Lamtor1 late endosomal/lysosomal adaptor, MAPK and MTOR activator 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Lamtor1provided by RGD
Official Full Name: late endosomal/lysosomal adaptor, MAPK and MTOR activator 1provided by RGD
Primary source: RGD:735078
See related: EnsemblRapid:ENSRNOG00000020016 AllianceGenome:RGD:735078
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: p18
Summary: Predicted to enable GTPase binding activity and protein-membrane adaptor activity. Predicted to contribute to guanyl-nucleotide exchange factor activity and molecular adaptor activity. Predicted to be involved in several processes, including cholesterol homeostasis; positive regulation of intracellular signal transduction; and regulation of cholesterol transport. Located in late endosome membrane and membrane raft. Orthologous to human LAMTOR1 (late endosomal/lysosomal adaptor, MAPK and MTOR activator 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in Kidney (RPKM 419.6), Heart (RPKM 334.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 1q32

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	1	NC_086019.1 (165684001..165689698)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	1	NC_051336.1 (156272116..156277687)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	1	NC_005100.4 (166991474..166997045)

Chromosome 1 - NC_086019.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

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Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

This study shows for the first time that neovascularization within the pulmonary vasculature is dependent on the prorecycling endocytic proteins Rab4 and p18.
Title: Neovascularization in the pulmonary endothelium is regulated by the endosome: Rab4-mediated trafficking and p18-dependent signaling.
Study suggest that PEBP and C11orf59 might be involved in controlling lipid or carbohydrate metabolism in diabetes via PPARalpha activation.
Title: Comparative analysis of fat and muscle proteins in fenofibrate-fed type II diabetic OLETF rats: the fenofibrate-dependent expression of PEBP or C11orf59 protein.
p18 is an endosomal membrane-anchored protein that interacts with the p14/MP1 ERK scaffold protein.
Title: The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH140986 (e-PCR)
- UniSTS:222987

NoName (e-PCR)
- UniSTS:493111

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables GTPase binding	ISO Inferred from Sequence Orthology more info
contributes_to guanyl-nucleotide exchange factor activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to guanyl-nucleotide exchange factor activity	ISO Inferred from Sequence Orthology more info
contributes_to guanyl-nucleotide exchange factor activity	ISS Inferred from Sequence or Structural Similarity more info
contributes_to molecular adaptor activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to molecular adaptor activity	ISO Inferred from Sequence Orthology more info
contributes_to molecular adaptor activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-membrane adaptor activity	ISO Inferred from Sequence Orthology more info
enables protein-membrane adaptor activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in cellular response to amino acid stimulus	IBA Inferred from Biological aspect of Ancestor more info
involved_in cellular response to amino acid stimulus	IEA Inferred from Electronic Annotation more info
involved_in cellular response to amino acid stimulus	ISO Inferred from Sequence Orthology more info
involved_in cellular response to amino acid stimulus	ISS Inferred from Sequence or Structural Similarity more info
involved_in cellular response to nutrient levels	ISO Inferred from Sequence Orthology more info
involved_in cholesterol homeostasis	IEA Inferred from Electronic Annotation more info
involved_in cholesterol homeostasis	ISO Inferred from Sequence Orthology more info
involved_in cholesterol homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in endosomal transport	IEA Inferred from Electronic Annotation more info
involved_in endosomal transport	ISO Inferred from Sequence Orthology more info
involved_in endosomal transport	ISS Inferred from Sequence or Structural Similarity more info
involved_in endosome organization	ISO Inferred from Sequence Orthology more info
involved_in endosome organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in lysosome localization	ISO Inferred from Sequence Orthology more info
involved_in lysosome localization	ISS Inferred from Sequence or Structural Similarity more info
involved_in lysosome organization	IEA Inferred from Electronic Annotation more info
involved_in lysosome organization	ISO Inferred from Sequence Orthology more info
involved_in lysosome organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of MAPK cascade	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of MAPK cascade	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of MAPK cascade	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of MAPK cascade	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of TOR signaling	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of TOR signaling	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of TOR signaling	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of TORC1 signaling	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of TORC1 signaling	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein localization to lysosome	ISO Inferred from Sequence Orthology more info
involved_in protein localization	ISO Inferred from Sequence Orthology more info
involved_in protein localization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein localization to membrane	ISO Inferred from Sequence Orthology more info
involved_in protein localization to membrane	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of cell growth	ISO Inferred from Sequence Orthology more info
involved_in regulation of cell growth	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of cholesterol efflux	ISO Inferred from Sequence Orthology more info
involved_in regulation of cholesterol efflux	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of cholesterol import	ISO Inferred from Sequence Orthology more info
involved_in regulation of cholesterol import	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of receptor recycling	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of receptor recycling	IEA Inferred from Electronic Annotation more info
involved_in regulation of receptor recycling	ISO Inferred from Sequence Orthology more info
involved_in regulation of receptor recycling	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
part_of FNIP-folliculin RagC/D GAP	ISO Inferred from Sequence Orthology more info
part_of Ragulator complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Ragulator complex	IEA Inferred from Electronic Annotation more info
part_of Ragulator complex	ISO Inferred from Sequence Orthology more info
part_of Ragulator complex	ISS Inferred from Sequence or Structural Similarity more info
located_in late endosome membrane	IDA Inferred from Direct Assay more info	PubMed
located_in late endosome membrane	IEA Inferred from Electronic Annotation more info
is_active_in lysosomal membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in lysosomal membrane	IEA Inferred from Electronic Annotation more info
is_active_in lysosomal membrane	ISO Inferred from Sequence Orthology more info
is_active_in lysosomal membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in lysosome	ISO Inferred from Sequence Orthology more info
located_in lysosome	ISS Inferred from Sequence or Structural Similarity more info
located_in membrane raft	IDA Inferred from Direct Assay more info	PubMed
located_in membrane raft	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: ragulator complex protein LAMTOR1

Names: RhoA activator C11orf59 homolog; late endosomal/lysosomal adaptor and MAPK and MTOR activator 1; lipid raft adaptor protein p18; p27Kip1-releasing factor from RhoA; p27RF-Rho

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.