SLC7A5
entrez
8140
canonical
uniprot
Q01650
canonical
ensembl
ENSG00000103257
resolver
ensp
ENSP00000261622
resolver
enst
ENST00000261622
resolver
genesymbol
SLC7A5
resolver
genesymbol_syn
CD98LC
resolver
genesymbol_syn
LAT1
resolver
genesymbol_syn
MPE16
resolver
hgnc
HGNC:11063
resolver
uniprot
Q8IV97
resolver
uniprot
Q9UBN8
resolver
uniprot
Q9UP15
resolver
uniprot
Q9UQC0
resolver
uniprot_entry
LAT1_HUMAN
resolver
uniprot_sec
Q8IV97
resolver
uniprot_sec
Q9UBN8
resolver
uniprot_sec
Q9UP15
resolver
uniprot_sec
Q9UQC0
resolver
activity_regulation
ACTIVITY REGULATION: The uptake of leucine, tyrosine and tryptophan is inhibited by the different iodothyronines, in particular T3 (PubMed:11564694). 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) (PubMed:11564694). 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 (PubMed:12117417). MeHg-L-cysteine uptake is inhibited by L-methionine, L-leucine, BCH and S-ethyl-L-cysteine (PubMed:12117417). L-leucine transport is inhibited by phenylalanine, tyrosine, L-dopa, 3-O-methyldopa, a-methyltyrosine, a-methyldopa, gabapentin, triiodothyronine, thyroxine, melphalan and BCH (PubMed:12225859). L-leucine uptake was inhibited by L-CNSO (PubMed:15769744). Tyrosine uptake in fibroblasts was inhibited by D-methionine, and methyl-aminoisobutyric acid (MeAIB) (PubMed:18262359). {ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:18262359}.
uniprot
proteins
amino_acid_sequence
MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET
uniprot
proteins
function
FUNCTION: Forms a heterodimer with SLC3A2 that functions as a sodium-independent transporter for large neutral amino acids (PubMed:9751058, PubMed:10049700, PubMed:11557028, PubMed:10574970, PubMed:11564694, PubMed:12117417, PubMed:12225859, PubMed:15769744, PubMed:18262359, PubMed:25998567, PubMed:30867591). Functions as an obligatory amino acid antiporter, mediating the exchange of amino acids and amino acid-related compounds across the plasma membrane (PubMed:11557028, PubMed:12117417, PubMed:12225859, PubMed:11847106, PubMed:17896864). Also mediates sodium-independent exchange of iodothyronines with neutral and aromatic L-alpha-amino acids (PubMed:11564694, PubMed:12225859). Mediates exchange of L-tryptophan with the tryptophan metabolites L-kynurenine and 3-hydroxy-L-kynurenine (PubMed:17896864). Mediates cellular uptake of iodothyronines, including thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and 3,3'-diiodo-L-thyronine (3,3'-T2), and iodotyrosines including 3-iodo-L-tyrosine (MIT) and 3,5-diiodo-L-tyrosine (DIT) (PubMed:26305885, PubMed:38661522). Involved in the uptake of methylmercury (MeHg) when administered as L-cysteine or D,L-homocysteine complexes, thereby contributing to metal ion homeostasis and toxicity (PubMed:12117417). Involved in the cellular activity of low-molecular-weight nitrosothiols through stereoselective transport of L-nitrosocysteine (L-CNSO) across the plasma membrane (PubMed:15769744). When associated with LAPTM4B, the heterodimer is recruited to lysosomes, where it promotes leucine uptake into these organelles and thereby contributes to mTORC1 activation (PubMed:25998567). {ECO:0000269|PubMed:10049700, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11847106, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:17896864, ECO:0000269|PubMed:18262359, ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:26305885, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:38661522, ECO:0000269|PubMed:9751058}.; FUNCTION: (Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis. {ECO:0000269|PubMed:30341327}.
uniprot
proteins
mass_dalton
55010
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="Y->A: Strongly decreased leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 246; /note="A->V: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 252; /note="F->A: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 257; /note="W->A: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 258; /note="N->A: Decreased leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 258; /note="N->D: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 259; /note="Y->A: Strongly decreased leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 303; /note="E->K: Decreased leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 375; /note="P->L: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591"; MUTAGEN 483..507; /note="Missing: Nearly abolishes leucine transport activity."; /evidence="ECO:0000269|PubMed:30867591
uniprot
proteins
protein_family
Amino acid-polyamine-organocation (APC) superfamily
uniprot
proteins
protein_family
L-type amino acid transporter (LAT) (TC 2.A.3.8) family
uniprot
proteins
pubmed
10049700
uniprot
proteins
pubmed
10072483
uniprot
proteins
pubmed
10574970
uniprot
proteins
pubmed
11389679
uniprot
proteins
pubmed
11557028
uniprot
proteins
pubmed
11564694
uniprot
proteins
pubmed
11742812
uniprot
proteins
pubmed
11847106
uniprot
proteins
pubmed
12117417
uniprot
proteins
pubmed
12225859
uniprot
proteins
pubmed
12824232
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15769744
uniprot
proteins
pubmed
1597461
uniprot
proteins
pubmed
16027961
uniprot
proteins
pubmed
16496379
uniprot
proteins
pubmed
17896864
uniprot
proteins
pubmed
18262359
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25998567
uniprot
proteins
pubmed
26305885
uniprot
proteins
pubmed
30341327
uniprot
proteins
pubmed
30867591
uniprot
proteins
pubmed
38661522
uniprot
proteins
pubmed
9751058
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11742812}; Multi-pass membrane protein {ECO:0000269|PubMed:30867591}. Cell membrane {ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:9751058}; Multi-pass membrane protein {ECO:0000269|PubMed:30867591}. Lysosome membrane {ECO:0000269|PubMed:25998567}; Multi-pass membrane protein {ECO:0000305|PubMed:25998567}. Note=Located to the plasma membrane by SLC3A2/4F2hc (PubMed:9751058). Localized to the apical membrane of placental syncytiotrophoblastic cells (PubMed:11742812). Recruited to lysosomes by LAPTM4B (PubMed:25998567). {ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:9751058}.
uniprot
proteins
transmembrane_region
TRANSMEM 50..70; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 84..104; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 127..147; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 170..190; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 193..214; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 243..263; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 277..297; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 325..345; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 370..390; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 396..416; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 431..451; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591"; TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000269|PubMed:30867591
uniprot
proteins