S38A9_CAEEL
ID S38A9_CAEEL Reviewed; 615 AA.
AC Q19425;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 9 homolog;
GN ORFNames=F13H10.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
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).
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. {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 -!- 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 -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC SLC38A9 subfamily. {ECO:0000305}.
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DR EMBL; Z68748; CAA92953.2; -; Genomic_DNA.
DR PIR; T20863; T20863.
DR RefSeq; NP_741486.1; NM_171417.5.
DR AlphaFoldDB; Q19425; -.
DR SMR; Q19425; -.
DR STRING; 6239.F13H10.3b; -.
DR PaxDb; Q19425; -.
DR EnsemblMetazoa; F13H10.3a.1; F13H10.3a.1; WBGene00008774.
DR GeneID; 177997; -.
DR KEGG; cel:CELE_F13H10.3; -.
DR UCSC; F13H10.3a; c. elegans.
DR CTD; 177997; -.
DR WormBase; F13H10.3a; CE27959; WBGene00008774; -.
DR eggNOG; KOG1305; Eukaryota.
DR InParanoid; Q19425; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-165159; MTOR signalling.
DR Reactome; R-CEL-166208; mTORC1-mediated signalling.
DR Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q19425; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008774; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q19425; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 2.
PE 3: Inferred from homology;
KW Amino-acid transport; Disulfide bond; Endosome; Glycoprotein; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Sodium; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Sodium-coupled neutral amino acid transporter 9
FT homolog"
FT /id="PRO_0000093832"
FT TOPO_DOM 1..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 166..186
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 187..192
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..213
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 214..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 247..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 274..341
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 342..358
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 359..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 368..392
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 393..413
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 414..434
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 435..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 473..491
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 492..512
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 513..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 534..554
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 555..561
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..582
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 583..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 595..615
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT REGION 41..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..180
FT /note="Important for arginine binding and amino acid
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 304..478
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
SQ SEQUENCE 615 AA; 68693 MW; 5092F2A8F4A3A420 CRC64;
MPPFFAEFTE SVFRHFRRNE PDEENSAICS EKMSSYGAIG VDDNDTDPLL DDEPPRRLPP
AGGVPIGRRR AISASQIGSI PSQSAATRQP YLFTGGLGLR DESLLSLHSE DDLHREHNNA
LRYRLYNRLD PGGEHLTMPD HVLPPNLFSI LPFEELKDVS GKQGSIVTIF SIWNTMMGTS
LLAMPWALQQ AGLVLGIIIM LSMAAICFYT AYIVIESPKR LQDLSVDPLL AEFSDVCKSL
FGRIGEYCAV VFSVCVLIGG VIVYWVLMSN FLYYTGAVVY ESMQPNSTTI PVMENKTFTC
DVYCPEQTSQ WTIPQWEKQL YDAVSEMEGG ETGDDSWSFD KFWTLRGTVP IYLAFALFPL
MNFKSPTFFT KFNVLGTISV MYLLMFVFSK LLECGVNMDF SNPKSIHYVQ LANMHFPALS
GTLTLSYFIH NAVLTILRNQ KHPENNARDL SIGYCLVAFC YVFIGFTFFA AFPVQRSCIS
DNFLNNFGAG DVLSSTARLF LLFQMITVLP LLMFLVRSQL FYAIFGQTWP GAIRVIILNV
LLIAVAVGFA TFYPNVGSIL RYVGSISGLV YVFALPAMVY IKQSEAAGTL TPMKKYAHYG
IIVIGVANLI AQFVI
