S38A9_HUMAN
ID S38A9_HUMAN Reviewed; 561 AA.
AC Q8NBW4; A0A0A8K8P2; B3KXV1; B7Z7D0; Q0P5S0; Q6MZJ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 9 {ECO:0000305};
DE AltName: Full=Solute carrier family 38 member 9 {ECO:0000312|HGNC:HGNC:26907};
DE AltName: Full=Up-regulated in lung cancer 11 {ECO:0000303|Ref.2};
GN Name=SLC38A9 {ECO:0000312|HGNC:HGNC:26907};
GN Synonyms=URLC11 {ECO:0000303|Ref.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP THR-182.
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-182.
RA Daigo Y., Nakamura Y.;
RT "Isolation and characterization of novel human genes, which are up-
RT regulated in lung cancer.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-182.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-561 (ISOFORM 2), AND VARIANT
RP THR-182.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBUNIT, GLYCOSYLATION, AND MUTAGENESIS OF 38-ARG--PHE-40; 70-TYR--ARG-73;
RP 85-PRO--HIS-87; 98-TYR--LEU-101 AND ASN-128.
RX PubMed=25561175; DOI=10.1038/nature14107;
RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M.,
RA Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X.,
RA Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.;
RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery that
RT controls mTORC1.";
RL Nature 519:477-481(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, AND MUTAGENESIS OF
RP HIS-60; ILE-68; TYR-71; LEU-74; PRO-85 AND PRO-90.
RX PubMed=25567906; DOI=10.1126/science.1257132;
RA Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
RA Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L.,
RA Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.;
RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT sufficiency to mTORC1.";
RL Science 347:188-194(2015).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP MUTAGENESIS OF ILE-68 AND THR-133.
RX PubMed=29053970; DOI=10.1016/j.cell.2017.09.046;
RA Wyant G.A., Abu-Remaileh M., Wolfson R.L., Chen W.W., Freinkman E.,
RA Danai L.V., Vander Heiden M.G., Sabatini D.M.;
RT "mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from
RT Lysosomes and Use Protein as a Nutrient.";
RL Cell 171:642-654(2017).
RN [11]
RP INTERACTION WITH TM4SF5, AND SUBCELLULAR LOCATION.
RX PubMed=30956113; DOI=10.1016/j.cmet.2019.03.005;
RA Jung J.W., Macalino S.J.Y., Cui M., Kim J.E., Kim H.J., Song D.G.,
RA Nam S.H., Kim S., Choi S., Lee J.W.;
RT "Transmembrane 4 L six family member 5 senses arginine for mTORC1
RT signaling.";
RL Cell Metab. 29:1306-1319(2019).
CC -!- FUNCTION: Lysosomal amino acid transporter involved in the activation
CC of mTORC1 in response to amino acid levels. Probably acts as an amino
CC acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes
CC involved in amino acid sensing and activation of mTORC1, a signaling
CC complex promoting cell growth in response to growth factors, energy
CC levels, and amino acids (PubMed:25561175, PubMed:25567906,
CC PubMed:29053970). Following activation by amino acids, the Ragulator
CC and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes
CC where it is in turn activated. SLC38A9 mediates transport of amino
CC acids with low capacity and specificity with a slight preference for
CC polar amino acids (PubMed:25561175, PubMed:25567906). Acts as an
CC arginine sensor (PubMed:25567906, PubMed:29053970). Following
CC activation by arginine binding, mediates transport of leucine, tyrosine
CC and phenylalanine with high efficiency, and is required for the
CC efficient utilization of these amino acids after lysosomal protein
CC degradation (PubMed:29053970). {ECO:0000269|PubMed:25561175,
CC ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:29053970}.
CC -!- ACTIVITY REGULATION: Amino acid transport is sodium-dependent (By
CC similarity). Transport of leucine, tyrosine and phenylalanine is
CC increased by arginine binding (PubMed:29053970).
CC {ECO:0000250|UniProtKB:Q08BA4, ECO:0000269|PubMed:29053970}.
CC -!- SUBUNIT: Associated component of the Ragulator complex (composed of
CC LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5). Associated component
CC of the Rag GTPases heterodimers (composed of RRAGA, RRAGB, RRAGC and
CC RRAGD). Interacts with TM4SF5 (PubMed:30956113).
