ID LST8_HUMAN Reviewed; 326 AA. AC Q9BVC4; B3KMM4; B4DY00; D3DU88; Q5M800; Q86Y18; Q8WUI5; Q9HA66; Q9UJV6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 183. DE RecName: Full=Target of rapamycin complex subunit LST8 {ECO:0000305}; DE Short=TORC subunit LST8; DE AltName: Full=G protein beta subunit-like {ECO:0000303|PubMed:12718876}; DE Short=Gable {ECO:0000303|PubMed:12718876}; DE Short=Protein GbetaL {ECO:0000303|PubMed:12718876}; DE AltName: Full=Mammalian lethal with SEC13 protein 8; DE Short=mLST8; GN Name=MLST8 {ECO:0000303|PubMed:34741373, ECO:0000312|HGNC:HGNC:24825}; GN Synonyms=GBL {ECO:0000303|PubMed:12718876}, LST8 {ECO:0000303|Ref.1}; 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] (ISOFORM 2). RA Mao Y., Li Y., Xie Y., Huo K., Hu Q.; RT "Cloning and characterization of human LST8 gene."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Embryo, Mammary gland, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, Placenta, Skin, and Uterus; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-326 (ISOFORMS 1/2). RC TISSUE=Promyelocytic leukemia; RA Ramachandiran S., Lau S.S., Monks T.J.; RT "A novel G protein beta subunit (G beta 6) in human promyelocytic leukemia RT (HL-60) cells."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP INTERACTION WITH MTOR AND RPTOR, IDENTIFICATION IN THE TORC1 COMPLEX, AND RP TISSUE SPECIFICITY. RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6; RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.; RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct RT roles in cell growth control."; RL Mol. Cell 10:457-468(2002). RN [8] RP FUNCTION, INTERACTION WITH MTOR, IDENTIFICATION IN THE TORC1 COMPLEX, RP MUTAGENESIS OF SER-72; GLY-192 AND PHE-320, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12718876; DOI=10.1016/s1097-2765(03)00114-x; RA Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P., RA Erdjument-Bromage H., Tempst P., Sabatini D.M.; RT "GbetaL, a positive regulator of the rapamycin-sensitive pathway required RT for the nutrient-sensitive interaction between raptor and mTOR."; RL Mol. Cell 11:895-904(2003). RN [9] RP FUNCTION, AND IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES. RX PubMed=15268862; DOI=10.1016/j.cub.2004.06.054; RA Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., RA Erdjument-Bromage H., Tempst P., Sabatini D.M.; RT "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive RT and raptor-independent pathway that regulates the cytoskeleton."; RL Curr. Biol. 14:1296-1302(2004). RN [10] RP IDENTIFICATION IN THE TORC2 COMPLEX, AND FUNCTION. RX PubMed=15467718; DOI=10.1038/ncb1183; RA Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.; RT "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin RT insensitive."; RL Nat. Cell Biol. 6:1122-1128(2004). RN [11] RP INTERACTION WITH RHEB. RX PubMed=15854902; DOI=10.1016/j.cub.2005.02.053; RA Long X., Lin Y., Ortiz-Vega S., Yonezawa K., Avruch J.; RT "Rheb binds and regulates the mTOR kinase."; RL Curr. Biol. 15:702-713(2005). RN [12] RP IDENTIFICATION IN THE TORC2 COMPLEX. RX PubMed=17461779; DOI=10.1042/bj20070540; RA Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M., RA Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.; RT "Identification of Protor as a novel Rictor-binding component of mTOR RT complex-2."; RL Biochem. J. 405:513-522(2007). RN [13] RP IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES. RX PubMed=17510057; DOI=10.1074/jbc.m702376200; RA Wang L., Harris T.E., Roth R.A., Lawrence J.C. Jr.; RT "PRAS40 regulates mTORC1 kinase activity by functioning as a direct RT inhibitor of substrate binding."; RL J. Biol. Chem. 282:20036-20044(2007). