SLC38A9
entrez
153129
canonical
uniprot
Q8NBW4
canonical
ensembl
ENSG00000177058
resolver
ensp
ENSP00000380074
resolver
ensp
ENSP00000397429
resolver
ensp
ENSP00000420934
resolver
ensp
ENSP00000427335
resolver
ensp
ENSP00000540488
resolver
ensp
ENSP00000540489
resolver
ensp
ENSP00000540490
resolver
ensp
ENSP00000540491
resolver
ensp
ENSP00000540493
resolver
ensp
ENSP00000540494
resolver
ensp
ENSP00000587137
resolver
ensp
ENSP00000587139
resolver
ensp
ENSP00000587141
resolver
ensp
ENSP00000587142
resolver
ensp
ENSP00000587143
resolver
ensp
ENSP00000587145
resolver
ensp
ENSP00000587146
resolver
ensp
ENSP00000587147
resolver
ensp
ENSP00000587148
resolver
ensp
ENSP00000587149
resolver
ensp
ENSP00000587151
resolver
ensp
ENSP00000587152
resolver
ensp
ENSP00000587153
resolver
ensp
ENSP00000615460
resolver
ensp
ENSP00000615461
resolver
ensp
ENSP00000712834
resolver
ensp
ENSP00000762561
resolver
enst
ENST00000416547
resolver
genesymbol
FLJ90709
resolver
genesymbol
SLC38A9
resolver
genesymbol_syn
URLC11
resolver
hgnc
HGNC:26907
resolver
uniprot
A0A0A8K8P2
resolver
uniprot
B3KVK8
resolver
uniprot
B3KXV1
resolver
uniprot
B7Z7D0
resolver
uniprot
F6UL64
resolver
uniprot
Q0P5S0
resolver
uniprot
Q6MZJ8
resolver
uniprot_entry
B3KVK8_HUMAN
resolver
uniprot_entry
F6UL64_HUMAN
resolver
uniprot_entry
S38A9_HUMAN
resolver
uniprot_sec
A0A0A8K8P2
resolver
uniprot_sec
B3KXV1
resolver
uniprot_sec
B7Z7D0
resolver
uniprot_sec
Q0P5S0
resolver
uniprot_sec
Q6MZJ8
resolver
activity_regulation
ACTIVITY REGULATION: Amino acid transport activity is increased by sodium and is most active at acidic pH (PubMed:25561175, PubMed:31295473). Transport of L-glutamine, leucine and tyrosine is increased by arginine binding (PubMed:29053970, PubMed:31295473). {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:29053970, ECO:0000269|PubMed:31295473}.
uniprot
proteins
amino_acid_sequence
MANMNSDSRHLGTSEVDHERDPGPMNIQFEPSDLRSKRPFCIEPTNIVNVNHVIQRVSDHASAMNKRIHYYSRLTTPADKALIAPDHVVPAPEECYVYSPLGSAYKLQSYTEGYGKNTSLVTIFMIWNTMMGTSILSIPWGIKQAGFTTGMCVIILMGLLTLYCCYRVVKSRTMMFSLDTTSWEYPDVCRHYFGSFGQWSSLLFSLVSLIGAMIVYWVLMSNFLFNTGKFIFNFIHHINDTDTILSTNNSNPVICPSAGSGGHPDNSSMIFYANDTGAQQFEKWWDKSRTVPFYLVGLLLPLLNFKSPSFFSKFNILGTVSVLYLIFLVTFKAVRLGFHLEFHWFIPTEFFVPEIRFQFPQLTGVLTLAFFIHNCIITLLKNNKKQENNVRDLCIAYMLVTLTYLYIGVLVFASFPSPPLSKDCIEQNFLDNFPSSDTLSFIARIFLLFQMMTVYPLLGYLARVQLLGHIFGDIYPSIFHVLILNLIIVGAGVIMACFYPNIGGIIRYSGAACGLAFVFIYPSLIYIISLHQEERLTWPKLIFHVFIIILGVANLIVQFFM
uniprot
proteins
function
FUNCTION: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels (PubMed:25561175, PubMed:25567906, PubMed:29053970). Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:25567906, PubMed:29053970). Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (PubMed:25561175, PubMed:25567906). SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids (PubMed:25561175, PubMed:25567906). Acts as an arginine sensor (PubMed:25567906, PubMed:29053970, PubMed:31295473). Following activation by arginine binding, mediates transport of L-glutamine, leucine and tyrosine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation (PubMed:29053970, PubMed:31295473). However, the transport mechanism is not well defined and the role of sodium is not clear (PubMed:25561175, PubMed:31295473). Can disassemble the lysosomal folliculin complex (LFC), and thereby triggers GAP activity of FLCN:FNIP2 toward RRAGC (PubMed:32868926). Acts as an cholesterol sensor that conveys increases in lysosomal cholesterol, leading to lysosomal recruitment and activation of mTORC1 via the Rag GTPases (PubMed:28336668). Guanine exchange factor (GEF) that, upon arginine binding, stimulates GDP release from RRAGA and therefore activates the Rag GTPase heterodimer and the mTORC1 pathway in response to nutrient sufficiency (PubMed:30181260). {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:28336668, ECO:0000269|PubMed:29053970, ECO:0000269|PubMed:30181260, ECO:0000269|PubMed:31295473, ECO:0000269|PubMed:32868926, ECO:0000305|PubMed:31295473}.