CC {ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
CC ECO:0000269|PubMed:29053970, ECO:0000269|PubMed:30956113}.
CC -!- INTERACTION:
CC Q8NBW4; Q6IAA8: LAMTOR1; NbExp=12; IntAct=EBI-9978316, EBI-715385;
CC Q8NBW4; Q9Y2Q5: LAMTOR2; NbExp=3; IntAct=EBI-9978316, EBI-2643704;
CC Q8NBW4; Q9UHA4: LAMTOR3; NbExp=5; IntAct=EBI-9978316, EBI-1038192;
CC Q8NBW4; Q0VGL1: LAMTOR4; NbExp=4; IntAct=EBI-9978316, EBI-5658976;
CC Q8NBW4; O43504: LAMTOR5; NbExp=4; IntAct=EBI-9978316, EBI-713382;
CC Q8NBW4; Q7L523: RRAGA; NbExp=13; IntAct=EBI-9978316, EBI-752376;
CC Q8NBW4; Q5VZM2: RRAGB; NbExp=2; IntAct=EBI-9978316, EBI-993049;
CC Q8NBW4; Q9HB90: RRAGC; NbExp=12; IntAct=EBI-9978316, EBI-752390;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25561175,
CC ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:29053970,
CC ECO:0000269|PubMed:30956113}; Multi-pass membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:25561175};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NBW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBW4-2; Sequence=VSP_032815;
CC Name=3;
CC IsoId=Q8NBW4-3; Sequence=VSP_045111, VSP_045112;
CC Name=4;
CC IsoId=Q8NBW4-4; Sequence=VSP_045110;
CC -!- DOMAIN: The cytosolic N-terminus part of the protein mediates
CC interaction with the Ragulator complex and the Rag GTPases
CC heterodimers. {ECO:0000269|PubMed:25561175,
CC ECO:0000269|PubMed:25567906}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:25561175,
CC ECO:0000269|PubMed:25567906}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SLC38A9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAQ19756.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK075190; BAC11460.1; -; mRNA.
DR EMBL; AK127988; BAG54613.1; -; mRNA.
DR EMBL; AK301850; BAH13566.1; -; mRNA.
DR EMBL; AB105188; BAQ19756.1; ALT_INIT; mRNA.
DR EMBL; AC008784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471123; EAW54926.1; -; Genomic_DNA.
DR EMBL; BC066891; AAH66891.1; -; mRNA.
DR EMBL; BC101362; AAI01363.1; -; mRNA.
DR EMBL; BX641065; CAE46032.1; -; mRNA.
DR CCDS; CCDS3968.1; -. [Q8NBW4-1]
DR CCDS; CCDS58947.1; -. [Q8NBW4-4]
DR CCDS; CCDS58948.1; -. [Q8NBW4-3]
DR RefSeq; NP_001245215.1; NM_001258286.1. [Q8NBW4-4]
DR RefSeq; NP_001245216.1; NM_001258287.1. [Q8NBW4-3]
DR RefSeq; NP_775785.2; NM_173514.3. [Q8NBW4-1]
DR RefSeq; XP_006714600.1; XM_006714537.2.
DR RefSeq; XP_006714601.1; XM_006714538.3.
DR RefSeq; XP_006714602.1; XM_006714539.3. [Q8NBW4-1]
DR RefSeq; XP_011541475.1; XM_011543173.1.
DR RefSeq; XP_011541476.1; XM_011543174.1. [Q8NBW4-1]
DR PDB; 6WJ2; EM; 3.20 A; H=1-119.
DR PDB; 6WJ3; EM; 3.90 A; H=1-119.
DR PDBsum; 6WJ2; -.
DR PDBsum; 6WJ3; -.
DR AlphaFoldDB; Q8NBW4; -.
DR SMR; Q8NBW4; -.
DR BioGRID; 127480; 32.
DR DIP; DIP-61480N; -.
DR IntAct; Q8NBW4; 26.
DR STRING; 9606.ENSP00000380074; -.
