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Protein

Ragulator complex protein LAMTOR1

Gene

Lamtor1

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

Functioni

As part of the Ragulator complex it is 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. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell growth Source: UniProtKB
  • cellular protein localization Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • cholesterol homeostasis Source: UniProtKB
  • endosome localization Source: UniProtKB
  • endosome organization Source: UniProtKB
  • lysosome localization Source: UniProtKB
  • lysosome organization Source: UniProtKB
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of TOR signaling Source: UniProtKB
  • regulation of cholesterol efflux Source: UniProtKB
  • regulation of cholesterol esterification Source: UniProtKB
  • regulation of cholesterol import Source: UniProtKB
  • regulation of receptor recycling Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR1
Alternative name(s):
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1
Lipid raft adaptor protein p18
Gene namesi
Name:Lamtor1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1913758. Lamtor1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryos die at egg cylinder stage due to growth retardation, associated with altered endosomes and lysosomes organizations and impaired membrane protein transport in the visceral endoderm.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 161160Ragulator complex protein LAMTOR1PRO_0000274293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei28 – 281PhosphothreonineCombined sources

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9CQ22.
MaxQBiQ9CQ22.
PaxDbiQ9CQ22.
PRIDEiQ9CQ22.

PTM databases

iPTMnetiQ9CQ22.
PhosphoSiteiQ9CQ22.
SwissPalmiQ9CQ22.

Expressioni

Developmental stagei

At E6.5 expressed throughout the embryo with relative abundance in the visceral endoderm.1 Publication

Gene expression databases

BgeeiQ9CQ22.
CleanExiMM_2400001E08RIK.
ExpressionAtlasiQ9CQ22. baseline and differential.
GenevisibleiQ9CQ22. MM.

Interactioni

Subunit structurei

Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator complex interacts with both the mTORC1 complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid availability. The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with LAMTOR2 and LAMTOR3; the interaction is direct (PubMed:19177150). Interacts with RRAGB and RRAGD; the interaction is direct indicating that it probably constitutes the main RAG-interacting subunit of the Ragulator complex. Interacts with MMP14. Interacts with CDKN1B; prevents the interaction of CDKN1B with RHOA leaving RHOA in a form accessible to activation by ARHGEF2 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi211525. 1 interaction.
IntActiQ9CQ22. 6 interactions.
MINTiMINT-4124770.
STRINGi10090.ENSMUSP00000033131.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 16141Interaction with LAMTOR2 and LAMTOR3By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the LAMTOR1 family.Curated

Phylogenomic databases

eggNOGiENOG410IH39. Eukaryota.
ENOG4112AMJ. LUCA.
GeneTreeiENSGT00390000016789.
HOVERGENiHBG081218.
InParanoidiQ9CQ22.
OMAiNLVVPFR.
OrthoDBiEOG7GXPDX.
PhylomeDBiQ9CQ22.
TreeFamiTF323788.

Family and domain databases

InterProiIPR026310. LAMTOR1-like.
IPR028209. LAMTOR1/MEH1.
[Graphical view]
PANTHERiPTHR13401. PTHR13401. 1 hit.
PfamiPF15454. LAMTOR. 1 hit.
[Graphical view]
SMARTiSM01262. LAMTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCCYSSENE DSDQDREERK LLLDPSSTPT KALNGAEPNY HSLPSARTDE
60 70 80 90 100
QALLSSILAK TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT
110 120 130 140 150
HWKKLPPLPS LTSQPHQVLA SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA
160
KEELVVQFGI P
Length:161
Mass (Da):17,749
Last modified:June 1, 2001 - v1
Checksum:iD50CC6C05C36B457
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821M → I in BAB28825 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009320 mRNA. Translation: BAB26214.1.
AK013389 mRNA. Translation: BAB28825.1.
AK019947 mRNA. Translation: BAB31928.1.
AK144476 mRNA. Translation: BAE25909.1.
BC020142 mRNA. Translation: AAH20142.1.
BC092062 mRNA. Translation: AAH92062.1.
BC096412 mRNA. Translation: AAH96412.1.
BC115458 mRNA. No translation available.
BC115459 mRNA. No translation available.
BC126973 mRNA. Translation: AAI26974.1.
CCDSiCCDS21519.1.
RefSeqiNP_079881.2. NM_025605.3.
UniGeneiMm.214841.
Mm.30003.

Genome annotation databases

EnsembliENSMUST00000033131; ENSMUSP00000033131; ENSMUSG00000030842.
GeneIDi66508.
KEGGimmu:66508.
UCSCiuc009ipw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009320 mRNA. Translation: BAB26214.1.
AK013389 mRNA. Translation: BAB28825.1.
AK019947 mRNA. Translation: BAB31928.1.
AK144476 mRNA. Translation: BAE25909.1.
BC020142 mRNA. Translation: AAH20142.1.
BC092062 mRNA. Translation: AAH92062.1.
BC096412 mRNA. Translation: AAH96412.1.
BC115458 mRNA. No translation available.
BC115459 mRNA. No translation available.
BC126973 mRNA. Translation: AAI26974.1.
CCDSiCCDS21519.1.
RefSeqiNP_079881.2. NM_025605.3.
UniGeneiMm.214841.
Mm.30003.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211525. 1 interaction.
IntActiQ9CQ22. 6 interactions.
MINTiMINT-4124770.
STRINGi10090.ENSMUSP00000033131.

PTM databases

iPTMnetiQ9CQ22.
PhosphoSiteiQ9CQ22.
SwissPalmiQ9CQ22.

Proteomic databases

EPDiQ9CQ22.
MaxQBiQ9CQ22.
PaxDbiQ9CQ22.
PRIDEiQ9CQ22.

Protocols and materials databases

DNASUi66508.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033131; ENSMUSP00000033131; ENSMUSG00000030842.
GeneIDi66508.
KEGGimmu:66508.
UCSCiuc009ipw.2. mouse.

Organism-specific databases

CTDi55004.
MGIiMGI:1913758. Lamtor1.

Phylogenomic databases

eggNOGiENOG410IH39. Eukaryota.
ENOG4112AMJ. LUCA.
GeneTreeiENSGT00390000016789.
HOVERGENiHBG081218.
InParanoidiQ9CQ22.
OMAiNLVVPFR.
OrthoDBiEOG7GXPDX.
PhylomeDBiQ9CQ22.
TreeFamiTF323788.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

PROiQ9CQ22.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ22.
CleanExiMM_2400001E08RIK.
ExpressionAtlasiQ9CQ22. baseline and differential.
GenevisibleiQ9CQ22. MM.

Family and domain databases

InterProiIPR026310. LAMTOR1-like.
IPR028209. LAMTOR1/MEH1.
[Graphical view]
PANTHERiPTHR13401. PTHR13401. 1 hit.
PfamiPF15454. LAMTOR. 1 hit.
[Graphical view]
SMARTiSM01262. LAMTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Embryo, Head, Ovary, Tongue and Uterus.
  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].
    Strain: Czech II and FVB/N.
    Tissue: Lung and Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes."
    Nada S., Hondo A., Kasai A., Koike M., Saito K., Uchiyama Y., Okada M.
    EMBO J. 28:477-489(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH LAMTOR2 AND LAMTOR3, DEVELOPMENTAL STAGE.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLTOR1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ22
Secondary accession number(s): Q9CYS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 107 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.