LTOR5_HUMAN
ID LTOR5_HUMAN Reviewed; 91 AA.
AC O43504; Q6IBD8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ragulator complex protein LAMTOR5;
DE AltName: Full=Hepatitis B virus X-interacting protein {ECO:0000303|PubMed:9499022, ECO:0000303|Ref.2};
DE Short=HBV X-interacting protein {ECO:0000303|PubMed:9499022, ECO:0000303|Ref.2};
DE Short=HBX-interacting protein {ECO:0000303|PubMed:9499022, ECO:0000303|Ref.2};
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5;
GN Name=LAMTOR5;
GN Synonyms=HBXIP {ECO:0000303|Ref.2}, XIP {ECO:0000303|PubMed:9499022};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF THR-12 AND THR-36, AND
RP INTERACTION WITH HBX (MICROBIAL INFECTION).
RC TISSUE=Liver;
RX PubMed=9499022; DOI=10.1128/jvi.72.3.1737-1743.1998;
RA Melegari M., Scaglioni P.P., Wands J.R.;
RT "Cloning and characterization of a novel hepatitis B virus x binding
RT protein that inhibits viral replication.";
RL J. Virol. 72:1737-1743(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RA Zhang X., Ye L., Shi Z.;
RT "Clone of human uterus hepatitis B virus x interacting protein (HBXIP)
RT gene.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Melanoma;
RA Bienvenut W.V., Quadroni M.;
RL Submitted (JUL-2005) to UniProtKB.
RN [8]
RP FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH BIRC5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12773388; DOI=10.1093/emboj/cdg263;
RA Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I.,
RA Reed J.C.;
RT "HBXIP functions as a cofactor of survivin in apoptosis suppression.";
RL EMBO J. 22:2729-2740(2003).
RN [9]
RP INTERACTION WITH SUPV3L1, AND SUBCELLULAR LOCATION.
RX PubMed=16176273; DOI=10.1111/j.1742-4658.2005.04910.x;
RA Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P.;
RT "Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of
RT survivin HBXIP.";
RL FEBS J. 272:5008-5019(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX,
RP INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES, AND SUBCELLULAR LOCATION.
RX PubMed=22980980; DOI=10.1016/j.cell.2012.07.032;
RA Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.;
RT "Ragulator is a GEF for the Rag GTPases that signal amino acid levels to
RT mTORC1.";
RL Cell 150:1196-1208(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH SLC38A9.
RX PubMed=25561175; DOI=10.1038/nature14107;
RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M.,
RA Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X.,
RA Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.;
RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery that
RT controls mTORC1.";
RL Nature 519:477-481(2015).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INTERACTION WITH SLC38A9.
RX PubMed=25567906; DOI=10.1126/science.1257132;
RA Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
RA Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L.,
RA Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.;
RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT sufficiency to mTORC1.";
RL Science 347:188-194(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS), AND SUBUNIT.
RX PubMed=21059355; DOI=10.1016/j.jmb.2010.10.046;
RA Garcia-Saez I., Lacroix F.B., Blot D., Gabel F., Skoufias D.A.;
RT "Structural characterization of HBXIP: the protein that interacts with the
RT anti-apoptotic protein survivin and the oncogenic viral protein HBx.";
RL J. Mol. Biol. 405:331-340(2011).
RN [19] {ECO:0007744|PDB:6ULG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR2; LAMTOR3 AND LAMTOR4, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31704029; DOI=10.1016/j.cell.2019.10.036;
RA Shen K., Rogala K.B., Chou H.T., Huang R.K., Yu Z., Sabatini D.M.;
RT "Cryo-EM structure of the human FLCN-FNIP2-Rag-Ragulator complex.";
RL Cell 179:1319-1329(2019).
RN [20] {ECO:0007744|PDB:6NZD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR2; LAMTOR3 AND LAMTOR4, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31672913; DOI=10.1126/science.aax0364;
RA Lawrence R.E., Fromm S.A., Fu Y., Yokom A.L., Kim D.J., Thelen A.M.,
RA Young L.N., Lim C.Y., Samelson A.J., Hurley J.H., Zoncu R.;
RT "Structural mechanism of a Rag GTPase activation checkpoint by the
RT lysosomal folliculin complex.";
RL Science 366:971-977(2019).
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. Down-regulates hepatitis B virus
CC (HBV) replication. {ECO:0000269|PubMed:12773388,
CC ECO:0000269|PubMed:22980980}.