DR TCDB; 2.A.18.9.1; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q8NBW4; 4 sites.
DR iPTMnet; Q8NBW4; -.
DR PhosphoSitePlus; Q8NBW4; -.
DR BioMuta; SLC38A9; -.
DR DMDM; 296452888; -.
DR EPD; Q8NBW4; -.
DR jPOST; Q8NBW4; -.
DR MassIVE; Q8NBW4; -.
DR MaxQB; Q8NBW4; -.
DR PaxDb; Q8NBW4; -.
DR PeptideAtlas; Q8NBW4; -.
DR PRIDE; Q8NBW4; -.
DR ProteomicsDB; 3820; -.
DR ProteomicsDB; 6851; -.
DR ProteomicsDB; 72830; -. [Q8NBW4-1]
DR ProteomicsDB; 72831; -. [Q8NBW4-2]
DR Antibodypedia; 23436; 56 antibodies from 15 providers.
DR DNASU; 153129; -.
DR Ensembl; ENST00000318672.7; ENSP00000316596.3; ENSG00000177058.12. [Q8NBW4-1]
DR Ensembl; ENST00000396865.7; ENSP00000380074.2; ENSG00000177058.12. [Q8NBW4-1]
DR Ensembl; ENST00000512595.5; ENSP00000427335.1; ENSG00000177058.12. [Q8NBW4-3]
DR Ensembl; ENST00000515629.5; ENSP00000420934.1; ENSG00000177058.12. [Q8NBW4-4]
DR GeneID; 153129; -.
DR KEGG; hsa:153129; -.
DR MANE-Select; ENST00000396865.7; ENSP00000380074.2; NM_173514.4; NP_775785.2.
DR UCSC; uc003jqd.4; human. [Q8NBW4-1]
DR CTD; 153129; -.
DR DisGeNET; 153129; -.
DR GeneCards; SLC38A9; -.
DR HGNC; HGNC:26907; SLC38A9.
DR HPA; ENSG00000177058; Tissue enhanced (placenta).
DR MIM; 616203; gene.
DR neXtProt; NX_Q8NBW4; -.
DR OpenTargets; ENSG00000177058; -.
DR PharmGKB; PA162403774; -.
DR VEuPathDB; HostDB:ENSG00000177058; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00390000005646; -.
DR InParanoid; Q8NBW4; -.
DR OMA; HWFTPTE; -.
DR OrthoDB; 941044at2759; -.
DR PhylomeDB; Q8NBW4; -.
DR TreeFam; TF312989; -.
DR PathwayCommons; Q8NBW4; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-165159; MTOR signalling.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q8NBW4; -.
DR SIGNOR; Q8NBW4; -.
DR BioGRID-ORCS; 153129; 6 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC38A9; human.
DR GenomeRNAi; 153129; -.
DR Pharos; Q8NBW4; Tbio.
DR PRO; PR:Q8NBW4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NBW4; protein.
DR Bgee; ENSG00000177058; Expressed in secondary oocyte and 171 other tissues.
DR ExpressionAtlas; Q8NBW4; baseline and differential.
DR Genevisible; Q8NBW4; HS.
DR GO; GO:1905103; C:integral component of lysosomal membrane; IMP:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:UniProtKB.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid transport; Disulfide bond;
KW Endosome; Glycoprotein; Lysosome; Membrane; Metal-binding;
KW Reference proteome; Sodium; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..561
FT /note="Sodium-coupled neutral amino acid transporter 9"
FT /id="PRO_0000328840"
FT TOPO_DOM 1..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25561175"
FT TRANSMEM 120..140
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 141..146
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 168..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..225
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 226..283
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 284..300
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 301..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 310..334
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 335..356
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..377
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 378..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 416..437
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 459..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 480..500
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 501..507
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 508..528
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 529..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 541..561
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..134
FT /note="Important for arginine binding and amino acid
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 255..424
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045110"
FT VAR_SEQ 1..37
FT /note="MANMNSDSRHLGTSEVDHERDPGPMNIQFEPSDLRSK -> MAICILTWRI
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045111"
FT VAR_SEQ 318..353
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045112"
FT VAR_SEQ 428..561
FT /note="NFLDNFPSSDTLSFIARIFLLFQMMTVYPLLGYLARVQLLGHIFGDIYPSIF
FT HVLILNLIIVGAGVIMACFYPNIGGIIRYSGAACGLAFVFIYPSLIYIISLHQEERLTW
FT PKLIFHVFIIILGVANLIVQFFM -> VRHRVPSLCDCVHFHVFIVGRVIQWQDITSDR
FT PGF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032815"
FT VARIANT 182
FT /note="S -> T (in dbSNP:rs4865615)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_042546"
FT MUTAGEN 38..40
FT /note="RPF->AAA: Abolishes interaction with the Ragulator
FT and Rag GTPases complexes."
