S38A9_XENTR
ID S38A9_XENTR Reviewed; 554 AA.
AC Q5M7S0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 9 {ECO:0000305};
DE AltName: Full=Solute carrier family 38 member 9;
GN Name=slc38a9;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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. Associated
CC component of the Rag GTPases heterodimers.
CC {ECO:0000250|UniProtKB:Q8NBW4}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBW4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q08BA4}. Late
CC endosome membrane {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q08BA4}.
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 -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SLC38A9 subfamily. {ECO:0000305}.
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DR EMBL; BC088486; AAH88486.1; -; mRNA.
DR RefSeq; NP_001011337.1; NM_001011337.1.
DR AlphaFoldDB; Q5M7S0; -.
DR SMR; Q5M7S0; -.
DR STRING; 8364.ENSXETP00000058281; -.
DR PaxDb; Q5M7S0; -.
DR DNASU; 496801; -.
DR Ensembl; ENSXETT00000058281; ENSXETP00000058281; ENSXETG00000028090.
DR GeneID; 496801; -.
DR KEGG; xtr:496801; -.
DR CTD; 153129; -.
DR eggNOG; KOG1305; Eukaryota.
DR HOGENOM; CLU_037564_0_0_1; -.
DR InParanoid; Q5M7S0; -.
DR OMA; HWFTPTE; -.
DR OrthoDB; 941044at2759; -.
DR PhylomeDB; Q5M7S0; -.
DR TreeFam; TF312989; -.
DR Reactome; R-XTR-1632852; Macroautophagy.
DR Reactome; R-XTR-165159; MTOR signalling.
DR Reactome; R-XTR-166208; mTORC1-mediated signalling.
DR Reactome; R-XTR-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-XTR-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-XTR-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000028090; Expressed in ovary and 13 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Amino-acid transport; Disulfide bond; Endosome; Glycoprotein; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Sodium; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Sodium-coupled neutral amino acid transporter 9"
FT /id="PRO_0000328845"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 134..139
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..160
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 161..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..218
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 219..276
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..293
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 294..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..327
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 328..349
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..370
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 371..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 409..430
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..451
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 452..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 494..500
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 501..521
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 522..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 534..554
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT REGION 122..127
FT /note="Important for arginine binding and amino acid
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 248..417
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
SQ SEQUENCE 554 AA; 62278 MW; 38A95ADCC06BA49E CRC64;
MDSDQTPLIN PSLFEECAQN HFAATDPRSR RPFHIEPSYI TSINDDDPQR ITSVASAMNK
RIHYYSKLSN PSDKGLIAPD HVLPAPEEIY VYSPLGTALK IDGSDGTGKN SSIVTIFMIW
NTMMGTSILS IPWGIKQAGF TTGVCILFLM GILTLYCCYR VVKSRGTIPL TDTSNWEFPD
VCQYYFGSFG RWSSLLFSLV SLIGAMIVYW VLMSNFLFNT GKFIYNYVND VNVTDDVLSN
NGSDKVICPN PDSTRPLNKS MDTYFGNGTN YEQFETWWSK TNTVPFYLVV LLLPLLSFRS
PSFFAKFNIL GTVSIIYLVS LVTLKAAHLG FHLRFSWNQV QEFFVPEFRL SFPQLTGILT
LAFFIHNCII TLLKNNRNQK NNVRDLSIAY LLVGLTYIYV GVAVFASFPS PPLSKQCIQQ
NFLDNFPSSD ILAFVARIFL LFQMMTVYPL LGYLVRVQLL GHIFGDIYPS VFHVLALNIA
VVGVGVIMAR FYPNIGGIIR FSGAACGLAF VFVYPSLIHM ISLHRRGQLK VHSILIHVSI
IVLGIANLIA QFFM
