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Protein

Ragulator complex protein LAMTOR5

Gene

Lamtor5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway (By similarity).By similarity

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR5
Alternative name(s):
Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
Gene namesi
Name:Lamtor5
Synonyms:Hbxip, Xip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1915826. Lamtor5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9191Ragulator complex protein LAMTOR5PRO_0000066008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D1L9.
MaxQBiQ9D1L9.
PaxDbiQ9D1L9.
PRIDEiQ9D1L9.

Expressioni

Gene expression databases

BgeeiQ9D1L9.
CleanExiMM_HBXIP.
ExpressionAtlasiQ9D1L9. baseline and differential.
GenevisibleiQ9D1L9. MM.

Interactioni

Subunit structurei

Homodimer. 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. Interacts with phosphorylated BIRC5; the resulting complex binds pro-caspase-9, as well as active caspase-9, but much less efficiently. Interacts with SUPV3L1. Interacts with hepatitis B virus (HBV) oncoprotein HBX C-terminus.By similarity

Protein-protein interaction databases

IntActiQ9D1L9. 3 interactions.
MINTiMINT-4140416.
STRINGi10090.ENSMUSP00000129012.

Structurei

3D structure databases

ProteinModelPortaliQ9D1L9.
SMRiQ9D1L9. Positions 1-91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LAMTOR5 family.Curated

Phylogenomic databases

eggNOGiENOG410IZVH. Eukaryota.
ENOG4111WFD. LUCA.
GeneTreeiENSGT00390000006247.
HOVERGENiHBG010343.
InParanoidiQ9D1L9.
KOiK16344.
PhylomeDBiQ9D1L9.

Family and domain databases

InterProiIPR024135. LAMTOR5.
[Graphical view]
PANTHERiPTHR13342. PTHR13342. 1 hit.
PfamiPF16672. LAMTOR5. 1 hit.
[Graphical view]
PRINTSiPR02092. HEPBVIRUSXIP.

Sequencei

Sequence statusi: Complete.

Q9D1L9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ
60 70 80 90
QAARLTSDPT DIPVVCLESD NGNIMIQKHD GITVAVHKMA S
Length:91
Mass (Da):9,642
Last modified:June 1, 2001 - v1
Checksum:i2CD9E762ABD07BE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003358 mRNA. Translation: BAB22734.1.
AK146289 mRNA. Translation: BAE27046.1.
BC028547 mRNA. Translation: AAH28547.1.
RefSeqiNP_081050.2. NM_026774.2.
UniGeneiMm.290035.

Genome annotation databases

EnsembliENSMUST00000199317; ENSMUSP00000143494; ENSMUSG00000087260.
GeneIDi68576.
KEGGimmu:68576.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003358 mRNA. Translation: BAB22734.1.
AK146289 mRNA. Translation: BAE27046.1.
BC028547 mRNA. Translation: AAH28547.1.
RefSeqiNP_081050.2. NM_026774.2.
UniGeneiMm.290035.

3D structure databases

ProteinModelPortaliQ9D1L9.
SMRiQ9D1L9. Positions 1-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1L9. 3 interactions.
MINTiMINT-4140416.
STRINGi10090.ENSMUSP00000129012.

Proteomic databases

EPDiQ9D1L9.
MaxQBiQ9D1L9.
PaxDbiQ9D1L9.
PRIDEiQ9D1L9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000199317; ENSMUSP00000143494; ENSMUSG00000087260.
GeneIDi68576.
KEGGimmu:68576.

Organism-specific databases

CTDi10542.
MGIiMGI:1915826. Lamtor5.

Phylogenomic databases

eggNOGiENOG410IZVH. Eukaryota.
ENOG4111WFD. LUCA.
GeneTreeiENSGT00390000006247.
HOVERGENiHBG010343.
InParanoidiQ9D1L9.
KOiK16344.
PhylomeDBiQ9D1L9.

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

NextBioi327486.
PROiQ9D1L9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1L9.
CleanExiMM_HBXIP.
ExpressionAtlasiQ9D1L9. baseline and differential.
GenevisibleiQ9D1L9. MM.

Family and domain databases

InterProiIPR024135. LAMTOR5.
[Graphical view]
PANTHERiPTHR13342. PTHR13342. 1 hit.
PfamiPF16672. LAMTOR5. 1 hit.
[Graphical view]
PRINTSiPR02092. HEPBVIRUSXIP.
ProtoNetiSearch...

Publicationsi

  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 and DBA/2.
    Tissue: Embryo.
  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].
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLTOR5_MOUSE
AccessioniPrimary (citable) accession number: Q9D1L9
Secondary accession number(s): Q3UJV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 94 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.