ID   LTOR5_PIG               Reviewed;          91 AA.
AC   Q66X52;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ragulator complex protein LAMTOR5;
DE   AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5;
GN   Name=LAMTOR5;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cui X.S., Jin Y.X., Hwang K.C., Kim N.H.;
RT   "Differentially expressed genes (DEGs) in porcine MII oocytes.";
RL   Submitted (JUL-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. When complexed to BIRC5, interferes with apoptosome
CC       assembly, preventing recruitment of pro-caspase-9 to oligomerized
CC       APAF1, thereby selectively suppressing apoptosis initiated via the
CC       mitochondrial/cytochrome c pathway. {ECO:0000250|UniProtKB:O43504}.
CC   -!- SUBUNIT: Homodimer. Part of the Ragulator complex composed of LAMTOR1,
CC       LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a
CC       heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3
CC       heterodimer. The Ragulator complex interacts with both the mTORC1
CC       complex and heterodimers constituted of the Rag GTPases RRAGA, RRAGB,
CC       RRAGC and RRAGD; regulated by amino acid availability. The Ragulator
CC       complex interacts with SLC38A9; the probable amino acid sensor.
CC       Component of the lysosomal folliculin complex (LFC), composed of FLCN,
CC       FNIP1 (or FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or
CC       RRAGD/RagD GTP-bound, and Ragulator. Interacts with phosphorylated
CC       BIRC5; the resulting complex binds pro-caspase-9, as well as active
CC       caspase-9, but much less efficiently. Interacts with SUPV3L1.
CC       {ECO:0000250|UniProtKB:O43504}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O43504}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43504}.
CC   -!- SIMILARITY: Belongs to the LAMTOR5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU05316.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY698063; AAU05316.1; ALT_INIT; mRNA.
DR   RefSeq; XP_013852731.1; XM_013997277.1.
DR   AlphaFoldDB; Q66X52; -.
DR   SMR; Q66X52; -.
DR   STRING; 9823.ENSSSCP00000007259; -.
DR   PaxDb; Q66X52; -.
DR   PeptideAtlas; Q66X52; -.
DR   Ensembl; ENSSSCT00060031869; ENSSSCP00060013652; ENSSSCG00060023500.
DR   GeneID; 448965; -.
DR   KEGG; ssc:448965; -.
DR   CTD; 10542; -.
DR   eggNOG; ENOG502S5TK; Eukaryota.
DR   InParanoid; Q66X52; -.
DR   OMA; AKGNINP; -.
DR   OrthoDB; 1405682at2759; -.
DR   Reactome; R-SSC-1632852; Macroautophagy.
DR   Reactome; R-SSC-165159; MTOR signalling.
DR   Reactome; R-SSC-166208; mTORC1-mediated signalling.
DR   Reactome; R-SSC-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-SSC-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-SSC-9639288; Amino acids regulate mTORC1.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0071986; C:Ragulator complex; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; ISS:UniProtKB.
DR   InterPro; IPR024135; LAMTOR5.
DR   PANTHER; PTHR13342; PTHR13342; 1.
DR   Pfam; PF16672; LAMTOR5; 1.
DR   PRINTS; PR02092; HEPBVIRUSXIP.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Lysosome; Reference proteome.
FT   CHAIN           1..91
FT                   /note="Ragulator complex protein LAMTOR5"
FT                   /id="PRO_0000331595"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O43504"
SQ   SEQUENCE   91 AA;  9614 MW;  01D9E762ABC63980 CRC64;
     MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ QAAKLTSDPT
     DIPVVCLESD NGNIMIQKHD GITVAVHKMA S