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Ragulator complex protein LAMTOR5 (Hepatitis B virus X-interacting protein) (HBV X-interacting protein) (HBX-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5)

 LTOR5_HUMAN             Reviewed;          91 AA.
O43504; Q6IBD8;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
23-MAY-2018, entry version 147.
RecName: Full=Ragulator complex protein LAMTOR5;
AltName: Full=Hepatitis B virus X-interacting protein;
Short=HBV X-interacting protein;
Short=HBX-interacting protein;
AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5;
Name=LAMTOR5; Synonyms=HBXIP, XIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
TISSUE=Liver;
PubMed=9499022;
Melegari M., Scaglioni P.P., Wands J.R.;
"Cloning and characterization of a novel hepatitis B virus x binding
protein that inhibits viral replication.";
J. Virol. 72:1737-1743(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterus;
Zhang X., Ye L., Shi Z.;
"Clone of human uterus hepatitis B virus x interacting protein (HBXIP)
gene.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Melanoma;
Bienvenut W.V., Quadroni M.;
Submitted (JUL-2005) to UniProtKB.
[8]
FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH BIRC5, AND
SUBCELLULAR LOCATION.
PubMed=12773388; DOI=10.1093/emboj/cdg263;
Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I.,
Reed J.C.;
"HBXIP functions as a cofactor of survivin in apoptosis suppression.";
EMBO J. 22:2729-2740(2003).
[9]
INTERACTION WITH SUPV3L1, AND SUBCELLULAR LOCATION.
PubMed=16176273; DOI=10.1111/j.1742-4658.2005.04910.x;
Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P.;
"Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the
cofactor of survivin HBXIP.";
FEBS J. 272:5008-5019(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX,
INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES, AND SUBCELLULAR
LOCATION.
PubMed=22980980; DOI=10.1016/j.cell.2012.07.032;
Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.;
"Ragulator is a GEF for the Rag GTPases that signal amino acid levels
to mTORC1.";
Cell 150:1196-1208(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
INTERACTION WITH SLC38A9.
PubMed=25561175; DOI=10.1038/nature14107;
Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L.,
Bruckner M., Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W.,
Heinz L.X., Kraft C., Bennett K.L., Indiveri C., Huber L.A.,
Superti-Furga G.;
"SLC38A9 is a component of the lysosomal amino acid sensing machinery
that controls mTORC1.";
Nature 519:477-481(2015).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
INTERACTION WITH SLC38A9.
PubMed=25567906; DOI=10.1126/science.1257132;
Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T.,
Bar-Peled L., Zoncu R., Straub C., Kim C., Park J., Sabatini B.L.,
Sabatini D.M.;
"Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
sufficiency to mTORC1.";
Science 347:188-194(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS), AND SUBUNIT.
PubMed=21059355; DOI=10.1016/j.jmb.2010.10.046;
Garcia-Saez I., Lacroix F.B., Blot D., Gabel F., Skoufias D.A.;
"Structural characterization of HBXIP: the protein that interacts with
the anti-apoptotic protein survivin and the oncogenic viral protein
HBx.";
J. Mol. Biol. 405:331-340(2011).
-!- FUNCTION: As part of the Ragulator complex it is involved in amino
acid sensing and activation of mTORC1, a signaling complex
promoting cell growth in response to growth factors, energy
levels, and amino acids. Activated by amino acids through a
mechanism involving the lysosomal V-ATPase, the Ragulator
functions as a guanine nucleotide exchange factor activating the
small GTPases Rag. Activated Ragulator and Rag GTPases function as
a scaffold recruiting mTORC1 to lysosomes where it is in turn
activated. When complexed to BIRC5, interferes with apoptosome
assembly, preventing recruitment of pro-caspase-9 to oligomerized
APAF1, thereby selectively suppressing apoptosis initiated via the
mitochondrial/cytochrome c pathway. Down-regulates hepatitis B
virus (HBV) replication. {ECO:0000269|PubMed:12773388,
ECO:0000269|PubMed:22980980}.
-!- SUBUNIT: Homodimer (Probable). Part of the Ragulator complex
composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5.
LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through
LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. The Ragulator
complex interacts with both the mTORC1 complex and heterodimers
constituted of the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD;
regulated by amino acid availability. The Ragulator complex
interacts with SLC38A9; the probable amino acid sensor
(PubMed:25561175, PubMed:25567906). Interacts with phosphorylated
BIRC5; the resulting complex binds pro-caspase-9, as well as
active caspase-9, but much less efficiently. Interacts with
SUPV3L1. Interacts with hepatitis B virus (HBV) oncoprotein HBX C-
terminus. {ECO:0000269|PubMed:12773388,
ECO:0000269|PubMed:16176273, ECO:0000269|PubMed:21059355,
ECO:0000269|PubMed:22980980, ECO:0000269|PubMed:25561175,
ECO:0000269|PubMed:25567906, ECO:0000305}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-713382, EBI-9028527;
Q0VGL1:LAMTOR4; NbExp=3; IntAct=EBI-713382, EBI-5658976;
Q8NBW4:SLC38A9; NbExp=4; IntAct=EBI-713382, EBI-9978316;
Q14765:STAT4; NbExp=2; IntAct=EBI-713382, EBI-1186538;
-!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac
muscle, followed by pancreas, kidney, liver, brain, placenta and
lung. Elevated levels in both cancerous and non-cancerous liver
tissue of patients with chronic HBV infection compared with
hepatic tissue without HBV infection.
