S38A9_RAT
ID S38A9_RAT Reviewed; 559 AA.
AC Q3B8Q3; Q561Z8; R9PXU2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 9 {ECO:0000305};
DE AltName: Full=Solute carrier family 38 member 9 {ECO:0000312|RGD:1311881};
GN Name=Slc38a9 {ECO:0000312|RGD:1311881};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Spleen;
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).
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}.
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DR EMBL; AABR06012861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092662; AAH92662.1; -; mRNA.
DR EMBL; BC105869; AAI05870.1; -; mRNA.
DR RefSeq; NP_001030328.1; NM_001035251.1.
DR RefSeq; XP_006231991.1; XM_006231929.3.
DR RefSeq; XP_006231992.1; XM_006231930.3.
DR RefSeq; XP_006231993.1; XM_006231931.3.
DR RefSeq; XP_006231994.1; XM_006231932.2.
DR RefSeq; XP_006231995.1; XM_006231933.2.
DR AlphaFoldDB; Q3B8Q3; -.
DR SMR; Q3B8Q3; -.
DR STRING; 10116.ENSRNOP00000013218; -.
DR GlyGen; Q3B8Q3; 3 sites.
DR PaxDb; Q3B8Q3; -.
DR Ensembl; ENSRNOT00000013218; ENSRNOP00000013218; ENSRNOG00000009851.
DR GeneID; 310091; -.
DR KEGG; rno:310091; -.
DR CTD; 153129; -.
DR RGD; 1311881; Slc38a9.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00390000005646; -.
DR HOGENOM; CLU_037564_0_0_1; -.
DR InParanoid; Q3B8Q3; -.
DR OMA; HWFTPTE; -.
DR OrthoDB; 941044at2759; -.
DR PhylomeDB; Q3B8Q3; -.
DR TreeFam; TF312989; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-165159; MTOR signalling.
DR Reactome; R-RNO-166208; mTORC1-mediated signalling.
DR Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q3B8Q3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000009851; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q3B8Q3; baseline and differential.
DR Genevisible; Q3B8Q3; RN.
DR GO; GO:1905103; C:integral component of lysosomal membrane; ISO:RGD.
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; IEA:Ensembl.
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:RGD.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:RGD.
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..559
FT /note="Sodium-coupled neutral amino acid transporter 9"
FT /id="PRO_0000328842"
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..281
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..298
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 299..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..332
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 333..354
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 355..375
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 376..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 393..413
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 414..435
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 436..456
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 457..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 478..498
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 499..505
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..526
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT TOPO_DOM 527..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 539..559
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 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 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 254..422
FT /evidence="ECO:0000250|UniProtKB:Q08BA4"
SQ SEQUENCE 559 AA; 63418 MW; B5311209F1530CC4 CRC64;
MANVDSDSRH LISEVEHEVN PGPMNIQFDS SDLRSKRPFY IEPTNIVNVN DVIQKVSDHA
AAMNKRIHYY SRLTTPADKA LIAPDHVVPA PEECYVYSPL GSAYKLKSYT EGYRKNTSLV
TIFMIWNTMM GTSILSIPWG IKQAGFTTGM CVIVLMGLLT LYCCYRVVKS RSMIVTSDTT
TWEYPDVCKH YFGSFGQWSS LLFSLVSLIG AMIVYWVLMS NFLFNTGKFI FNFIHHINDT
DTVLSTNNSS PVICPSAGSG HPDNSSMIFY NSDTEVRLFE RWWDKSKTVP FYLIGLLLPL
LNFKSPSFFS KFNILGTVSV LYLIFIVTLK AIRLGFHLEF HWFAPTEFFV PEIRAQFPQL
TGVLTLAFFI HNCIITLLKN NKNQENNVRD LCIAYMLVTL TYLYIGVLVF ASFPSPPLPK
DCIEQNFLDN FPSSDTLSFI ARICLLFQMM TVYPLLGYLA RVQLLGHIFG DIYPSIFHVL
ILNLIIVGAG VTMACFYPNI GGIIRYSGAA CGLAFVFIYP SLIYILSQHQ EERLTWPKLV
FHIIIIILGL ANLIAQFFM
