LST8_BOVIN
ID LST8_BOVIN Reviewed; 326 AA.
AC Q17QU5; Q58DN5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Target of rapamycin complex subunit LST8;
DE Short=TORC subunit LST8;
DE AltName: Full=G protein beta subunit-like;
DE Short=Protein GbetaL;
DE AltName: Full=Mammalian lethal with SEC13 protein 8;
DE Short=mLST8;
GN Name=MLST8; Synonyms=GBL, LST8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell
CC growth and survival in response to nutrient and hormonal signals.
CC mTORC1 is activated in response to growth factors or amino acids.
CC Growth factor-stimulated mTORC1 activation involves a AKT1-mediated
CC phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB
CC GTPase that potently activates the protein kinase activity of mTORC1.
CC Amino acid-signaling to mTORC1 requires its relocalization to the
CC lysosomes mediated by the Ragulator complex and the Rag GTPases.
CC Activated mTORC1 up-regulates protein synthesis by phosphorylating key
CC regulators of mRNA translation and ribosome synthesis. mTORC1
CC phosphorylates EIF4EBP1 and releases it from inhibiting the elongation
CC initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1
CC at 'Thr-389', which then promotes protein synthesis by phosphorylating
CC PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts
CC directly with MTOR and enhances its kinase activity. In nutrient-poor
CC conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-
CC mediated inhibition of MTOR activity. mTORC2 is also activated by
CC growth factors, but seems to be nutrient-insensitive. mTORC2 seems to
CC function upstream of Rho GTPases to regulate the actin cytoskeleton,
CC probably by activating one or more Rho-type guanine nucleotide exchange
CC factors. mTORC2 promotes the serum-induced formation of stress-fibers
CC or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473'
CC phosphorylation, which may facilitate the phosphorylation of the
CC activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite
CC for full activation. mTORC2 regulates the phosphorylation of SGK1 at
CC 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-
CC 657' (By similarity). {ECO:0000250|UniProtKB:Q9BVC4,
CC ECO:0000250|UniProtKB:Q9DCJ1}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR (By
CC similarity). mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part
CC of the mammalian target of rapamycin complex 2 (mTORC2) which contains
CC MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR (By similarity). Contrary
CC to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
CC rapamycin. Interacts directly with MTOR and RPTOR (By similarity).
CC Interacts with RHEB (By similarity). Interacts with MEAK7 (By
CC similarity). Interacts with SIK3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BVC4, ECO:0000250|UniProtKB:Q9DCJ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2K5}.
CC -!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46409.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021562; AAX46409.1; ALT_FRAME; mRNA.
DR EMBL; BC118176; AAI18177.1; -; mRNA.
DR RefSeq; NP_001030488.1; NM_001035411.1.
DR RefSeq; XP_005224583.1; XM_005224526.3.
DR AlphaFoldDB; Q17QU5; -.
DR SMR; Q17QU5; -.
DR STRING; 9913.ENSBTAP00000013104; -.
DR PaxDb; Q17QU5; -.
DR Ensembl; ENSBTAT00000013104; ENSBTAP00000013104; ENSBTAG00000009928.
DR Ensembl; ENSBTAT00000053181; ENSBTAP00000048491; ENSBTAG00000009928.
DR GeneID; 535236; -.
DR KEGG; bta:535236; -.
DR CTD; 64223; -.
DR VEuPathDB; HostDB:ENSBTAG00000009928; -.
DR VGNC; VGNC:31507; MLST8.
DR eggNOG; KOG0315; Eukaryota.
DR GeneTree; ENSGT00390000014795; -.
DR HOGENOM; CLU_000288_57_5_1; -.
DR InParanoid; Q17QU5; -.
DR OMA; VQRNYKH; -.
DR OrthoDB; 779909at2759; -.
DR TreeFam; TF318577; -.
DR Reactome; R-BTA-1632852; Macroautophagy.
DR Reactome; R-BTA-165159; MTOR signalling.
DR Reactome; R-BTA-166208; mTORC1-mediated signalling.
DR Reactome; R-BTA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009928; Expressed in retina and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037588; MLST8.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR PANTHER; PTHR19842; PTHR19842; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..326
FT /note="Target of rapamycin complex subunit LST8"
FT /id="PRO_0000326498"
FT REPEAT 1..37
FT /note="WD 1"
FT REPEAT 40..80
FT /note="WD 2"
FT REPEAT 83..122
FT /note="WD 3"
FT REPEAT 126..165
FT /note="WD 4"
FT REPEAT 168..207
FT /note="WD 5"
FT REPEAT 218..257
FT /note="WD 6"
FT REPEAT 268..309
FT /note="WD 7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVC4"
SQ SEQUENCE 326 AA; 35920 MW; D3FDCDF6EC03E541 CRC64;
MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEI TPDRTMIAAA
GYQHIRMYDL NSNNPNPIIS YDGVNKNVAS VGFHEDGRWM YTGGEDCTAR IWDLRSRNLQ
CQRIFQVNAP INCVCLHPNQ AELIVGDQSG AIHIWDLKTD HNEQLIPEPE VSITSAHIDP
DASYMAAVNS TGNCYVWNLT GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA
DQTCKIWRTS NFSLMTELSI KSSNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE
TGEIKREYGG HQKAVVCLAF NDSVLG