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE RP ANALYSIS] AT MET-1 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-7 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP FUNCTION, AND IDENTIFICATION IN THE MTORC1 COMPLEX. RX PubMed=24403073; DOI=10.1074/jbc.m113.482067; RA Coffman K., Yang B., Lu J., Tetlow A.L., Pelliccio E., Lu S., Guo D.C., RA Tang C., Dong M.Q., Tamanoi F.; RT "Characterization of the Raptor/4E-BP1 interaction by chemical cross- RT linking coupled with mass spectrometry analysis."; RL J. Biol. Chem. 289:4723-4734(2014). RN [19] RP INTERACTION WITH MEAK7. RX PubMed=29750193; DOI=10.1126/sciadv.aao5838; RA Nguyen J.T., Ray C., Fox A.L., Mendonca D.B., Kim J.K., Krebsbach P.H.; RT "Mammalian EAK-7 activates alternative mTOR signaling to regulate cell RT proliferation and migration."; RL Sci. Adv. 4:EAAO5838-EAAO5838(2018). RN [20] RP INTERACTION WITH SIK3. RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356; RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L., RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.; RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR RT signaling."; RL Sci. Transl. Med. 10:0-0(2018). RN [21] RP PHOSPHORYLATION AT THR-51, UBIQUITINATION, AND MUTAGENESIS OF THR-51 AND RP SER-55. RX PubMed=34741373; DOI=10.1111/cas.15188; RA Zhang E., Chen S., Tang H., Fei C., Yuan Z., Mu X., Qin Y., Liu H., Fan Y., RA Tan M., Wang X.; RT "CDK1/FBXW7 facilitates degradation and ubiquitination of MLST8 to inhibit RT progression of renal cell carcinoma."; RL Cancer Sci. 113:91-108(2022). RN [22] RP INTERACTION WITH SLC38A7. RX PubMed=35561222; DOI=10.1073/pnas.2123261119; RA Meng D., Yang Q., Jeong M.H., Curukovic A., Tiwary S., Melick C.H., RA Lama-Sherpa T.D., Wang H., Huerta-Rosario M., Urquhart G., Zacharias L.G., RA Lewis C., DeBerardinis R.J., Jewell J.L.; RT "SNAT7 regulates mTORC1 via macropinocytosis."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2123261119-e2123261119(2022). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH MTOR, WD REPEATS, AND RP SUBUNIT. RX PubMed=23636326; DOI=10.1038/nature12122; RA Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J., Pavletich N.P.; RT "mTOR kinase structure, mechanism and regulation."; RL Nature 497:217-223(2013). RN [24] {ECO:0007744|PDB:5H64} RP STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) IN COMPLEX WITH MTOR AND RP RPTOR, AND IDENTIFICATION IN THE MTORC1 COMPLEX. RX PubMed=27909983; DOI=10.1007/s13238-016-0346-6; RA Yang H., Wang J., Liu M., Chen X., Huang M., Tan D., Dong M.Q., Wong C.C., RA Wang J., Xu Y., Wang H.W.; RT "4.4 Aa Resolution Cryo-EM structure of human mTOR Complex 1."; RL Protein Cell 7:878-887(2016). RN [25] {ECO:0007744|PDB:5FLC} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS) IN COMPLEX WITH MTOR. RX PubMed=26678875; DOI=10.1126/science.aaa3870; RA Aylett C.H., Sauer E., Imseng S., Boehringer D., Hall M.N., Ban N., RA Maier T.; RT "Architecture of human mTOR complex 1."; RL Science 351:48-52(2016). RN [26] {ECO:0007744|PDB:5WBU, ECO:0007744|PDB:5WBY, ECO:0007744|PDB:6BCU, ECO:0007744|PDB:6BCX} RP STRUCTURE BY ELECTRON MICROSCOPY (3.43 ANGSTROMS) IN COMPLEX WITH MTOR; RP RPTOR; AKT1S1; RHEB AND EIF4EBP1, AND