeHg-L-cysteine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=99 uM for methionine {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=55.2 uM for phenylalanine (in T24 human bladder carcinoma
cells) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=60.4 uM for tyrosine (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=16.4 uM for tyrosine (in human fibroblasts)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=138 uM for Dopa (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=96.5 uM for 3-O-methyldopa (in T24 human bladder carcinoma
cells) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=153 uM for alpha-methyltyrosine (in T24 human bladder
carcinoma cells) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=216 uM for alpha-methyldopa (in T24 human bladder carcinoma
cells) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=191 uM for gabapentin (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=7.3 uM for triiodothyronine (in T24 human bladder carcinoma
cells) {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:18262359};
KM=162 uM for thyroxine (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=75.3 uM for melphanan (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
KM=156 uM for BCH (in T24 human bladder carcinoma cells)
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859,
ECO:0000269|PubMed:18262359};
-!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
transport protein SLC3A2/4F2hc (PubMed:10049700, PubMed:11311135,
PubMed:11389679, PubMed:11557028, PubMed:11564694,
PubMed:12225859, PubMed:15769744, PubMed:9751058). Interacts with
LAPTM4B; recruits SLC3A2 and SLC7A5 to lysosomes to promote
leucine uptake into these organelles and is required for mTORC1
activation (PubMed:25998567). {ECO:0000269|PubMed:10049700,
ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679,
ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744,
ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:9751058}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Apical cell membrane;
Multi-pass membrane protein. Note=Located to the plasma membrane
by SLC3A2/4F2hc. Localized to the apical membrane of placental
syncytiophoblastic cells. Expressed in both luminal and abluminal
membranes of brain capillary endothelial cells (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed abundantly in adult lung, liver,
brain, skeletal muscle, placenta, bone marrow, testis, resting
lymphocytes and monocytes, and in fetal liver. Weaker expression
in thymus, cornea, retina, peripheral leukocytes, spleen, kidney,
colon and lymph node. During gestation, expression in the placenta
was significantly stronger at full-term than at the mid-trimester
stage. Also expressed in all human tumor cell lines tested and in
the astrocytic process of primary astrocytic gliomas. Expressed in
retinal endothelial cells and in the intestinal epithelial cell
line Caco-2. {ECO:0000269|PubMed:10049700,
ECO:0000269|PubMed:10072483, ECO:0000269|PubMed:11389679,
ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11742812,
ECO:0000269|PubMed:12824232, ECO:0000269|PubMed:1597461,
ECO:0000269|PubMed:16027961, ECO:0000269|PubMed:16496379}.
-!- INDUCTION: Expression induced in quiescent peripheral blood
lymphocytes after treatment with phorbol myristate acetate (PMA)
and phytohemagglutinin (PHA). Expression and the uptake of leucine
is stimulated in mononuclear, cytotrophoblast-like choriocarcinoma
cells by combined treatment with PMA and calcium ionophore.
{ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:1597461}.
-!- MISCELLANEOUS: The uptake of leucine, tyrosine and tryptophan is
inhibited by the different iodothyronines, in particular T3.
Leucine transport is also inhibited by small zwitterionic amino
acids (i.e. glycine, alanine, serine, threonine and cysteine) and
by glutamine and asparginine. The uptake of T3 is almost
completely blocked by coincubation with leucine, tryptophan,
tyrosine, and phenylalanine, or 2-amino-bicyclo-(2,2,1)-heptane-2-
carboxylate (BCH). Methionine uptake was inhibited by the L-system
substrates L-leucine, BCH, L-cysteine and by the MeHg-L-cysteine
complex and structurally related S-ethyl-L-cysteine. MeHg-L-
cysteine uptake is inhibited by L-methionine, L-leucine, BCH and
S-ethyl-L-cysteine. L-leucine uptake was inhibited by L-CNSO.
Tyrosine uptake in fibroblasts was inhibited by D-methionine, and
methyl-aminoisobutyric acid (MeAIB).
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF077866; AAC61479.1; -; mRNA.
EMBL; AF104032; AAD20464.1; -; mRNA.
EMBL; AB018542; BAA33851.1; -; mRNA.
EMBL; AB018009; BAA84648.1; -; mRNA.
EMBL; AB017908; BAA75746.1; -; mRNA.
EMBL; BC039692; AAH39692.1; -; mRNA.
EMBL; BC042600; AAH42600.1; -; mRNA.
EMBL; M80244; AAA35780.1; -; mRNA.
CCDS; CCDS10964.1; -.
PIR; JG0165; JG0165.
RefSeq; NP_003477.4; NM_003486.6.
UniGene; Hs.513797; -.
ProteinModelPortal; Q01650; -.
BioGrid; 113801; 16.
IntAct; Q01650; 19.
MINT; MINT-5000558; -.
STRING; 9606.ENSP00000261622; -.
ChEMBL; CHEMBL4459; -.
DrugBank; DB01746; D-Leucine.
DrugBank; DB02556; D-Phenylalanine.
DrugBank; DB00509; Dextrothyroxine.
DrugBank; DB01235; Levodopa.
DrugBank; DB00451; Levothyroxine.
DrugBank; DB00279; Liothyronine.
DrugBank; DB01042; Melphalan.
DrugBank; DB02750; S-(Methylmercury)-L-Cysteine.
