LTOR1_XENLA
ID LTOR1_XENLA Reviewed; 162 AA.
AC Q7SYW7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Ragulator complex protein LAMTOR1;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1;
GN Name=lamtor1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of the TOR pathway, a signaling cascade that
CC promotes cell growth in response to growth factors, energy levels, and
CC amino acids. As part of the Ragulator complex, may activate the TOR
CC signaling cascade in response to amino acids. May play a role in late
CC endosomes/lysosomes biogenesis and regulate both the recycling of
CC receptors through endosomes and the MAPK signaling pathway. May be
CC involved in cholesterol homeostasis. May also play a role in RHOA
CC activation (By similarity). Involved in the control of embryonic stem
CC cells differentiation; together with FLCN it is necessary to recruit
CC and activate RRAGC/RagC and RRAGD/RagD at the lysosomes, and to induce
CC exit of embryonic stem cells from pluripotency via non-canonical, mTOR-
CC independent TFE3 inactivation (By similarity).
CC {ECO:0000250|UniProtKB:Q6IAA8, ECO:0000250|UniProtKB:Q9CQ22}.
CC -!- SUBUNIT: Part of the Ragulator complex composed of lamtor1, lamtor2,
CC lamtor3, lamtor4 and lamtor5. The Ragulator complex interacts with
CC slc38a9; the probable amino acid sensor. Component of the lysosomal
CC folliculin complex (LFC). {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}.
CC -!- SIMILARITY: Belongs to the LAMTOR1 family. {ECO:0000305}.
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DR EMBL; BC054238; AAH54238.1; -; mRNA.
DR RefSeq; NP_001080198.1; NM_001086729.1.
DR AlphaFoldDB; Q7SYW7; -.
DR SMR; Q7SYW7; -.
DR MaxQB; Q7SYW7; -.
DR DNASU; 379890; -.
DR GeneID; 379890; -.
DR KEGG; xla:379890; -.
DR CTD; 379890; -.
DR Xenbase; XB-GENE-6079175; lamtor1.S.
DR OMA; LHETAAN; -.
DR OrthoDB; 1420294at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 379890; Expressed in internal ear and 19 other tissues.
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 Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..162
FT /note="Ragulator complex protein LAMTOR1"
FT /id="PRO_0000274296"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 162 AA; 17827 MW; D7A1DAD6EB4FAF8B CRC64;
MGCCYSGETD TGKGDQGERE HLLPQNQSLP NNKQNGSEQN PTNNPSARTD EQAMLSRILA
KTAQNIIDVS AVESQGMEQH ECMDRARQYS TRLAKLSSNL MDWKNVPPLP SLTSQPHQIL
ASDPVPFTDI QQVSKIAAYA FSALSQIRVD AKEDLVVQFG IP