LTOR1_BOVIN
ID LTOR1_BOVIN Reviewed; 161 AA.
AC Q3T0D8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ragulator complex protein LAMTOR1;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1;
GN Name=LAMTOR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. LAMTOR1 is directly responsible for anchoring the
CC Ragulator complex to membranes. Also required for late
CC endosomes/lysosomes biogenesis it may regulate both the recycling of
CC receptors through endosomes and the MAPK signaling pathway through
CC recruitment of some of its components to late endosomes. May be
CC involved in cholesterol homeostasis regulating LDL uptake and
CC cholesterol release from late endosomes/lysosomes. May also play a role
CC in RHOA activation (By similarity). Involved in the control of
CC embryonic stem cells differentiation; together with FLCN it is
CC necessary to recruit and activate RRAGC/RagC and RRAGD/RagD at the
CC lysosomes, and to induce exit of embryonic stem cells from pluripotency
CC via non-canonical, mTOR-independent TFE3 inactivation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9CQ22}.
CC -!- SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2,
CC LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer
CC that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer.
CC Interacts with LAMTOR2 and LAMTOR3; the interaction is direct. The
CC Ragulator complex interacts with both the mTORC1 complex and
CC heterodimers constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and
CC RRAGD; regulated by amino acid availability. The Ragulator complex
CC interacts with SLC38A9; the probable amino acid sensor. Component of
CC the lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or
CC FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD
CC GTP-bound, and Ragulator. Interacts with RRAGB and RRAGD; the
CC interaction is direct indicating that it probably constitutes the main
CC RAG-interacting subunit of the Ragulator complex. Interacts with MMP14.
CC Interacts with CDKN1B; prevents the interaction of CDKN1B with RHOA
CC leaving RHOA in a form accessible to activation by ARHGEF2. Interacts
CC with PIP4P1. {ECO:0000250|UniProtKB:Q6IAA8}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q6IAA8}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q6IAA8}.
CC -!- SIMILARITY: Belongs to the LAMTOR1 family. {ECO:0000305}.
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DR EMBL; BC102442; AAI02443.1; -; mRNA.
DR RefSeq; NP_001029941.1; NM_001034769.1.
DR AlphaFoldDB; Q3T0D8; -.
DR SMR; Q3T0D8; -.
DR STRING; 9913.ENSBTAP00000003907; -.
DR PaxDb; Q3T0D8; -.
DR PeptideAtlas; Q3T0D8; -.
DR PRIDE; Q3T0D8; -.
DR Ensembl; ENSBTAT00000003907; ENSBTAP00000003907; ENSBTAG00000003001.
DR GeneID; 614849; -.
DR KEGG; bta:614849; -.
DR CTD; 55004; -.
DR VEuPathDB; HostDB:ENSBTAG00000003001; -.
DR VGNC; VGNC:30779; LAMTOR1.
DR eggNOG; ENOG502RYX2; Eukaryota.
DR GeneTree; ENSGT00940000167530; -.
DR HOGENOM; CLU_136283_1_0_1; -.
DR InParanoid; Q3T0D8; -.
DR OMA; LHETAAN; -.
DR OrthoDB; 1420294at2759; -.
DR TreeFam; TF323788; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000003001; Expressed in monocyte and 105 other tissues.
DR ExpressionAtlas; Q3T0D8; baseline and differential.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071986; C:Ragulator complex; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0010872; P:regulation of cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0060620; P:regulation of cholesterol import; ISS:UniProtKB.
DR GO; GO:0001919; P:regulation of receptor recycling; ISS:UniProtKB.
DR InterPro; IPR028209; LAMTOR1/MEH1.
DR Pfam; PF15454; LAMTOR; 1.
DR SMART; SM01262; LAMTOR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; Lipoprotein; Lysosome; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT CHAIN 2..161
FT /note="Ragulator complex protein LAMTOR1"
FT /id="PRO_0000274291"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..161
FT /note="Interaction with LAMTOR2 and LAMTOR3"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q6IAA8"
SQ SEQUENCE 161 AA; 17731 MW; A20CC6C54826D86A CRC64;
MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE QALLSSILAK
TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT HWKKLPPLPS LTSQPHQVLA
SEPVPFSDLQ QVSRIAAYAY SALSQIRVDA KEELVVQFGI P