IDENTIFICATION IN THE MTORC1 COMPLEX. RX PubMed=29236692; DOI=10.1038/nature25023; RA Yang H., Jiang X., Li B., Yang H.J., Miller M., Yang A., Dhar A., RA Pavletich N.P.; RT "Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40."; RL Nature 552:368-373(2017). RN [27] {ECO:0007744|PDB:6SB0, ECO:0007744|PDB:6SB2} RP STRUCTURE BY ELECTRON MICROSCOPY (5.50 ANGSTROMS) IN COMPLEX WITH RRAGA; RP RRAGC; RPTOR; MTOR AND AKT1S1, IDENTIFICATION IN THE MTORC1 COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=31601764; DOI=10.1126/science.aax3939; RA Anandapadamanaban M., Masson G.R., Perisic O., Berndt A., Kaufman J., RA Johnson C.M., Santhanam B., Rogala K.B., Sabatini D.M., Williams R.L.; RT "Architecture of human Rag GTPase heterodimers and their complex with RT mTORC1."; RL Science 366:203-210(2019). RN [28] {ECO:0007744|PDB:7PE7, ECO:0007744|PDB:7PE8, ECO:0007744|PDB:7PE9, ECO:0007744|PDB:7PEA, ECO:0007744|PDB:7PEB, ECO:0007744|PDB:7PEC} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-230 IN COMPLEX WITH DEPTOR; RP MTOR; MAPKAP1; RICTOR AND RPTOR, IDENTIFICATION IN THE MTORC1 COMPLEX, AND RP IDENTIFICATION IN THE MTORC2 COMPLEX. RX PubMed=34519268; DOI=10.7554/elife.70871; RA Waelchli M., Berneiser K., Mangia F., Imseng S., Craigie L.M., RA Stuttfeld E., Hall M.N., Maier T.; RT "Regulation of human mTOR complexes by DEPTOR."; RL Elife 10:0-0(2021). RN [29] {ECO:0007744|PDB:7OWG} RP STRUCTURE BY ELECTRON MICROSCOPY (4.70 ANGSTROMS) IN COMPLEX WITH DEPTOR; RP MTOR AND RPTOR, AND IDENTIFICATION IN THE MTORC1 COMPLEX. RX PubMed=34519269; DOI=10.7554/elife.68799; RA Heimhalt M., Berndt A., Wagstaff J., Anandapadamanaban M., Perisic O., RA Maslen S., McLaughlin S., Yu C.W., Masson G.R., Boland A., Ni X., RA Yamashita K., Murshudov G.N., Skehel M., Freund S.M., Williams R.L.; RT "Bipartite binding and partial inhibition links DEPTOR and mTOR in a RT mutually antagonistic embrace."; RL Elife 10:0-0(2021). RN [30] {ECO:0007744|PDB:7UXC, ECO:0007744|PDB:7UXH} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH RRAGA; RP RRAGC; LAMTOR1; LAMTOR2; LAMTOR3; LAMTOR4; RPTOR; MTOR AND TFEB, AND RP DENTIFICATION IN THE MTORC1 COMPLEX. RX PubMed=36697823; DOI=10.1038/s41586-022-05652-7; RA Cui Z., Napolitano G., de Araujo M.E.G., Esposito A., Monfregola J., RA Huber L.A., Ballabio A., Hurley J.H.; RT "Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex."; RL Nature 614:572-579(2023). CC -!- FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell CC growth and survival in response to nutrient and hormonal signals CC (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). CC mTORC1 is activated in response to growth factors or amino acids CC (PubMed:12718876, PubMed:15268862, PubMed:15467718, PubMed:24403073). CC In response to nutrients, mTORC1 is recruited to the lysosome membrane CC and promotes protein, lipid and nucleotide synthesis by phosphorylating CC several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and CC RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12718876, PubMed:15268862, CC PubMed:15467718, PubMed:24403073). In the same time, it inhibits CC catabolic pathways by phosphorylating the autophagy initiation CC components ULK1 and ATG13, as well as transcription factor TFEB, a CC master regulators of lysosomal biogenesis and autophagy CC (PubMed:24403073). The mTORC1 complex is inhibited in response to CC starvation and amino acid depletion (PubMed:24403073). Within mTORC1, CC LST8 interacts directly with MTOR and enhances its kinase activity CC (PubMed:12718876). In nutrient-poor conditions, stabilizes the MTOR- CC RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity CC (PubMed:12718876). mTORC2 is also activated by growth factors, but CC seems to be nutrient-insensitive (PubMed:15467718). 