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Q9DCJ1

- LST8_MOUSE

UniProt

Q9DCJ1 - LST8_MOUSE

Protein

Target of rapamycin complex subunit LST8

Gene

Mlst8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.1 Publication

    GO - Biological processi

    1. positive regulation of actin filament polymerization Source: MGI
    2. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
    3. positive regulation of TOR signaling Source: Ensembl
    4. regulation of Rac GTPase activity Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_213550. HSF1-dependent transactivation.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Target of rapamycin complex subunit LST8
    Short name:
    TORC subunit LST8
    Alternative name(s):
    G protein beta subunit-like
    Short name:
    Protein GbetaL
    Mammalian lethal with SEC13 protein 8
    Short name:
    mLST8
    Gene namesi
    Name:Mlst8
    Synonyms:Gbl, Lst8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1929514. Mlst8.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. TORC1 complex Source: MGI
    3. TORC2 complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Death around E10.5 due to multiple defects in vascular system development. In addition, they exhibit a delayed development of their cephalic region.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Target of rapamycin complex subunit LST8PRO_0000326500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9DCJ1.
    PRIDEiQ9DCJ1.

    PTM databases

    PhosphoSiteiQ9DCJ1.

    Expressioni

    Gene expression databases

    BgeeiQ9DCJ1.
    GenevestigatoriQ9DCJ1.

    Interactioni

    Subunit structurei

    Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR By similarity. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR By similarity. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts directly with MTOR and RPTOR. Interacts with RHEB By similarity. Interacts with MTOR.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi208141. 3 interactions.
    DIPiDIP-46976N.
    IntActiQ9DCJ1. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DCJ1.
    SMRiQ9DCJ1. Positions 8-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 3737WD 1Add
    BLAST
    Repeati40 – 8041WD 2Add
    BLAST
    Repeati83 – 12240WD 3Add
    BLAST
    Repeati126 – 16540WD 4Add
    BLAST
    Repeati168 – 20740WD 5Add
    BLAST
    Repeati218 – 25740WD 6Add
    BLAST
    Repeati268 – 30942WD 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat LST8 family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00390000014795.
    HOGENOMiHOG000208395.
    HOVERGENiHBG054763.
    InParanoidiQ9DCJ1.
    KOiK08266.
    OMAiAGHHTVK.
    OrthoDBiEOG7BCNBX.
    PhylomeDBiQ9DCJ1.
    TreeFamiTF318577.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 5 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DCJ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTTPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEI    50
    TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVSKNIAS VGFHEDGRWM 100
    YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG 150
    AIHIWDLKTD HNEQLIPEPE SSITSAHIDP DASYMAAVNS AGNCYVWNLT 200
    GGIGDDVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS 250
    NFSLMTELSI KSSNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE 300
    TGEIKREYGG HQKAVVCLAF NDSVLG 326
    Length:326
    Mass (Da):35,851
    Last modified:June 1, 2001 - v1
    Checksum:i2F6E75383905667A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241V → G in BAC39006. (PubMed:16141072)Curated
    Sequence conflicti127 – 1271V → G in BAC39006. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711S → F in AAF37719. (PubMed:11182770)Curated
    Sequence conflicti195 – 1951Y → F in AAF37719. (PubMed:11182770)Curated
    Sequence conflicti206 – 2061D → E in AAF37719. (PubMed:11182770)Curated
    Sequence conflicti229 – 2291S → G in BAC33243. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237676 mRNA. Translation: AAF37719.1.
    AK002751 mRNA. Translation: BAB22328.1.
    AK038515 mRNA. Translation: BAC30024.1.
    AK040100 mRNA. Translation: BAC30510.1.
    AK048102 mRNA. Translation: BAC33243.1.
    AK077680 mRNA. Translation: BAC36952.1.
    AK083731 mRNA. Translation: BAC39006.1.
    BC015279 mRNA. Translation: AAH15279.1.
    CCDSiCCDS28484.1.
    RefSeqiNP_001239392.1. NM_001252463.1.
    NP_001239393.1. NM_001252464.1.
    NP_001239394.1. NM_001252465.1.
    NP_064372.2. NM_019988.5.
    UniGeneiMm.289516.

    Genome annotation databases

    EnsembliENSMUST00000070888; ENSMUSP00000065004; ENSMUSG00000024142.
    ENSMUST00000179163; ENSMUSP00000136287; ENSMUSG00000024142.
    GeneIDi56716.
    KEGGimmu:56716.
    UCSCiuc008awg.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237676 mRNA. Translation: AAF37719.1 .
    AK002751 mRNA. Translation: BAB22328.1 .
    AK038515 mRNA. Translation: BAC30024.1 .
    AK040100 mRNA. Translation: BAC30510.1 .
    AK048102 mRNA. Translation: BAC33243.1 .
    AK077680 mRNA. Translation: BAC36952.1 .
    AK083731 mRNA. Translation: BAC39006.1 .
    BC015279 mRNA. Translation: AAH15279.1 .
    CCDSi CCDS28484.1.
    RefSeqi NP_001239392.1. NM_001252463.1.
    NP_001239393.1. NM_001252464.1.
    NP_001239394.1. NM_001252465.1.
    NP_064372.2. NM_019988.5.
    UniGenei Mm.289516.

    3D structure databases

    ProteinModelPortali Q9DCJ1.
    SMRi Q9DCJ1. Positions 8-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208141. 3 interactions.
    DIPi DIP-46976N.
    IntActi Q9DCJ1. 3 interactions.

    PTM databases

    PhosphoSitei Q9DCJ1.

    Proteomic databases

    PaxDbi Q9DCJ1.
    PRIDEi Q9DCJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070888 ; ENSMUSP00000065004 ; ENSMUSG00000024142 .
    ENSMUST00000179163 ; ENSMUSP00000136287 ; ENSMUSG00000024142 .
    GeneIDi 56716.
    KEGGi mmu:56716.
    UCSCi uc008awg.3. mouse.

    Organism-specific databases

    CTDi 64223.
    MGIi MGI:1929514. Mlst8.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00390000014795.
    HOGENOMi HOG000208395.
    HOVERGENi HBG054763.
    InParanoidi Q9DCJ1.
    KOi K08266.
    OMAi AGHHTVK.
    OrthoDBi EOG7BCNBX.
    PhylomeDBi Q9DCJ1.
    TreeFami TF318577.

    Enzyme and pathway databases

    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_213550. HSF1-dependent transactivation.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    NextBioi 313187.
    PROi Q9DCJ1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DCJ1.
    Genevestigatori Q9DCJ1.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 5 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Insulin regulation of a novel WD-40 repeat protein in adipocytes."
      Rodgers B.D., Levine M.A., Bernier M., Montrose-Rafizadeh C.
      J. Endocrinol. 168:325-332(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head, Hypothalamus, Kidney and Thymus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR."
      Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P., Erdjument-Bromage H., Tempst P., Sabatini D.M.
      Mol. Cell 11:895-904(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR.
    5. "Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1."
      Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.
      Dev. Cell 11:859-871(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
      Takai H., Xie Y., de Lange T., Pavletich N.P.
      Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR.

    Entry informationi

    Entry nameiLST8_MOUSE
    AccessioniPrimary (citable) accession number: Q9DCJ1
    Secondary accession number(s): Q8BNG8, Q8C882, Q9JKK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3