CC -!- SUBUNIT: Homodimer (PubMed:21059355). Part of the Ragulator complex
CC composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and
CC LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a
CC LAMTOR2, LAMTOR3 heterodimer (PubMed:22980980). The Ragulator complex
CC interacts with both the mTORC1 complex and heterodimers constituted of
CC the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid
CC availability (PubMed:22980980). The Ragulator complex interacts with
CC SLC38A9; the probable amino acid sensor (PubMed:25561175,
CC PubMed:25567906). Component of the lysosomal folliculin complex (LFC),
CC composed of FLCN, FNIP1 (or FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound,
CC RRAGC/RagC or RRAGD/RagD GTP-bound, and Ragulator (PubMed:31704029,
CC PubMed:31672913). Interacts with phosphorylated BIRC5; the resulting
CC complex binds pro-caspase-9, as well as active caspase-9, but much less
CC efficiently (PubMed:12773388). Interacts with SUPV3L1
CC (PubMed:16176273). {ECO:0000269|PubMed:12773388,
CC ECO:0000269|PubMed:16176273, ECO:0000269|PubMed:21059355,
CC ECO:0000269|PubMed:22980980, ECO:0000269|PubMed:25561175,
CC ECO:0000269|PubMed:25567906, ECO:0000269|PubMed:31672913,
CC ECO:0000269|PubMed:31704029}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus (HBV)
CC oncoprotein HBX C-terminus. {ECO:0000269|PubMed:9499022}.
CC -!- INTERACTION:
CC O43504; Q0VGL1: LAMTOR4; NbExp=5; IntAct=EBI-713382, EBI-5658976;
CC O43504; Q8NBW4: SLC38A9; NbExp=4; IntAct=EBI-713382, EBI-9978316;
CC O43504; Q14765: STAT4; NbExp=2; IntAct=EBI-713382, EBI-1186538;
CC O43504; PRO_0000037547 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-713382, EBI-9028527;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:22980980}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:12773388}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac muscle,
CC followed by pancreas, kidney, liver, brain, placenta and lung. Elevated
CC levels in both cancerous and non-cancerous liver tissue of patients
CC with chronic HBV infection compared with hepatic tissue without HBV
CC infection.
CC -!- MISCELLANEOUS: Suppression of caspase activation by the BIRC5/HBXIP
CC complex is increased in the presence of HBX.
CC -!- SIMILARITY: Belongs to the LAMTOR5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62619.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF029890; AAC52032.1; -; mRNA.
DR EMBL; AY623819; AAV30683.1; -; mRNA.
DR EMBL; CR456866; CAG33147.1; -; mRNA.
DR EMBL; CR542130; CAG46927.1; -; mRNA.
DR EMBL; AL390797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062619; AAH62619.2; ALT_INIT; mRNA.
DR RefSeq; NP_006393.2; NM_006402.2.
DR PDB; 3MS6; X-ray; 2.08 A; A=1-91.
DR PDB; 3MSH; X-ray; 1.51 A; A=1-91.
DR PDB; 5VOK; X-ray; 2.89 A; A/C/E/G=1-91.
DR PDB; 5X6U; X-ray; 2.40 A; C=1-91.
DR PDB; 5X6V; X-ray; 2.02 A; C=1-91.
DR PDB; 5Y38; X-ray; 2.80 A; A=1-91.
DR PDB; 5Y39; X-ray; 2.65 A; E/J=1-90.
DR PDB; 5Y3A; X-ray; 2.90 A; E/J=1-91.
DR PDB; 5YK3; X-ray; 3.01 A; E/J=1-91, o=1-90.
DR PDB; 6EHP; X-ray; 2.30 A; C=1-91.
DR PDB; 6EHR; X-ray; 2.90 A; C=1-91.
DR PDB; 6NZD; EM; 3.60 A; E=1-91.
DR PDB; 6U62; EM; 3.18 A; H=1-91.
DR PDB; 6ULG; EM; 3.31 A; C=1-91.
DR PDB; 7T3A; EM; 4.00 A; Q=1-91.
DR PDB; 7T3B; EM; 3.90 A; J=1-91.
DR PDB; 7T3C; EM; 4.00 A; J/Q=1-91.
DR PDBsum; 3MS6; -.
DR PDBsum; 3MSH; -.
DR PDBsum; 5VOK; -.
DR PDBsum; 5X6U; -.
DR PDBsum; 5X6V; -.
DR PDBsum; 5Y38; -.
DR PDBsum; 5Y39; -.
DR PDBsum; 5Y3A; -.