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 (PubMed:15467718). mTORC2 promotes the serum-induced formation CC of stress-fibers or F-actin (PubMed:15467718). mTORC2 plays a critical CC role in AKT1 'Ser-473' phosphorylation, which may facilitate the CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 CC which is a prerequisite for full activation (PubMed:15467718). mTORC2 CC regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:15467718). CC mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657' CC (PubMed:15467718). {ECO:0000269|PubMed:12718876, CC ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, CC ECO:0000269|PubMed:24403073}. CC -!- SUBUNIT: Part of the mechanistic target of rapamycin complex 1 (mTORC1) CC which contains MTOR, MLST8 and RPTOR (PubMed:12718876, PubMed:12408816, CC PubMed:15268862, PubMed:17510057, PubMed:23636326, PubMed:27909983, CC PubMed:26678875, PubMed:31601764, PubMed:24403073, PubMed:29236692, CC PubMed:34519268, PubMed:34519269, PubMed:36697823). mTORC1 associates CC with AKT1S1/PRAS40, which inhibits its activity (PubMed:31601764). CC mTORC1 binds to and is inhibited by FKBP12-rapamycin (PubMed:12408816). CC Within mTORC1, interacts directly with MTOR and RPTOR CC (PubMed:12718876). Part of the mechanistic target of rapamycin complex CC 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR CC (PubMed:15268862, PubMed:15467718, PubMed:17461779, PubMed:17510057, CC PubMed:23636326, PubMed:26678875, PubMed:34519268). Contrary to mTORC1, CC mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin CC (PubMed:12408816). mTORC1 and mTORC2 associate with DEPTOR, which CC regulates its activity (PubMed:34519268, PubMed:34519269). Interacts CC with RHEB (PubMed:15854902). Interacts with MEAK7 (PubMed:29750193). CC Interacts with SIK3 (PubMed:30232230). Interacts with SLC38A7; this CC interaction promotes the recruitment of mTORC1 to the lysosome and its CC subsequent activation (PubMed:35561222). {ECO:0000269|PubMed:12408816, CC ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15268862, CC ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15854902, CC ECO:0000269|PubMed:17461779, ECO:0000269|PubMed:17510057, CC ECO:0000269|PubMed:23636326, ECO:0000269|PubMed:24403073, CC ECO:0000269|PubMed:26678875, ECO:0000269|PubMed:27909983, CC ECO:0000269|PubMed:29236692, ECO:0000269|PubMed:29750193, CC ECO:0000269|PubMed:30232230, ECO:0000269|PubMed:31601764, CC ECO:0000269|PubMed:34519268, ECO:0000269|PubMed:34519269, CC ECO:0000269|PubMed:35561222, ECO:0000269|PubMed:36697823}. CC -!- INTERACTION: CC Q9BVC4; P42345: MTOR; NbExp=5; IntAct=EBI-1387471, EBI-359260; CC Q9BVC4; Q8N122: RPTOR; NbExp=3; IntAct=EBI-1387471, EBI-1567928; CC Q9BVC4-1; P42345: MTOR; NbExp=7; IntAct=EBI-16056342, EBI-359260; CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:31601764}. CC Cytoplasm {ECO:0000250|UniProtKB:Q9Z2K5}. Note=Targeting to lysosomal CC membrane depends on amino acid availability: mTORC1 is recruited to CC lysosome membranes via interaction with GTP-bound form of RagA/RRAGA CC (or RagB/RRAGB) in complex with the GDP-bound form of RagC/RRAGC (or CC RagD/RRAGD), promoting its mTORC1 recruitment to the lysosomes. CC {ECO:0000269|PubMed:31601764}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BVC4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BVC4-3; Sequence=VSP_032665; CC Name=3; CC IsoId=Q9BVC4-4; Sequence=VSP_032666, VSP_032667, VSP_032668; CC Name=4; CC IsoId=Q9BVC4-5; Sequence=VSP_047368; CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal CC muscle, heart and kidney. {ECO:0000269|PubMed:12408816}. CC -!