LTOR1_HUMAN
ID LTOR1_HUMAN Reviewed; 161 AA.
AC Q6IAA8; Q8WZ09; Q9NWT0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ragulator complex protein LAMTOR1;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1;
DE AltName: Full=Lipid raft adaptor protein p18;
DE AltName: Full=Protein associated with DRMs and endosomes;
DE AltName: Full=p27Kip1-releasing factor from RhoA;
DE Short=p27RF-Rho;
GN Name=LAMTOR1; Synonyms=C11orf59, PDRO; ORFNames=PP7157;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP PROTEIN SEQUENCE OF 48-60 AND 135-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MMP14 AND CDKN1B.
RX PubMed=19654316; DOI=10.1074/jbc.m109.041400;
RA Hoshino D., Tomari T., Nagano M., Koshikawa N., Seiki M.;
RT "A novel protein associated with membrane-type 1 matrix metalloproteinase
RT binds p27(kip1) and regulates RhoA activation, actin remodeling, and
RT matrigel invasion.";
RL J. Biol. Chem. 284:27315-27326(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP FUNCTION, IDENTIFICATION IN RAGULATOR COMPLEX, AND INTERACTION WITH RRAGB
RP AND RRAGD.
RX PubMed=20381137; DOI=10.1016/j.cell.2010.02.024;
RA Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.;
RT "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is
RT necessary for its activation by amino acids.";
RL Cell 141:290-303(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY CHOLESTEROL.
RX PubMed=20544018; DOI=10.1371/journal.pone.0010977;
RA Guillaumot P., Luquain C., Malek M., Huber A.L., Brugiere S., Garin J.,
RA Grunwald D., Regnier D., Petrilli V., Lefai E., Manie S.N.;
RT "Pdro, a protein associated with late endosomes and lysosomes and
RT implicated in cellular cholesterol homeostasis.";
RL PLoS ONE 5:E10977-E10977(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX, AND
RP INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES.
RX PubMed=22980980; DOI=10.1016/j.cell.2012.07.032;
RA Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.;
RT "Ragulator is a GEF for the Rag GTPases that signal amino acid levels to
RT mTORC1.";
RL Cell 150:1196-1208(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-42; SER-56; SER-98
RP AND SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [20]
RP INTERACTION WITH SLC38A9.
RX PubMed=25561175; DOI=10.1038/nature14107;
RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M.,
RA Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X.,
RA Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.;
RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery that
RT controls mTORC1.";
RL Nature 519:477-481(2015).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP INTERACTION WITH SLC38A9.
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).
RN [23]
RP INTERACTION WITH PIP4P1.
RX PubMed=29644770; DOI=10.1111/gtc.12583;
RA Hashimoto Y., Shirane M., Nakayama K.I.;
RT "TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1
RT activation.";
RL Genes Cells 23:418-434(2018).
RN [24] {ECO:0007744|PDB:6ULG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31704029; DOI=10.1016/j.cell.2019.10.036;
RA Shen K., Rogala K.B., Chou H.T., Huang R.K., Yu Z., Sabatini D.M.;
RT "Cryo-EM structure of the human FLCN-FNIP2-Rag-Ragulator complex.";
RL Cell 179:1319-1329(2019).
RN [25] {ECO:0007744|PDB:6NZD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 5-161 IN COMPLEX WITH
RP FLCN; FNIP2; RRAGA; RRAGC; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31672913; DOI=10.1126/science.aax0364;
RA Lawrence R.E., Fromm S.A., Fu Y., Yokom A.L., Kim D.J., Thelen A.M.,
RA Young L.N., Lim C.Y., Samelson A.J., Hurley J.H., Zoncu R.;
RT "Structural mechanism of a Rag GTPase activation checkpoint by the
RT lysosomal folliculin complex.";
RL Science 366:971-977(2019).
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. LAMTOR1 is directly responsible for anchoring the
CC Ragulator complex to membranes. Also required for late
CC endosomes/lysosomes biogenesis it may regulate both the recycling of
CC receptors through endosomes and the MAPK signaling pathway through
CC recruitment of some of its components to late endosomes. May be
CC involved in cholesterol homeostasis regulating LDL uptake and
CC cholesterol release from late endosomes/lysosomes. May also play a role
CC in RHOA activation. Involved in the control of embryonic stem cells
CC differentiation; together with FLCN it is necessary to recruit and
CC activate RRAGC/RagC and RRAGD/RagD at the lysosomes, and to induce exit
CC of embryonic stem cells from pluripotency via non-canonical, mTOR-
CC independent TFE3 inactivation (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQ22, ECO:0000269|PubMed:19654316,
CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:20544018,
CC ECO:0000269|PubMed:22980980}.
CC -!- SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2,
CC LAMTOR3, LAMTOR4 and LAMTOR5 (PubMed:20381137, PubMed:22980980).
CC LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1,
CC with a LAMTOR2, LAMTOR3 heterodimer (PubMed:20381137, PubMed:22980980).
