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Protein

Ragulator complex protein LAMTOR3

Gene

Lamtor3

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. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.2 Publications

GO - Molecular functioni

  • kinase activator activity Source: MGI

GO - Biological processi

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.
R-MMU-5674135. MAP2K and MAPK activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR3
Alternative name(s):
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3
MEK-binding partner 1
Short name:
Mp1
Mitogen-activated protein kinase kinase 1-interacting protein 1
Mitogen-activated protein kinase scaffold protein 1
Gene namesi
Name:Lamtor3
Synonyms:Map2k1ip1, Mapbp, Mapksp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 3, Chromosome 7

Organism-specific databases

MGIiMGI:1929467. Lamtor3.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • late endosome Source: UniProtKB
  • Ragulator complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Ragulator complex protein LAMTOR3PRO_0000221006Add
BLAST

Proteomic databases

EPDiO88653.
PaxDbiO88653.
PRIDEiO88653.
TopDownProteomicsiO88653.

PTM databases

iPTMnetiO88653.
PhosphoSiteiO88653.

Expressioni

Gene expression databases

BgeeiO88653.
ExpressionAtlasiO88653. baseline.
GenevisibleiO88653. 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 LAMTOR1 and LAMTOR2; the interaction is direct (PubMed:11266467, PubMed:15263099, PubMed:19177150). Interacts with MAP2K1/MEK1 and MAPK2 (PubMed:9733512). Interacts with MORG1 (PubMed:15118098).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamtor1Q6P7915EBI-1039530,EBI-919067From a different organism.
Lamtor2Q9JHS32EBI-1039530,EBI-1038198

Protein-protein interaction databases

IntActiO88653. 11 interactions.
MINTiMINT-4102054.
STRINGi10090.ENSMUSP00000136999.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Helixi13 – 153Combined sources
Beta strandi19 – 268Combined sources
Beta strandi31 – 366Combined sources
Helixi42 – 454Combined sources
Helixi47 – 504Combined sources
Helixi52 – 609Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 747Combined sources
Beta strandi76 – 8510Combined sources
Beta strandi88 – 958Combined sources
Helixi100 – 11718Combined sources
Turni118 – 1214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VETX-ray1.90A1-124[»]
1VEUX-ray2.15A1-124[»]
ProteinModelPortaliO88653.
SMRiO88653. Positions 2-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88653.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 7014Required for interaction with LAMTOR2Add
BLAST

Sequence similaritiesi

Belongs to the LAMTOR3 family.Curated

Phylogenomic databases

eggNOGiENOG410IWYZ. Eukaryota.
ENOG4111KCU. LUCA.
HOVERGENiHBG052480.
InParanoidiO88653.
KOiK04370.
OMAiDCNTGHI.
OrthoDBiEOG7V4B1G.
PhylomeDBiO88653.
TreeFamiTF324889.

Family and domain databases

InterProiIPR015019. LAMTOR3.
[Graphical view]
PANTHERiPTHR13378. PTHR13378. 1 hit.
PfamiPF08923. MAPKK1_Int. 1 hit.
[Graphical view]
SMARTiSM01278. MAPKK1_Int. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDSA PEHALRPGFL
60 70 80 90 100
STFALATDQG SKLGLSKNKS IICYYNTYQV VQFNRLPLVV SFIASSSANT
110 120
GLIVSLEKEL APLFEELIKV VEVS
Length:124
Mass (Da):13,553
Last modified:November 1, 1998 - v1
Checksum:i3B9C8A0241D806A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082526 mRNA. Translation: AAC34591.1.
BC016417 mRNA. Translation: AAH16417.1.
BC083155 mRNA. Translation: AAH83155.1.
CCDSiCCDS51078.1.
RefSeqiNP_064304.1. NM_019920.2.
UniGeneiMm.331392.

Genome annotation databases

EnsembliENSMUST00000168345; ENSMUSP00000130811; ENSMUSG00000091512.
ENSMUST00000179862; ENSMUSP00000136999; ENSMUSG00000094685.
ENSMUST00000197064; ENSMUSP00000142512; ENSMUSG00000091512.
GeneIDi56692.
KEGGimmu:56692.
UCSCiuc008rms.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082526 mRNA. Translation: AAC34591.1.
BC016417 mRNA. Translation: AAH16417.1.
BC083155 mRNA. Translation: AAH83155.1.
CCDSiCCDS51078.1.
RefSeqiNP_064304.1. NM_019920.2.
UniGeneiMm.331392.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VETX-ray1.90A1-124[»]
1VEUX-ray2.15A1-124[»]
ProteinModelPortaliO88653.
SMRiO88653. Positions 2-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88653. 11 interactions.
MINTiMINT-4102054.
STRINGi10090.ENSMUSP00000136999.

PTM databases

iPTMnetiO88653.
PhosphoSiteiO88653.

Proteomic databases

EPDiO88653.
PaxDbiO88653.
PRIDEiO88653.
TopDownProteomicsiO88653.

Protocols and materials databases

DNASUi56692.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000168345; ENSMUSP00000130811; ENSMUSG00000091512.
ENSMUST00000179862; ENSMUSP00000136999; ENSMUSG00000094685.
ENSMUST00000197064; ENSMUSP00000142512; ENSMUSG00000091512.
GeneIDi56692.
KEGGimmu:56692.
UCSCiuc008rms.1. mouse.

Organism-specific databases

CTDi8649.
MGIiMGI:1929467. Lamtor3.

Phylogenomic databases

eggNOGiENOG410IWYZ. Eukaryota.
ENOG4111KCU. LUCA.
HOVERGENiHBG052480.
InParanoidiO88653.
KOiK04370.
OMAiDCNTGHI.
OrthoDBiEOG7V4B1G.
PhylomeDBiO88653.
TreeFamiTF324889.

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.
R-MMU-5674135. MAP2K and MAPK activation.

Miscellaneous databases

EvolutionaryTraceiO88653.
PROiO88653.
SOURCEiSearch...

Gene expression databases

BgeeiO88653.
ExpressionAtlasiO88653. baseline.
GenevisibleiO88653. MM.

Family and domain databases

InterProiIPR015019. LAMTOR3.
[Graphical view]
PANTHERiPTHR13378. PTHR13378. 1 hit.
PfamiPF08923. MAPKK1_Int. 1 hit.
[Graphical view]
SMARTiSM01278. MAPKK1_Int. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade."
    Schaeffer H.J., Catling A.D., Eblen S.T., Collier L.S., Krauss A., Weber M.J.
    Science 281:1668-1671(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAP2K1/MEK1.
  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: 129.
    Tissue: Mammary gland.
  3. "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: PROTEIN SEQUENCE OF 109-119, INTERACTION WITH LAMTOR1, SUBCELLULAR LOCATION.
  4. "A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment."
    Wunderlich W., Fialka I., Teis D., Alpi A., Pfeifer A., Parton R.G., Lottspeich F., Huber L.A.
    J. Cell Biol. 152:765-776(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAMTOR2.
  5. "Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists."
    Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E., Bissonette E.A., Weber M.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MORG1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes."
    Kurzbauer R., Teis D., de Araujo M.E.G., Maurer-Stroh S., Eisenhaber F., Bourenkov G.P., Bartunik H.D., Hekman M., Rapp U.R., Huber L.A., Clausen T.
    Proc. Natl. Acad. Sci. U.S.A. 101:10984-10989(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH LAMTOR2, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLTOR3_MOUSE
AccessioniPrimary (citable) accession number: O88653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 132 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.