uniprot
proteins
mass_dalton
63776
uniprot
proteins
mutagenesis
MUTAGEN 38..40; /note="RPF->AAA: Abolishes interaction with the Ragulator and Rag GTPases complexes."; /evidence="ECO:0000269|PubMed:25561175"; MUTAGEN 60; /note="H->A: Does not affect association with the Ragulator complex. Abolishes the interaction with the Rag GTPases heterodimer complex."; /evidence="ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:32868926"; MUTAGEN 68; /note="I->A: Abolishes association with the Ragulator complex. No effect on amino acid transport activity. Abolishes the interaction with the Rag GTPases heterodimer complex."; /evidence="ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:29053970, ECO:0000269|PubMed:32868926"; MUTAGEN 70..73; /note="YYSR->AAAA: Abolishes interaction with the Ragulator and Rag GTPases complexes."; /evidence="ECO:0000269|PubMed:25561175"; MUTAGEN 71; /note="Y->A: Abolishes association with the Ragulator complex. Abolishes the interaction with the Rag GTPases heterodimer complex."; /evidence="ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:32868926"; MUTAGEN 74; /note="L->A: Abolishes association with the Ragulator complex. Abolishes the interaction with the Rag GTPases heterodimer complex."; /evidence="ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:32868926"; MUTAGEN 85..87; /note="PDH->AAA: Abolishes interaction with the Ragulator and Rag GTPases complexes."; /evidence="ECO:0000269|PubMed:25561175"; MUTAGEN 85; /note="P->A: Abolishes association with the Ragulator complex."; /evidence="ECO:0000269|PubMed:25567906"; MUTAGEN 90; /note="P->A: Abolishes association with the Ragulator complex."; /evidence="ECO:0000269|PubMed:25567906"; MUTAGEN 98..101; /note="YSPL->AAAA: Does not affect interaction with the Ragulator and Rag GTPases complexes."; /evidence="ECO:0000269|PubMed:25561175"; MUTAGEN 128; /note="N->A: Moderately affects amino acid transport."; /evidence="ECO:0000269|PubMed:25561175"; MUTAGEN 133; /note="T->W: Abolishes arginine transport. No effect on subcellular location and interaction with Ragulator complex."; /evidence="ECO:0000269|PubMed:29053970"; MUTAGEN 449; /note="F->I: Abolishes cholesterol binding; when associated with I-460. Does not affect disrupted arginine-mediated activation of mTORC1; when associated with I-460. Does not affect lysosomal localization; when associated with I-460. Increases interactions with both Rag GTPase and Ragulator subunits; when associated with I-460. Loss of L-glutamine transport stimulation by cholesterol."; /evidence="ECO:0000269|PubMed:28336668, ECO:0000269|PubMed:31295473"; MUTAGEN 453; /note="T->A: Does not affect L-glutamine transport activity."; /evidence="ECO:0000269|PubMed:31295473"; MUTAGEN 460; /note="Y->I: Decreases cholesterol binding. Abolishes cholesterol binding; when associated with I-449. Does not affect disrupted arginine-mediated activation of mTORC1; when associated with I-449. Does not affect lysosomal localization; when associated with I-449. Increases interactions with both Rag GTPase and Ragulator subunits; when associated with I-449. Loss of L-glutamine transport stimulation by cholesterol."; /evidence="ECO:0000269|PubMed:28336668, ECO:0000269|PubMed:31295473
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.
uniprot
proteins
protein_family
Amino acid/polyamine transporter 2 family
uniprot
proteins
protein_family
SLC38A9 subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
25561175
uniprot
proteins
pubmed
25567906
uniprot
proteins
pubmed
28336668
uniprot
proteins
pubmed
29053970
uniprot
proteins
pubmed
30181260
uniprot
proteins
pubmed
30956113
uniprot
proteins
pubmed
31295473
uniprot
proteins
pubmed
32868926
uniprot
proteins
pubmed
36103527
uniprot
proteins
sequence_length
561
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:29053970, ECO:0000269|PubMed:30956113}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q08BA4}. Late endosome membrane {ECO:0000269|PubMed:25561175}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q08BA4}.
uniprot
proteins
transmembrane_region
TRANSMEM 120..140; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 147..167; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 199..225; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 284..300; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 310..334; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 357..377; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 395..415; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 438..458; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 480..500; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 508..528; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:Q08BA4"; TRANSMEM 541..561; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:Q08BA4
uniprot
proteins