CC Interacts with LAMTOR2 and LAMTOR3; the interaction is direct
CC (PubMed:20381137, PubMed:22980980). The Ragulator complex interacts
CC with both the mTORC1 complex and heterodimers constituted of the Rag
CC GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid
CC availability (PubMed:20381137, PubMed:22980980). The Ragulator complex
CC interacts with SLC38A9; the probable amino acid sensor
CC (PubMed:25561175, PubMed:25567906). Component of the lysosomal
CC folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2),
CC RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD GTP-bound,
CC and Ragulator (PubMed:31704029, PubMed:31672913). Interacts with RRAGB
CC and RRAGD; the interaction is direct indicating that it probably
CC constitutes the main RAG-interacting subunit of the Ragulator complex
CC (PubMed:22980980). Interacts with MMP14 (PubMed:19654316). Interacts
CC with CDKN1B; prevents the interaction of CDKN1B with RHOA leaving RHOA
CC in a form accessible to activation by ARHGEF2 (PubMed:19654316).
CC Interacts with PIP4P1 (PubMed:29644770). {ECO:0000269|PubMed:19654316,
CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980,
CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
CC ECO:0000269|PubMed:29644770, ECO:0000269|PubMed:31672913,
CC ECO:0000269|PubMed:31704029}.
CC -!- INTERACTION:
CC Q6IAA8; P28329-3: CHAT; NbExp=3; IntAct=EBI-715385, EBI-25837549;
CC Q6IAA8; P78358: CTAG1B; NbExp=3; IntAct=EBI-715385, EBI-1188472;
CC Q6IAA8; P22607: FGFR3; NbExp=3; IntAct=EBI-715385, EBI-348399;
CC Q6IAA8; P06396: GSN; NbExp=3; IntAct=EBI-715385, EBI-351506;
CC Q6IAA8; Q9Y2Q5: LAMTOR2; NbExp=14; IntAct=EBI-715385, EBI-2643704;
CC Q6IAA8; P16284: PECAM1; NbExp=3; IntAct=EBI-715385, EBI-716404;
CC Q6IAA8; P20339: RAB5A; NbExp=3; IntAct=EBI-715385, EBI-399437;
CC Q6IAA8; Q7L523: RRAGA; NbExp=11; IntAct=EBI-715385, EBI-752376;
CC Q6IAA8; Q8NBW4: SLC38A9; NbExp=12; IntAct=EBI-715385, EBI-9978316;
CC Q6IAA8; P61086: UBE2K; NbExp=3; IntAct=EBI-715385, EBI-473850;
CC Q6IAA8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-715385, EBI-741480;
CC Q6IAA8; P08670: VIM; NbExp=3; IntAct=EBI-715385, EBI-353844;
CC Q6IAA8; Q9Y649; NbExp=3; IntAct=EBI-715385, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor; Cytoplasmic
CC side. Lysosome membrane {ECO:0000269|PubMed:20544018}; Lipid-anchor;
CC Cytoplasmic side. Cell membrane.
CC -!- INDUCTION: Down-regulated by cholesterol (at protein level).
CC {ECO:0000269|PubMed:20544018}.
CC -!- SIMILARITY: Belongs to the LAMTOR1 family. {ECO:0000305}.
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DR EMBL; AF289583; AAL55767.1; -; mRNA.
DR EMBL; CR457247; CAG33528.1; -; mRNA.
DR EMBL; AK000632; BAA91297.1; -; mRNA.
DR EMBL; BC001706; AAH01706.1; -; mRNA.
DR CCDS; CCDS8209.1; -.
DR RefSeq; NP_060377.1; NM_017907.2.
DR PDB; 5X6U; X-ray; 2.40 A; E=42-161.
DR PDB; 5X6V; X-ray; 2.02 A; E=42-161.
DR PDB; 5Y39; X-ray; 2.65 A; A/F=76-145.
DR PDB; 5Y3A; X-ray; 2.90 A; A/F=50-161.
DR PDB; 6B9X; X-ray; 1.42 A; A=1-161.
DR PDB; 6EHP; X-ray; 2.30 A; E=21-161.
DR PDB; 6EHR; X-ray; 2.90 A; E=21-161.
DR PDB; 6NZD; EM; 3.60 A; A=5-161.
DR PDB; 6U62; EM; 3.18 A; D=6-161.
DR PDB; 6ULG; EM; 3.31 A; E=1-161.
DR PDB; 6WJ2; EM; 3.20 A; A=1-161.
DR PDB; 6WJ3; EM; 3.90 A; A=1-161.
DR PDB; 7T3A; EM; 4.00 A; M=1-161.
DR PDB; 7T3B; EM; 3.90 A; F=1-161.
DR PDB; 7T3C; EM; 4.00 A; F/M=1-161.
DR PDBsum; 5X6U; -.
DR PDBsum; 5X6V; -.
DR PDBsum; 5Y39; -.
DR PDBsum; 5Y3A; -.
DR PDBsum; 6B9X; -.