- PTM: Phosphorylation at Thr-51 by CDK1 promotes ubiquitination by the CC SCF(FBXW7) complex, followed by degradation. CC {ECO:0000269|PubMed:34741373}. CC -!- PTM: Ubiquitination by the SCF(FBXW7) and SCF(FBXW11) complexes CC following phosphorylation at Thr-51 by CDK1, leads to its degradation CC by the proteasome. {ECO:0000269|PubMed:34741373}. CC -!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EAW85539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY223837; AAO73410.1; -; mRNA. DR EMBL; AK021536; BAG51036.1; -; mRNA. DR EMBL; AK022227; BAB13990.1; -; mRNA. DR EMBL; AK302201; BAG63562.1; -; mRNA. DR EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85538.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85539.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471112; EAW85541.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85542.1; -; Genomic_DNA. DR EMBL; BC001313; AAH01313.1; -; mRNA. DR EMBL; BC017119; AAH17119.1; -; mRNA. DR EMBL; BC052292; AAH52292.1; -; mRNA. DR EMBL; BC088354; AAH88354.1; -; mRNA. DR EMBL; AF195883; AAF04308.1; -; mRNA. DR CCDS; CCDS10462.2; -. [Q9BVC4-1] DR CCDS; CCDS58409.1; -. [Q9BVC4-5] DR RefSeq; NP_001186102.1; NM_001199173.1. [Q9BVC4-1] DR RefSeq; NP_001186103.1; NM_001199174.1. [Q9BVC4-1] DR RefSeq; NP_001186104.1; NM_001199175.1. [Q9BVC4-5] DR RefSeq; NP_071767.3; NM_022372.4. [Q9BVC4-1] DR RefSeq; XP_016879037.1; XM_017023548.1. DR RefSeq; XP_016879038.1; XM_017023549.1. DR PDB; 4JSN; X-ray; 3.20 A; C/D=1-326. DR PDB; 4JSP; X-ray; 3.30 A; C/D=1-326. DR PDB; 4JSV; X-ray; 3.50 A; C/D=1-326. DR PDB; 4JSX; X-ray; 3.50 A; C/D=1-326. DR PDB; 4JT5; X-ray; 3.45 A; C/D=1-323. DR PDB; 4JT6; X-ray; 3.60 A; C/D=1-326. DR PDB; 5FLC; EM; 5.90 A; D/H=1-326. DR PDB; 5H64; EM; 4.40 A; C/c=1-326. DR PDB; 5WBU; X-ray; 3.42 A; C/D=1-326. DR PDB; 5WBY; X-ray; 3.10 A; C/D=1-326. DR PDB; 5ZCS; EM; 4.90 A; C/D=1-326. DR PDB; 6BCU; EM; 3.43 A; D/E=1-326. DR PDB; 6BCX; EM; 3.00 A; D/E=1-326. DR PDB; 6SB0; EM; 5.50 A; E/H=1-326. DR PDB; 6SB2; EM; 6.20 A; E/H=1-326. DR PDB; 6ZWM; EM; 3.20 A; C/D=1-326. DR PDB; 6ZWO; EM; 3.00 A; D=1-326. DR PDB; 7OWG; EM; 4.70 A; E=1-326. DR PDB; 7PE7; EM; 3.41 A; C/D=1-326. DR PDB; 7PE8; EM; 3.20 A; C=1-326. DR PDB; 7PE9; EM; 3.70 A; C=1-326. DR PDB; 7PEA; EM; 4.07 A; C/D=1-326. DR PDB; 7PEB; EM; 3.67 A; C=1-326. DR PDB; 7PEC; EM; 4.24 A; C=1-326. DR PDB; 7TZO; EM; 3.28 A; C/D=1-326. DR PDB; 7UXC; EM; 3.20 A; B=1-326. DR PDB; 7UXH; EM; 3.20 A; B/D=1-326. DR PDB; 8ERA; EM; 2.86 A; C=1-326. DR PDBsum; 4JSN; -. DR PDBsum; 4JSP; -. DR PDBsum; 4JSV; -. DR PDBsum; 4JSX; -. DR PDBsum; 4JT5; -. DR PDBsum; 4JT6; -. DR PDBsum; 5FLC; -. DR PDBsum; 5H64; -. DR PDBsum; 5WBU; -. DR PDBsum; 5WBY; -. DR PDBsum; 5ZCS; -. DR PDBsum; 6BCU; -. DR PDBsum; 6BCX; -. DR PDBsum; 6SB0; -. DR PDBsum; 6SB2; -. DR PDBsum; 6ZWM; -. DR PDBsum; 6ZWO; -. DR PDBsum; 7OWG; -. DR PDBsum; 7PE7; -. DR PDBsum; 7PE8; -. DR PDBsum; 7PE9; -. DR PDBsum; 7PEA; -. DR PDBsum; 7PEB; -. DR PDBsum; 