LTOR3_HUMAN
ID LTOR3_HUMAN Reviewed; 124 AA.
AC Q9UHA4; B2R4A1; J3KMX4; Q9H364;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ragulator complex protein LAMTOR3;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3;
DE AltName: Full=MEK-binding partner 1;
DE Short=Mp1;
DE AltName: Full=Mitogen-activated protein kinase kinase 1-interacting protein 1;
DE AltName: Full=Mitogen-activated protein kinase scaffold protein 1;
GN Name=LAMTOR3; Synonyms=MAP2K1IP1, MAPKSP1; ORFNames=PRO2783;
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] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Li Y., Huang C., Ren S., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP FUNCTION, AND IDENTIFICATION IN RAGULATOR COMPLEX.
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-124 IN COMPLEX WITH LAMTOR2.
RX PubMed=15016825; DOI=10.1074/jbc.m401648200;
RA Lunin V.V., Munger C., Wagner J., Ye Z., Cygler M., Sacher M.;
RT "The structure of the MAPK scaffold, MP1, bound to its partner, p14. A
RT complex with a critical role in endosomal MAP kinase signaling.";
RL J. Biol. Chem. 279:23422-23430(2004).
RN [15] {ECO:0007744|PDB:6ULG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR2; 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 [16] {ECO:0007744|PDB:6NZD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR2; 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. Adapter protein that enhances the efficiency of the MAP
CC kinase cascade facilitating the activation of MAPK2.
CC {ECO:0000269|PubMed:20381137, 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 LAMTOR1 and LAMTOR2; 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). The Ragulator complex interacts with
CC SLC38A9; the probable amino acid sensor (PubMed:25561175,
CC PubMed:25567906). Component of the lysosomal folliculin complex (LFC),
CC composed of FLCN, FNIP1 (or FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound,
CC RRAGC/RagC or RRAGD/RagD GTP-bound, and Ragulator (PubMed:31704029,
CC PubMed:31672913). Interacts with MAP2K1/MEK1 and MAPK2 (By similarity).
CC Interacts with MORG1 (By similarity). {ECO:0000250|UniProtKB:O88653,
CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980,
CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
CC ECO:0000269|PubMed:31672913, ECO:0000269|PubMed:31704029}.
CC -!- INTERACTION:
CC Q9UHA4; Q9BWW8: APOL6; NbExp=3; IntAct=EBI-1038192, EBI-11574440;
CC Q9UHA4; Q9Y2Q5: LAMTOR2; NbExp=18; IntAct=EBI-1038192, EBI-2643704;
CC Q9UHA4; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-1038192, EBI-740897;
CC Q9UHA4; Q8NBW4: SLC38A9; NbExp=5; IntAct=EBI-1038192, EBI-9978316;
CC Q9UHA4; P19532: TFE3; NbExp=3; IntAct=EBI-1038192, EBI-1048957;
CC Q9UHA4; Q96PF1: TGM7; NbExp=3; IntAct=EBI-1038192, EBI-12029034;
CC Q9UHA4; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-1038192, EBI-7252920;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHA4-2; Sequence=VSP_046372;
CC -!- SIMILARITY: Belongs to the LAMTOR3 family. {ECO:0000305}.
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DR EMBL; AF201947; AAF17239.1; -; mRNA.
DR EMBL; AF130115; AAG35540.1; -; mRNA.
DR EMBL; AL544981; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK311755; BAG34698.1; -; mRNA.
DR EMBL; AP001962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06112.1; -; Genomic_DNA.
DR EMBL; BC026245; AAH26245.1; -; mRNA.
DR CCDS; CCDS3652.1; -. [Q9UHA4-1]
DR CCDS; CCDS58920.1; -. [Q9UHA4-2]
DR RefSeq; NP_001230665.1; NM_001243736.1. [Q9UHA4-2]
DR RefSeq; NP_068805.1; NM_021970.3. [Q9UHA4-1]
DR PDB; 1SKO; X-ray; 2.00 A; A=2-124.
DR PDB; 2ZL1; X-ray; 2.00 A; A=2-124.
DR PDB; 3CPT; X-ray; 1.90 A; A=2-124.
DR PDB; 5X6U; X-ray; 2.40 A; A=2-124.
DR PDB; 5X6V; X-ray; 2.02 A; A=2-124.
DR PDB; 5Y39; X-ray; 2.65 A; C/H=1-124.
DR PDB; 5Y3A; X-ray; 2.90 A; C/H=1-124.
DR PDB; 6B9X; X-ray; 1.42 A; C=1-124.
DR PDB; 6EHP; X-ray; 2.30 A; A=1-124.
DR PDB; 6EHR; X-ray; 2.90 A; A=1-124.
DR PDB; 6NZD; EM; 3.60 A; C=1-124.
DR PDB; 6U62; EM; 3.18 A; F=1-124.
DR PDB; 6ULG; EM; 3.31 A; A=1-124.
DR PDB; 6WJ2; EM; 3.20 A; C=1-124.