DR PDBsum; 5YK3; -.
DR PDBsum; 6EHP; -.
DR PDBsum; 6EHR; -.
DR PDBsum; 6NZD; -.
DR PDBsum; 6U62; -.
DR PDBsum; 6ULG; -.
DR PDBsum; 7T3A; -.
DR PDBsum; 7T3B; -.
DR PDBsum; 7T3C; -.
DR AlphaFoldDB; O43504; -.
DR SMR; O43504; -.
DR BioGRID; 115796; 145.
DR ComplexPortal; CPX-4741; Ragulator complex.
DR CORUM; O43504; -.
DR DIP; DIP-61482N; -.
DR IntAct; O43504; 64.
DR MINT; O43504; -.
DR STRING; 9606.ENSP00000256644; -.
DR iPTMnet; O43504; -.
DR PhosphoSitePlus; O43504; -.
DR BioMuta; LAMTOR5; -.
DR EPD; O43504; -.
DR jPOST; O43504; -.
DR MassIVE; O43504; -.
DR MaxQB; O43504; -.
DR PaxDb; O43504; -.
DR PeptideAtlas; O43504; -.
DR PRIDE; O43504; -.
DR ProteomicsDB; 48997; -.
DR TopDownProteomics; O43504; -.
DR Antibodypedia; 1857; 173 antibodies from 28 providers.
DR DNASU; 10542; -.
DR Ensembl; ENST00000602318.6; ENSP00000473439.1; ENSG00000134248.14.
DR GeneID; 10542; -.
DR KEGG; hsa:10542; -.
DR MANE-Select; ENST00000602318.6; ENSP00000473439.1; NM_001382293.1; NP_001369222.1.
DR UCSC; uc001dzr.4; human.
DR CTD; 10542; -.
DR DisGeNET; 10542; -.
DR GeneCards; LAMTOR5; -.
DR HGNC; HGNC:17955; LAMTOR5.
DR HPA; ENSG00000134248; Low tissue specificity.
DR MIM; 608521; gene.
DR neXtProt; NX_O43504; -.
DR OpenTargets; ENSG00000134248; -.
DR PharmGKB; PA29211; -.
DR VEuPathDB; HostDB:ENSG00000134248; -.
DR eggNOG; ENOG502S5TK; Eukaryota.
DR GeneTree; ENSGT00390000006247; -.
DR HOGENOM; CLU_164970_0_0_1; -.
DR InParanoid; O43504; -.
DR OMA; AKGNINP; -.
DR OrthoDB; 1405682at2759; -.
DR PhylomeDB; O43504; -.
DR TreeFam; TF324433; -.
DR PathwayCommons; O43504; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-165159; MTOR signalling.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; O43504; -.
DR SIGNOR; O43504; -.
DR BioGRID-ORCS; 10542; 67 hits in 1084 CRISPR screens.
DR ChiTaRS; LAMTOR5; human.
DR EvolutionaryTrace; O43504; -.
DR GeneWiki; HBXIP; -.
DR GenomeRNAi; 10542; -.
DR Pharos; O43504; Tbio.
DR PRO; PR:O43504; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43504; protein.
DR Bgee; ENSG00000134248; Expressed in nephron tubule and 208 other tissues.
DR ExpressionAtlas; O43504; baseline and differential.
DR Genevisible; O43504; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:ComplexPortal.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IGI:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:ARUK-UCL.
DR GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0038202; P:TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
DR InterPro; IPR024135; LAMTOR5.
DR PANTHER; PTHR13342; PTHR13342; 1.
DR Pfam; PF16672; LAMTOR5; 1.
DR PRINTS; PR02092; HEPBVIRUSXIP.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lysosome;
KW Reference proteome.
FT CHAIN 1..91
FT /note="Ragulator complex protein LAMTOR5"
FT /id="PRO_0000066007"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MUTAGEN 12
FT /note="T->A: No change."
FT /evidence="ECO:0000269|PubMed:9499022"
FT MUTAGEN 36
FT /note="T->A: No interaction with XABX14-154 (truncated form
FT of HBX)."
FT /evidence="ECO:0000269|PubMed:9499022"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:3MSH"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5VOK"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3MSH"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5VOK"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3MSH"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3MSH"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:3MSH"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5VOK"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3MSH"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:3MSH"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3MSH"
SQ SEQUENCE 91 AA; 9614 MW; 01D9E762ABC63980 CRC64;
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ QAAKLTSDPT
DIPVVCLESD NGNIMIQKHD GITVAVHKMA S