TCDB; 2.A.3.8.25; the amino acid-polyamine-organocation (apc) family.
iPTMnet; Q01650; -.
PhosphoSitePlus; Q01650; -.
SwissPalm; Q01650; -.
BioMuta; SLC7A5; -.
DMDM; 12643412; -.
EPD; Q01650; -.
MaxQB; Q01650; -.
PaxDb; Q01650; -.
PeptideAtlas; Q01650; -.
PRIDE; Q01650; -.
TopDownProteomics; Q01650; -.
DNASU; 8140; -.
Ensembl; ENST00000261622; ENSP00000261622; ENSG00000103257.
GeneID; 8140; -.
KEGG; hsa:8140; -.
UCSC; uc002fkm.4; human.
CTD; 8140; -.
DisGeNET; 8140; -.
EuPathDB; HostDB:ENSG00000103257.8; -.
GeneCards; SLC7A5; -.
HGNC; HGNC:11063; SLC7A5.
HPA; HPA052673; -.
HPA; HPA056077; -.
MIM; 600182; gene.
neXtProt; NX_Q01650; -.
OpenTargets; ENSG00000103257; -.
PharmGKB; PA35923; -.
eggNOG; KOG1287; Eukaryota.
eggNOG; COG0531; LUCA.
GeneTree; ENSGT00760000119037; -.
HOGENOM; HOG000098892; -.
HOVERGEN; HBG000476; -.
InParanoid; Q01650; -.
KO; K13780; -.
OMA; FTCIMTL; -.
OrthoDB; EOG091G07EM; -.
PhylomeDB; Q01650; -.
TreeFam; TF313355; -.
BioCyc; MetaCyc:ENSG00000103257-MONOMER; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
Reactome; R-HSA-71240; Tryptophan catabolism.
SABIO-RK; Q01650; -.
ChiTaRS; SLC7A5; human.
GeneWiki; SLC7A5; -.
GenomeRNAi; 8140; -.
PRO; PR:Q01650; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103257; -.
CleanEx; HS_SLC7A5; -.
ExpressionAtlas; Q01650; baseline and differential.
Genevisible; Q01650; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015171; F:amino acid transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; TAS:ProtInc.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
GO; GO:0006810; P:transport; TAS:ProtInc.
InterPro; IPR002293; AA/rel_permease1.
InterPro; IPR004760; L_AA_transporter.
Pfam; PF13520; AA_permease_2; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
TIGRFAMs; TIGR00911; 2A0308; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Isopeptide bond; Membrane; Neurogenesis;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 507 Large neutral amino acids transporter
small subunit 1.
/FTId=PRO_0000054270.
TRANSMEM 50 70 Helical. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TRANSMEM 146 166 Helical. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TRANSMEM 274 294 Helical. {ECO:0000255}.
TRANSMEM 319 339 Helical. {ECO:0000255}.
TRANSMEM 396 416 Helical. {ECO:0000255}.
TRANSMEM 431 451 Helical. {ECO:0000255}.
TRANSMEM 458 478 Helical. {ECO:0000255}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 45 45 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VARIANT 223 223 D -> V (in dbSNP:rs17853937).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_070119.
VARIANT 230 230 N -> K (in dbSNP:rs1060250).
{ECO:0000269|PubMed:9751058}.
/FTId=VAR_048157.
CONFLICT 15 15 A -> V (in Ref. 5; BAA75746).
{ECO:0000305}.
CONFLICT 29 31 AKS -> SKR (in Ref. 5; BAA75746).
{ECO:0000305}.
CONFLICT 35 35 S -> A (in Ref. 5; BAA75746).
{ECO:0000305}.
CONFLICT 62 62 T -> A (in Ref. 5; BAA75746).
{ECO:0000305}.
CONFLICT 88 88 V -> M (in Ref. 5; BAA75746).
{ECO:0000305}.
CONFLICT 154 154 T -> A (in Ref. 5; BAA75746).
{ECO:0000305}.
SEQUENCE 507 AA; 55010 MW; 767F3C60B62C0F02 CRC64;
MAGAGPKRRA LAAPAAEEKE EAREKMLAAK SADGSAPAGE GEGVTLQRNI TLLNGVAIIV
GTIIGSGIFV TPTGVLKEAG SPGLALVVWA ACGVFSIVGA LCYAELGTTI SKSGGDYAYM
LEVYGSLPAF LKLWIELLII RPSSQYIVAL VFATYLLKPL FPTCPVPEEA AKLVACLCVL
LLTAVNCYSV KAATRVQDAF AAAKLLALAL IILLGFVQIG KGDVSNLDPN FSFEGTKLDV
GNIVLALYSG LFAYGGWNYL NFVTEEMINP YRNLPLAIII SLPIVTLVYV LTNLAYFTTL
STEQMLSSEA VAVDFGNYHL GVMSWIIPVF VGLSCFGSVN GSLFTSSRLF FVGSREGHLP
SILSMIHPQL LTPVPSLVFT CVMTLLYAFS KDIFSVINFF SFFNWLCVAL AIIGMIWLRH
RKPELERPIK VNLALPVFFI LACLFLIAVS FWKTPVECGI GFTIILSGLP VYFFGVWWKN
KPKWLLQGIF STTVLCQKLM QVVPQET


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