DR PDBsum; 6EHP; -.
DR PDBsum; 6EHR; -.
DR PDBsum; 6NZD; -.
DR PDBsum; 6U62; -.
DR PDBsum; 6ULG; -.
DR PDBsum; 6WJ2; -.
DR PDBsum; 6WJ3; -.
DR PDBsum; 7T3A; -.
DR PDBsum; 7T3B; -.
DR PDBsum; 7T3C; -.
DR AlphaFoldDB; Q6IAA8; -.
DR SMR; Q6IAA8; -.
DR BioGRID; 120336; 702.
DR ComplexPortal; CPX-4741; Ragulator complex.
DR CORUM; Q6IAA8; -.
DR DIP; DIP-39650N; -.
DR IntAct; Q6IAA8; 57.
DR MINT; Q6IAA8; -.
DR STRING; 9606.ENSP00000278671; -.
DR iPTMnet; Q6IAA8; -.
DR PhosphoSitePlus; Q6IAA8; -.
DR SwissPalm; Q6IAA8; -.
DR BioMuta; LAMTOR1; -.
DR DMDM; 125863645; -.
DR EPD; Q6IAA8; -.
DR jPOST; Q6IAA8; -.
DR MassIVE; Q6IAA8; -.
DR MaxQB; Q6IAA8; -.
DR PaxDb; Q6IAA8; -.
DR PeptideAtlas; Q6IAA8; -.
DR PRIDE; Q6IAA8; -.
DR ProteomicsDB; 66364; -.
DR TopDownProteomics; Q6IAA8; -.
DR Antibodypedia; 721; 88 antibodies from 24 providers.
DR DNASU; 55004; -.
DR Ensembl; ENST00000278671.10; ENSP00000278671.5; ENSG00000149357.10.
DR GeneID; 55004; -.
DR KEGG; hsa:55004; -.
DR MANE-Select; ENST00000278671.10; ENSP00000278671.5; NM_017907.3; NP_060377.1.
DR UCSC; uc001ort.3; human.
DR CTD; 55004; -.
DR DisGeNET; 55004; -.
DR GeneCards; LAMTOR1; -.
DR HGNC; HGNC:26068; LAMTOR1.
DR HPA; ENSG00000149357; Low tissue specificity.
DR MIM; 613510; gene.
DR neXtProt; NX_Q6IAA8; -.
DR OpenTargets; ENSG00000149357; -.
DR PharmGKB; PA143485354; -.
DR VEuPathDB; HostDB:ENSG00000149357; -.
DR eggNOG; ENOG502RYX2; Eukaryota.
DR GeneTree; ENSGT00390000016789; -.
DR HOGENOM; CLU_136283_1_0_1; -.
DR InParanoid; Q6IAA8; -.
DR OMA; LHETAAN; -.
DR OrthoDB; 1274244at2759; -.
DR PhylomeDB; Q6IAA8; -.
DR TreeFam; TF323788; -.
DR PathwayCommons; Q6IAA8; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-165159; MTOR signalling.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q6IAA8; -.
DR SIGNOR; Q6IAA8; -.
DR BioGRID-ORCS; 55004; 137 hits in 1087 CRISPR screens.
DR ChiTaRS; LAMTOR1; human.
DR GenomeRNAi; 55004; -.
DR Pharos; Q6IAA8; Tbio.
DR PRO; PR:Q6IAA8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6IAA8; protein.
DR Bgee; ENSG00000149357; Expressed in monocyte and 179 other tissues.
DR ExpressionAtlas; Q6IAA8; baseline and differential.
DR Genevisible; Q6IAA8; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:ComplexPortal.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0010872; P:regulation of cholesterol esterification; IMP:UniProtKB.
DR GO; GO:0060620; P:regulation of cholesterol import; IMP:UniProtKB.
DR GO; GO:0001919; P:regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; IC:ComplexPortal.
DR InterPro; IPR028209; LAMTOR1/MEH1.
DR Pfam; PF15454; LAMTOR; 1.
DR SMART; SM01262; LAMTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Endosome;
KW Lipoprotein; Lysosome; Membrane; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..161
FT /note="Ragulator complex protein LAMTOR1"
FT /id="PRO_0000274292"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..161
FT /note="Interaction with LAMTOR2 and LAMTOR3"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT VARIANT 73
FT /note="S -> L (in dbSNP:rs1053443)"
FT /id="VAR_030250"
FT CONFLICT 50
FT /note="E -> V (in Ref. 2; CAG33528)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="K -> R (in Ref. 1; AAL55767)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="S -> P (in Ref. 2; CAG33528)"
FT /evidence="ECO:0000305"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:5X6V"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6EHR"
FT HELIX 78..95
FT /evidence="ECO:0007829|PDB:5X6V"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6EHR"
SQ SEQUENCE 161 AA; 17745 MW; 610CC6C548356051 CRC64;
MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE QALLSSILAK
TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT HWKKLPPLPS LTSQPHQVLA
SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA KEELVVQFGI P