-!- MISCELLANEOUS: Suppression of caspase activation by the
BIRC5/HBXIP complex is increased in the presence of HBX.
-!- SIMILARITY: Belongs to the LAMTOR5 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH62619.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF029890; AAC52032.1; -; mRNA.
EMBL; AY623819; AAV30683.1; -; mRNA.
EMBL; CR456866; CAG33147.1; -; mRNA.
EMBL; CR542130; CAG46927.1; -; mRNA.
EMBL; AL390797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC062619; AAH62619.2; ALT_INIT; mRNA.
RefSeq; NP_006393.2; NM_006402.2.
UniGene; Hs.439815; -.
PDB; 3MS6; X-ray; 2.08 A; A=1-91.
PDB; 3MSH; X-ray; 1.51 A; A=1-91.
PDB; 5X6U; X-ray; 2.40 A; C=1-91.
PDB; 5X6V; X-ray; 2.02 A; C=1-91.
PDB; 5Y38; X-ray; 2.80 A; A=1-91.
PDB; 5Y39; X-ray; 2.65 A; E/J=1-90.
PDB; 5Y3A; X-ray; 2.90 A; E/J=1-91.
PDB; 6EHP; X-ray; 2.30 A; C=1-91.
PDB; 6EHR; X-ray; 2.90 A; C=1-91.
PDBsum; 3MS6; -.
PDBsum; 3MSH; -.
PDBsum; 5X6U; -.
PDBsum; 5X6V; -.
PDBsum; 5Y38; -.
PDBsum; 5Y39; -.
PDBsum; 5Y3A; -.
PDBsum; 6EHP; -.
PDBsum; 6EHR; -.
ProteinModelPortal; O43504; -.
SMR; O43504; -.
BioGrid; 115796; 84.
DIP; DIP-61482N; -.
IntAct; O43504; 62.
MINT; O43504; -.
STRING; 9606.ENSP00000256644; -.
iPTMnet; O43504; -.
PhosphoSitePlus; O43504; -.
BioMuta; LAMTOR5; -.
EPD; O43504; -.
MaxQB; O43504; -.
PaxDb; O43504; -.
PeptideAtlas; O43504; -.
PRIDE; O43504; -.
TopDownProteomics; O43504; -.
DNASU; 10542; -.
Ensembl; ENST00000602318; ENSP00000473439; ENSG00000134248.
GeneID; 10542; -.
KEGG; hsa:10542; -.
UCSC; uc001dzr.4; human.
CTD; 10542; -.
DisGeNET; 10542; -.
EuPathDB; HostDB:ENSG00000134248.13; -.
GeneCards; LAMTOR5; -.
H-InvDB; HIX0029151; -.
HGNC; HGNC:17955; LAMTOR5.
MIM; 608521; gene.
neXtProt; NX_O43504; -.
OpenTargets; ENSG00000134248; -.
PharmGKB; PA29211; -.
eggNOG; ENOG410IZVH; Eukaryota.
eggNOG; ENOG4111WFD; LUCA.
GeneTree; ENSGT00390000006247; -.
HOGENOM; HOG000045746; -.
HOVERGEN; HBG010343; -.
InParanoid; O43504; -.
KO; K16344; -.
PhylomeDB; O43504; -.
TreeFam; TF324433; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SIGNOR; O43504; -.
ChiTaRS; LAMTOR5; human.
EvolutionaryTrace; O43504; -.
GeneWiki; HBXIP; -.
GenomeRNAi; 10542; -.
PRO; PR:O43504; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134248; -.
CleanEx; HS_HBXIP; -.
ExpressionAtlas; O43504; baseline and differential.
Genevisible; O43504; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0061462; P:protein localization to lysosome; IMP:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
InterPro; IPR024135; LAMTOR5.
PANTHER; PTHR13342; PTHR13342; 1.
Pfam; PF16672; LAMTOR5; 1.
PRINTS; PR02092; HEPBVIRUSXIP.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Lysosome; Reference proteome.
CHAIN 1 91 Ragulator complex protein LAMTOR5.
/FTId=PRO_0000066007.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7}.
MUTAGEN 12 12 T->A: No change.
{ECO:0000269|PubMed:9499022}.
MUTAGEN 36 36 T->A: No interaction with XABX14-154
(truncated form of HBX).
{ECO:0000269|PubMed:9499022}.
HELIX 5 13 {ECO:0000244|PDB:3MSH}.
STRAND 18 24 {ECO:0000244|PDB:3MSH}.
STRAND 30 35 {ECO:0000244|PDB:3MSH}.
HELIX 39 41 {ECO:0000244|PDB:3MSH}.
HELIX 42 54 {ECO:0000244|PDB:3MSH}.
STRAND 59 61 {ECO:0000244|PDB:6EHR}.
STRAND 65 69 {ECO:0000244|PDB:3MSH}.
STRAND 72 79 {ECO:0000244|PDB:3MSH}.
STRAND 82 88 {ECO:0000244|PDB:3MSH}.
SEQUENCE 91 AA; 9614 MW; 01D9E762ABC63980 CRC64;
MEATLEQHLE DTMKNPSIVG VLCTDSQGLN LGCRGTLSDE HAGVISVLAQ QAAKLTSDPT
DIPVVCLESD NGNIMIQKHD GITVAVHKMA S


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