LTOR5_MOUSE
ID LTOR5_MOUSE Reviewed; 91 AA.
AC Q9D1L9; Q3UJV9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ragulator complex protein LAMTOR5;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5;
GN Name=Lamtor5; Synonyms=Hbxip, Xip;
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, and DBA/2J; TISSUE=Embryo;
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=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: As part of the Ragulator complex it is involved in amino acid
CC sensing and activation of mTORC1, a signaling complex promoting cell
CC growth in response to growth factors, energy levels, and amino acids.
CC Activated by amino acids through a mechanism involving the lysosomal V-
CC ATPase, the Ragulator functions as a guanine nucleotide exchange factor
CC activating the small GTPases Rag. Activated Ragulator and Rag GTPases
CC function as a scaffold recruiting mTORC1 to lysosomes where it is in
CC turn activated. When complexed to BIRC5, interferes with apoptosome
CC assembly, preventing recruitment of pro-caspase-9 to oligomerized
CC APAF1, thereby selectively suppressing apoptosis initiated via the
CC mitochondrial/cytochrome c pathway. {ECO:0000250|UniProtKB:O43504}.
CC -!- SUBUNIT: Homodimer. Part of the Ragulator complex composed of LAMTOR1,
CC LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a
CC heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3
CC heterodimer. The Ragulator complex interacts with both the mTORC1
CC complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB,
CC RRAGC and RRAGD; regulated by amino acid availability. The Ragulator
CC complex interacts with SLC38A9; the probable amino acid sensor.
CC Component of the lysosomal folliculin complex (LFC), composed of FLCN,
CC FNIP1 (or FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or
CC RRAGD/RagD GTP-bound, and Ragulator. Interacts with phosphorylated
CC BIRC5; the resulting complex binds pro-caspase-9, as well as active
CC caspase-9, but much less efficiently. Interacts with SUPV3L1.
CC {ECO:0000250|UniProtKB:O43504}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O43504}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43504}.
CC -!- SIMILARITY: Belongs to the LAMTOR5 family. {ECO:0000305}.
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DR EMBL; AK003358; BAB22734.1; -; mRNA.
DR EMBL; AK146289; BAE27046.1; -; mRNA.
DR EMBL; BC028547; AAH28547.1; -; mRNA.
DR RefSeq; NP_081050.2; NM_026774.2.
DR AlphaFoldDB; Q9D1L9; -.
DR SMR; Q9D1L9; -.
DR BioGRID; 212935; 17.
DR ComplexPortal; CPX-4761; Ragulator complex.
DR CORUM; Q9D1L9; -.
DR STRING; 10090.ENSMUSP00000129012; -.
DR iPTMnet; Q9D1L9; -.
DR PhosphoSitePlus; Q9D1L9; -.
DR EPD; Q9D1L9; -.
DR jPOST; Q9D1L9; -.
DR MaxQB; Q9D1L9; -.
DR PaxDb; Q9D1L9; -.
DR PeptideAtlas; Q9D1L9; -.
DR PRIDE; Q9D1L9; -.
DR ProteomicsDB; 252686; -.
DR Antibodypedia; 1857; 173 antibodies from 28 providers.
DR Ensembl; ENSMUST00000199317; ENSMUSP00000143494; ENSMUSG00000087260.
DR GeneID; 68576; -.
DR KEGG; mmu:68576; -.
DR CTD; 10542; -.
DR MGI; MGI:1915826; Lamtor5.
DR VEuPathDB; HostDB:ENSMUSG00000087260; -.
DR eggNOG; ENOG502S5TK; Eukaryota.
DR GeneTree; ENSGT00390000006247; -.
DR HOGENOM; CLU_164970_0_0_1; -.
DR InParanoid; Q9D1L9; -.
DR OrthoDB; 1405682at2759; -.
DR PhylomeDB; Q9D1L9; -.
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; 68576; 17 hits in 60 CRISPR screens.
DR ChiTaRS; Lamtor5; mouse.
DR PRO; PR:Q9D1L9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D1L9; protein.
DR Bgee; ENSMUSG00000087260; Expressed in right kidney and 254 other tissues.
DR ExpressionAtlas; Q9D1L9; baseline and differential.
DR Genevisible; Q9D1L9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0071986; C:Ragulator complex; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; ISS:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; IC:ComplexPortal.
DR InterPro; IPR024135; LAMTOR5.
DR PANTHER; PTHR13342; PTHR13342; 1.
DR Pfam; PF16672; LAMTOR5; 1.
DR PRINTS; PR02092; HEPBVIRUSXIP.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Lysosome; Reference proteome.
FT CHAIN 1..91
FT /note="Ragulator complex protein LAMTOR5"
FT /id="PRO_0000066008"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43504"
SQ SEQUENCE 91 AA; 9642 MW; 2CD9E762ABD07BE4 CRC64;
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ QAARLTSDPT
DIPVVCLESD NGNIMIQKHD GITVAVHKMA S