DR PDB; 6WJ3; EM; 3.90 A; C=1-124.
DR PDB; 7T3A; EM; 4.00 A; O=1-124.
DR PDB; 7T3B; EM; 3.90 A; H=1-124.
DR PDB; 7T3C; EM; 4.00 A; H/O=1-124.
DR PDBsum; 1SKO; -.
DR PDBsum; 2ZL1; -.
DR PDBsum; 3CPT; -.
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; Q9UHA4; -.
DR SMR; Q9UHA4; -.
DR BioGRID; 114201; 123.
DR ComplexPortal; CPX-4741; Ragulator complex.
DR CORUM; Q9UHA4; -.
DR IntAct; Q9UHA4; 36.
DR MINT; Q9UHA4; -.
DR STRING; 9606.ENSP00000424183; -.
DR iPTMnet; Q9UHA4; -.
DR PhosphoSitePlus; Q9UHA4; -.
DR BioMuta; LAMTOR3; -.
DR DMDM; 24418562; -.
DR EPD; Q9UHA4; -.
DR jPOST; Q9UHA4; -.
DR MassIVE; Q9UHA4; -.
DR MaxQB; Q9UHA4; -.
DR PaxDb; Q9UHA4; -.
DR PeptideAtlas; Q9UHA4; -.
DR PRIDE; Q9UHA4; -.
DR ProteomicsDB; 84292; -. [Q9UHA4-1]
DR TopDownProteomics; Q9UHA4-1; -. [Q9UHA4-1]
DR Antibodypedia; 3792; 234 antibodies from 33 providers.
DR DNASU; 8649; -.
DR Ensembl; ENST00000226522.8; ENSP00000226522.8; ENSG00000109270.13. [Q9UHA4-2]
DR Ensembl; ENST00000499666.7; ENSP00000424183.1; ENSG00000109270.13. [Q9UHA4-1]
DR GeneID; 8649; -.
DR KEGG; hsa:8649; -.
DR MANE-Select; ENST00000499666.7; ENSP00000424183.1; NM_021970.4; NP_068805.1.
DR UCSC; uc003hvg.3; human. [Q9UHA4-1]
DR CTD; 8649; -.
DR DisGeNET; 8649; -.
DR GeneCards; LAMTOR3; -.
DR HGNC; HGNC:15606; LAMTOR3.
DR HPA; ENSG00000109270; Low tissue specificity.
DR MIM; 603296; gene.
DR neXtProt; NX_Q9UHA4; -.
DR OpenTargets; ENSG00000109270; -.
DR PharmGKB; PA164722189; -.
DR VEuPathDB; HostDB:ENSG00000109270; -.
DR eggNOG; ENOG502RYGZ; Eukaryota.
DR GeneTree; ENSGT00390000013159; -.
DR HOGENOM; CLU_134641_0_0_1; -.
DR InParanoid; Q9UHA4; -.
DR OMA; FLYKQMQ; -.
DR OrthoDB; 1525606at2759; -.
DR PhylomeDB; Q9UHA4; -.
DR TreeFam; TF324889; -.
DR PathwayCommons; Q9UHA4; -.
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-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9UHA4; -.
DR SIGNOR; Q9UHA4; -.
DR BioGRID-ORCS; 8649; 440 hits in 1061 CRISPR screens.
DR ChiTaRS; LAMTOR3; human.
DR EvolutionaryTrace; Q9UHA4; -.
DR GeneWiki; MAP2K1IP1; -.
DR GenomeRNAi; 8649; -.
DR Pharos; Q9UHA4; Tbio.
DR PRO; PR:Q9UHA4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UHA4; protein.
DR Bgee; ENSG00000109270; Expressed in mucosa of sigmoid colon and 204 other tissues.
DR Genevisible; Q9UHA4; HS.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
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:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:ComplexPortal.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:1902414; P:protein localization to cell junction; IEA:Ensembl.
DR GO; GO:0038202; P:TORC1 signaling; IC:ComplexPortal.
DR InterPro; IPR015019; LAMTOR3.
DR PANTHER; PTHR13378; PTHR13378; 1.
DR Pfam; PF08923; MAPKK1_Int; 1.
DR SMART; SM01278; MAPKK1_Int; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endosome; Membrane; Reference proteome.
FT CHAIN 1..124
FT /note="Ragulator complex protein LAMTOR3"
FT /id="PRO_0000221005"
FT REGION 57..70
FT /note="Required for interaction with LAMTOR2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 35..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046372"
FT CONFLICT 49
FT /note="F -> L (in Ref. 2; AAG35540)"
FT /evidence="ECO:0000305"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6B9X"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6EHR"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:6B9X"
SQ SEQUENCE 124 AA; 13623 MW; 0A5196CF41D83D13 CRC64;
MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG
SKLGLSKNKS IICYYNTYQV VQFNRLPLVV SFIASSSANT GLIVSLEKEL APLFEELRQV
VEVS
