ID   LTOR3_PONAB             Reviewed;         124 AA.
AC   Q5R3Z6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Ragulator complex protein LAMTOR3;
DE   AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3;
GN   Name=LAMTOR3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. Adapter protein that enhances the efficiency of the MAP
CC       kinase cascade facilitating the activation of MAPK2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UHA4}.
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 LAMTOR1 and LAMTOR2; 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 (By similarity). Interacts with MAP2K1/MEK1
CC       and MAPK2 (By similarity). Interacts with MORG1 (By similarity).
CC       {ECO:0000250|UniProtKB:O88653, ECO:0000250|UniProtKB:Q9UHA4}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LAMTOR3 family. {ECO:0000305}.
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DR   EMBL; CR861464; CAH93520.1; -; mRNA.
DR   RefSeq; NP_001127674.1; NM_001134202.1.
DR   AlphaFoldDB; Q5R3Z6; -.
DR   SMR; Q5R3Z6; -.
DR   STRING; 9601.ENSPPYP00000016698; -.
DR   GeneID; 100174756; -.
DR   KEGG; pon:100174756; -.
DR   CTD; 8649; -.
DR   eggNOG; ENOG502RYGZ; Eukaryota.
DR   InParanoid; Q5R3Z6; -.
DR   OrthoDB; 1525606at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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: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   InterPro; IPR015019; LAMTOR3.
DR   PANTHER; PTHR13378; PTHR13378; 1.
DR   Pfam; PF08923; MAPKK1_Int; 1.
DR   SMART; SM01278; MAPKK1_Int; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Membrane; Reference proteome.
FT   CHAIN           1..124
FT                   /note="Ragulator complex protein LAMTOR3"
FT                   /id="PRO_0000240657"
FT   REGION          57..70
FT                   /note="Required for interaction with LAMTOR2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13639 MW;  474C96CF41CE6BC8 CRC64;
     MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG
     SKLGLSKNKS TICYYNTYQV VQFNRLPLVV SFIASSSANT GLIVSLEKEL APLFEELRRV
     VEVS