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Protein

Sodium-coupled neutral amino acid transporter 9

Gene

Slc38a9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acids. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids, suggesting that it acts as an amino acid sensor instead. The high concentration of arginine in lysosomes suggests that it acts as an arginine sensor.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium-coupled neutral amino acid transporter 9Curated
Alternative name(s):
Solute carrier family 38 member 9Imported
Gene namesi
Name:Slc38a9Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1918839. Slc38a9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 118118CytoplasmicBy similarityAdd
BLAST
Transmembranei119 – 13921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini140 – 1434LumenalCurated
Transmembranei144 – 16421Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini165 – 19733CytoplasmicCuratedAdd
BLAST
Transmembranei198 – 21821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini219 – 28971LumenalCuratedAdd
BLAST
Transmembranei290 – 31021Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini311 – 3122CytoplasmicCurated
Transmembranei313 – 33321Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini334 – 35724LumenalCuratedAdd
BLAST
Transmembranei358 – 37821Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini379 – 39113CytoplasmicCuratedAdd
BLAST
Transmembranei392 – 41221Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini413 – 43624LumenalCuratedAdd
BLAST
Transmembranei437 – 45721Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini458 – 47619CytoplasmicCuratedAdd
BLAST
Transmembranei477 – 49721Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini498 – 50811LumenalCuratedAdd
BLAST
Transmembranei509 – 52921Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini530 – 53910CytoplasmicCurated
Transmembranei540 – 56021Helical; Name=11Sequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Sodium-coupled neutral amino acid transporter 9PRO_0000328841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineCombined sources
Glycosylationi238 – 2381N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi247 – 2471N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi265 – 2651N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi273 – 2731N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8BGD6.
MaxQBiQ8BGD6.
PaxDbiQ8BGD6.
PRIDEiQ8BGD6.

PTM databases

iPTMnetiQ8BGD6.
PhosphoSiteiQ8BGD6.

Expressioni

Gene expression databases

BgeeiQ8BGD6.
GenevisibleiQ8BGD6. MM.

Interactioni

Subunit structurei

Associated component of the Ragulator complex (composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5). Associated component of the Rag GTPases heterodimers (composed of RRAGA, RRAGB, RRAGC and RRAGD).By similarity

Protein-protein interaction databases

IntActiQ8BGD6. 1 interaction.
STRINGi10090.ENSMUSP00000052172.

Structurei

3D structure databases

ProteinModelPortaliQ8BGD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The cytosolic N-terminus part of the protein mediates interaction with the Ragulator complex and the Rag GTPases heterodimers.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1305. Eukaryota.
COG0814. LUCA.
GeneTreeiENSGT00390000005646.
HOGENOMiHOG000294102.
HOVERGENiHBG106242.
InParanoidiQ8BGD6.
KOiK14995.
OMAiDCIEQNF.
OrthoDBiEOG7V1FQQ.
PhylomeDBiQ8BGD6.
TreeFamiTF312989.

Family and domain databases

InterProiIPR013057. AA_transpt_TM.
[Graphical view]
PfamiPF01490. Aa_trans. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVDGDSRH LLSEVEHEVS PGPMNIQFDS SDLRSKRPFY IEPTNIVNVN
60 70 80 90 100
DVIQRVSDHA AAMNKRIHYY SRLTTPADKA LIAPDHVVPA PEECYVYSPL
110 120 130 140 150
GSAYKLKSYT EGYGKNTSLV TIFMIWNTMM GTSILSIPWG IKQAGFTTGM
160 170 180 190 200
CVIVLMGLLT LYCCYRVVKS RSTISTSDTS TWEYPDVCKH YFGSFGQWSS
210 220 230 240 250
LLFSLVSLIG AMIVYWVLMS NFLFNTGKFI FNFIHHINDT DTVLSTNNSN
260 270 280 290 300
PVICPNAGSG GRPDNSSMIF YNNNTEVQLF EKWWDKSRTV PFYLIGLLLP
310 320 330 340 350
LLNFKSPSFF SKFNILGTVS VLYLIFVVTL KAVRLGFHLE FHWFVPTEFF
360 370 380 390 400
VPEIRAQFPQ LMGVLTLAFF IHNCIITLLK NNKNQENNVR DLCIAYMLVT
410 420 430 440 450
LTYLYIGILV FASFPSPPLP KDCIEQNFLD NFPSSDILSF IARIFLLFQM
460 470 480 490 500
MTVYPLLGYL ARVQLLGHIF GDIYPSIFHV LILNLVIVGA GVTMACFYPN
510 520 530 540 550
IGGIIRYSGA ACGLAFVFIY PSLIYIISLH QEERLTWPKL VFHVIIIILG
560
LANLIAQFFM
Length:560
Mass (Da):63,392
Last modified:March 1, 2003 - v1
Checksum:iA425A51A2187CAE5
GO

Sequence cautioni

The sequence BAC37465.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti472 – 4721D → V in AAH52361 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK043402 mRNA. Translation: BAC31537.1.
AK044735 mRNA. Translation: BAC32057.1.
AK078926 mRNA. Translation: BAC37465.1. Different initiation.
BC052361 mRNA. Translation: AAH52361.1.
CCDSiCCDS26775.1.
RefSeqiNP_848861.1. NM_178746.4.
XP_006517733.1. XM_006517670.2.
UniGeneiMm.397106.
Mm.40834.
Mm.480005.

Genome annotation databases

EnsembliENSMUST00000052514; ENSMUSP00000052172; ENSMUSG00000047789.
GeneIDi268706.
KEGGimmu:268706.
UCSCiuc007rwo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK043402 mRNA. Translation: BAC31537.1.
AK044735 mRNA. Translation: BAC32057.1.
AK078926 mRNA. Translation: BAC37465.1. Different initiation.
BC052361 mRNA. Translation: AAH52361.1.
CCDSiCCDS26775.1.
RefSeqiNP_848861.1. NM_178746.4.
XP_006517733.1. XM_006517670.2.
UniGeneiMm.397106.
Mm.40834.
Mm.480005.

3D structure databases

ProteinModelPortaliQ8BGD6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BGD6. 1 interaction.
STRINGi10090.ENSMUSP00000052172.

PTM databases

iPTMnetiQ8BGD6.
PhosphoSiteiQ8BGD6.

Proteomic databases

EPDiQ8BGD6.
MaxQBiQ8BGD6.
PaxDbiQ8BGD6.
PRIDEiQ8BGD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052514; ENSMUSP00000052172; ENSMUSG00000047789.
GeneIDi268706.
KEGGimmu:268706.
UCSCiuc007rwo.2. mouse.

Organism-specific databases

CTDi153129.
MGIiMGI:1918839. Slc38a9.

Phylogenomic databases

eggNOGiKOG1305. Eukaryota.
COG0814. LUCA.
GeneTreeiENSGT00390000005646.
HOGENOMiHOG000294102.
HOVERGENiHBG106242.
InParanoidiQ8BGD6.
KOiK14995.
OMAiDCIEQNF.
OrthoDBiEOG7V1FQQ.
PhylomeDBiQ8BGD6.
TreeFamiTF312989.

Miscellaneous databases

ChiTaRSiSlc38a9. mouse.
PROiQ8BGD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGD6.
GenevisibleiQ8BGD6. MM.

Family and domain databases

InterProiIPR013057. AA_transpt_TM.
[Graphical view]
PfamiPF01490. Aa_trans. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum, Cerebellum and Retina.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiS38A9_MOUSE
AccessioniPrimary (citable) accession number: Q8BGD6
Secondary accession number(s): Q80W70, Q8C5C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.