FT /evidence="ECO:0000269|PubMed:25561175"
FT MUTAGEN 60
FT /note="H->A: Does not affect association with the Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:25567906"
FT MUTAGEN 68
FT /note="I->A: Abolishes association with the Ragulator
FT complex. No effect on amino acid transport activity."
FT /evidence="ECO:0000269|PubMed:25567906,
FT ECO:0000269|PubMed:29053970"
FT MUTAGEN 70..73
FT /note="YYSR->AAAA: Abolishes interaction with the Ragulator
FT and Rag GTPases complexes."
FT /evidence="ECO:0000269|PubMed:25561175"
FT MUTAGEN 71
FT /note="Y->A: Abolishes association with the Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:25567906"
FT MUTAGEN 74
FT /note="L->A: Abolishes association with the Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:25567906"
FT MUTAGEN 85..87
FT /note="PDH->AAA: Abolishes interaction with the Ragulator
FT and Rag GTPases complexes."
FT /evidence="ECO:0000269|PubMed:25561175"
FT MUTAGEN 85
FT /note="P->A: Abolishes association with the Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:25567906"
FT MUTAGEN 90
FT /note="P->A: Abolishes association with the Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:25567906"
FT MUTAGEN 98..101
FT /note="YSPL->AAAA: Does not affect interaction with the
FT Ragulator and Rag GTPases complexes."
FT /evidence="ECO:0000269|PubMed:25561175"
FT MUTAGEN 128
FT /note="N->A: Moderately affects amino acid transport."
FT /evidence="ECO:0000269|PubMed:25561175"
FT MUTAGEN 133
FT /note="T->W: Abolishes arginine transport. No effect on
FT subcellular location and interaction with Ragulator
FT complex."
FT /evidence="ECO:0000269|PubMed:29053970"
FT CONFLICT 84
FT /note="A -> P (in Ref. 5; AAH66891)"
FT /evidence="ECO:0000305"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6WJ2"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:6WJ2"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6WJ2"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6WJ2"
SQ SEQUENCE 561 AA; 63776 MW; 0C1A3A136158168A CRC64;
MANMNSDSRH LGTSEVDHER DPGPMNIQFE PSDLRSKRPF CIEPTNIVNV NHVIQRVSDH
ASAMNKRIHY YSRLTTPADK ALIAPDHVVP APEECYVYSP LGSAYKLQSY TEGYGKNTSL
VTIFMIWNTM MGTSILSIPW GIKQAGFTTG MCVIILMGLL TLYCCYRVVK SRTMMFSLDT
TSWEYPDVCR HYFGSFGQWS SLLFSLVSLI GAMIVYWVLM SNFLFNTGKF IFNFIHHIND
TDTILSTNNS NPVICPSAGS GGHPDNSSMI FYANDTGAQQ FEKWWDKSRT VPFYLVGLLL
PLLNFKSPSF FSKFNILGTV SVLYLIFLVT FKAVRLGFHL EFHWFIPTEF FVPEIRFQFP
QLTGVLTLAF FIHNCIITLL KNNKKQENNV RDLCIAYMLV TLTYLYIGVL VFASFPSPPL
SKDCIEQNFL DNFPSSDTLS FIARIFLLFQ MMTVYPLLGY LARVQLLGHI FGDIYPSIFH
VLILNLIIVG AGVIMACFYP NIGGIIRYSG AACGLAFVFI YPSLIYIISL HQEERLTWPK
LIFHVFIIIL GVANLIVQFF M
