S38A9_MOUSE
ID S38A9_MOUSE Reviewed; 560 AA.
AC Q8BGD6; Q80W70; Q8C5C3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 9 {ECO:0000305};
DE AltName: Full=Solute carrier family 38 member 9 {ECO:0000312|MGI:MGI:1918839};
GN Name=Slc38a9 {ECO:0000312|MGI:MGI:1918839};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, Cerebellum, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
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. Following activation by amino acids, the
CC Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to
CC lysosomes where it is in turn activated. SLC38A9 mediates transport of
CC amino acids with low capacity and specificity with a slight preference
CC for polar amino acids. Acts as an arginine sensor. Following activation
CC by arginine binding, mediates transport of leucine, tyrosine and
CC phenylalanine with high efficiency, and is required for the efficient
CC utilization of these amino acids after lysosomal protein degradation.
CC {ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- ACTIVITY REGULATION: Amino acid transport is sodium-dependent (By
CC similarity). Transport of leucine, tyrosine and phenylalanine is
CC increased by arginine binding (By similarity).
CC {ECO:0000250|UniProtKB:Q08BA4, ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- SUBUNIT: Associated component of the Ragulator complex (composed of
CC LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5) (By similarity).
CC Associated component of the Rag GTPases heterodimers (composed of
CC RRAGA, RRAGB, RRAGC and RRAGD) (By similarity). Interacts with TM4SF5
CC (By similarity). {ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBW4};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The cytosolic N-terminus part of the protein mediates
CC interaction with the Ragulator complex and the Rag GTPases
CC heterodimers. {ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SLC38A9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37465.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK043402; BAC31537.1; -; mRNA.
DR EMBL; AK044735; BAC32057.1; -; mRNA.
DR EMBL; AK078926; BAC37465.1; ALT_INIT; mRNA.
DR EMBL; BC052361; AAH52361.1; -; mRNA.
DR CCDS; CCDS26775.1; -.
DR RefSeq; NP_848861.1; NM_178746.4.
DR RefSeq; XP_006517733.1; XM_006517670.2.
DR AlphaFoldDB; Q8BGD6; -.
DR SMR; Q8BGD6; -.
DR IntAct; Q8BGD6; 1.
DR STRING; 10090.ENSMUSP00000052172; -.
DR GlyGen; Q8BGD6; 4 sites.
DR iPTMnet; Q8BGD6; -.
DR PhosphoSitePlus; Q8BGD6; -.
DR EPD; Q8BGD6; -.
DR jPOST; Q8BGD6; -.
DR MaxQB; Q8BGD6; -.
DR PaxDb; Q8BGD6; -.
DR PeptideAtlas; Q8BGD6; -.
DR PRIDE; Q8BGD6; -.
DR ProteomicsDB; 256683; -.
DR Antibodypedia; 23436; 56 antibodies from 15 providers.
DR DNASU; 268706; -.
DR Ensembl; ENSMUST00000052514; ENSMUSP00000052172; ENSMUSG00000047789.
DR GeneID; 268706; -.
DR KEGG; mmu:268706; -.
DR UCSC; uc007rwo.2; mouse.
DR CTD; 153129; -.
DR MGI; MGI:1918839; Slc38a9.
DR VEuPathDB; HostDB:ENSMUSG00000047789; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00390000005646; -.
DR HOGENOM; CLU_037564_0_0_1; -.
DR InParanoid; Q8BGD6; -.
DR OMA; HWFTPTE; -.
DR OrthoDB; 941044at2759; -.
DR PhylomeDB; Q8BGD6; -.
DR TreeFam; TF312989; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165159; MTOR signalling.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 268706; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc38a9; mouse.
DR PRO; PR:Q8BGD6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BGD6; protein.
DR Bgee; ENSMUSG00000047789; Expressed in lumbar dorsal root ganglion and 224 other tissues.
DR ExpressionAtlas; Q8BGD6; baseline and differential.
DR Genevisible; Q8BGD6; MM.
DR GO; GO:1905103; C:integral component of lysosomal membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0071986; C:Ragulator complex; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISS: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; ISO:MGI.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 2.
PE 1: Evidence at protein level;
KW Amino-acid transport; Disulfide bond; Endosome; Glycoprotein; Lysosome;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Sodium;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Sodium-coupled neutral amino acid transporter 9"
FT /id="PRO_0000328841"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 140..145
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 167..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..224
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 225..282
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..299
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 300..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..333
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 334..355
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 356..376
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 377..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..414
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 415..436
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..457
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 458..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 479..499
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 500..506
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 507..527
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 528..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 540..560
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT REGION 128..133
FT /note="Important for arginine binding and amino acid
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 254..423
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT CONFLICT 472
FT /note="D -> V (in Ref. 2; AAH52361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 63392 MW; A425A51A2187CAE5 CRC64;
MASVDGDSRH LLSEVEHEVS PGPMNIQFDS SDLRSKRPFY IEPTNIVNVN DVIQRVSDHA
AAMNKRIHYY SRLTTPADKA LIAPDHVVPA PEECYVYSPL GSAYKLKSYT EGYGKNTSLV
TIFMIWNTMM GTSILSIPWG IKQAGFTTGM CVIVLMGLLT LYCCYRVVKS RSTISTSDTS
TWEYPDVCKH YFGSFGQWSS LLFSLVSLIG AMIVYWVLMS NFLFNTGKFI FNFIHHINDT
DTVLSTNNSN PVICPNAGSG GRPDNSSMIF YNNNTEVQLF EKWWDKSRTV PFYLIGLLLP
LLNFKSPSFF SKFNILGTVS VLYLIFVVTL KAVRLGFHLE FHWFVPTEFF VPEIRAQFPQ
LMGVLTLAFF IHNCIITLLK NNKNQENNVR DLCIAYMLVT LTYLYIGILV FASFPSPPLP
KDCIEQNFLD NFPSSDILSF IARIFLLFQM MTVYPLLGYL ARVQLLGHIF GDIYPSIFHV
LILNLVIVGA GVTMACFYPN IGGIIRYSGA ACGLAFVFIY PSLIYIISLH QEERLTWPKL
VFHVIIIILG LANLIAQFFM