7PEC; -. DR PDBsum; 7TZO; -. DR PDBsum; 7UXC; -. DR PDBsum; 7UXH; -. DR PDBsum; 8ERA; -. DR AlphaFoldDB; Q9BVC4; -. DR EMDB; EMD-10132; -. DR EMDB; EMD-10133; -. DR EMDB; EMD-11488; -. DR EMDB; EMD-11489; -. DR EMDB; EMD-11490; -. DR EMDB; EMD-11491; -. DR EMDB; EMD-11492; -. DR EMDB; EMD-13097; -. DR EMDB; EMD-13347; -. DR EMDB; EMD-13348; -. DR EMDB; EMD-13349; -. DR EMDB; EMD-13350; -. DR EMDB; EMD-13351; -. DR EMDB; EMD-13352; -. DR EMDB; EMD-26857; -. DR EMDB; EMD-26861; -. DR EMDB; EMD-28551; -. DR EMDB; EMD-3212; -. DR EMDB; EMD-3213; -. DR EMDB; EMD-6668; -. DR EMDB; EMD-6913; -. DR EMDB; EMD-7086; -. DR EMDB; EMD-7087; -. DR SMR; Q9BVC4; -. DR BioGRID; 122113; 143. DR ComplexPortal; CPX-4402; mTORC2 complex. DR ComplexPortal; CPX-503; mTORC1 complex. DR CORUM; Q9BVC4; -. DR DIP; DIP-39481N; -. DR IntAct; Q9BVC4; 39. DR MINT; Q9BVC4; -. DR STRING; 9606.ENSP00000457870; -. DR BindingDB; Q9BVC4; -. DR ChEMBL; CHEMBL4296661; -. DR ChEMBL; CHEMBL4523999; -. DR iPTMnet; Q9BVC4; -. DR PhosphoSitePlus; Q9BVC4; -. DR BioMuta; MLST8; -. DR DMDM; 74761285; -. DR EPD; Q9BVC4; -. DR jPOST; Q9BVC4; -. DR MassIVE; Q9BVC4; -. DR MaxQB; Q9BVC4; -. DR PaxDb; 9606-ENSP00000456405; -. DR PeptideAtlas; Q9BVC4; -. DR ProteomicsDB; 79194; -. [Q9BVC4-1] DR ProteomicsDB; 79195; -. [Q9BVC4-3] DR ProteomicsDB; 79196; -. [Q9BVC4-4] DR Pumba; Q9BVC4; -. DR Antibodypedia; 23622; 529 antibodies from 39 providers. DR DNASU; 64223; -. DR Ensembl; ENST00000382450.8; ENSP00000371888.4; ENSG00000167965.18. [Q9BVC4-5] DR Ensembl; ENST00000397124.5; ENSP00000380313.1; ENSG00000167965.18. [Q9BVC4-1] DR Ensembl; ENST00000564088.5; ENSP00000457870.1; ENSG00000167965.18. [Q9BVC4-1] DR Ensembl; ENST00000565250.1; ENSP00000455046.1; ENSG00000167965.18. [Q9BVC4-1] DR Ensembl; ENST00000569417.6; ENSP00000456405.1; ENSG00000167965.18. [Q9BVC4-1] DR GeneID; 64223; -. DR KEGG; hsa:64223; -. DR MANE-Select; ENST00000569417.6; ENSP00000456405.1; NM_022372.6; NP_071767.3. DR UCSC; uc002coz.4; human. [Q9BVC4-1] DR AGR; HGNC:24825; -. DR CTD; 64223; -. DR DisGeNET; 64223; -. DR GeneCards; MLST8; -. DR HGNC; HGNC:24825; MLST8. DR HPA; ENSG00000167965; Low tissue specificity. DR MIM; 612190; gene. DR neXtProt; NX_Q9BVC4; -. DR OpenTargets; ENSG00000167965; -. DR PharmGKB; PA165450213; -. DR VEuPathDB; HostDB:ENSG00000167965; -. DR eggNOG; KOG0315; Eukaryota. DR GeneTree; ENSGT00390000014795; -. DR InParanoid; Q9BVC4; -. DR OMA; VQRNYKH; -. DR OrthoDB; 650241at2759; -. DR PhylomeDB; Q9BVC4; -. DR TreeFam; TF318577; -. DR PathwayCommons; Q9BVC4; -. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. 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-3371571; HSF1-dependent transactivation. DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer. DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR SignaLink; Q9BVC4; -. DR SIGNOR; Q9BVC4; -. DR BioGRID-ORCS; 64223; 513 hits in 1171 CRISPR screens. DR ChiTaRS; MLST8; human. DR GeneWiki; MLST8; -. DR GenomeRNAi; 64223; -. DR Pharos; Q9BVC4; Tbio. DR PRO; PR:Q9BVC4; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9BVC4; Protein. DR Bgee; ENSG00000167965; Expressed in right hemisphere of cerebellum and 183 other cell types or tissues. DR ExpressionAtlas; Q9BVC4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB. DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:WormBase. DR GO; GO:0071456; P:cellular response to hypoxia; NAS:ComplexPortal. DR GO; GO:0031669; P:cellular response to nutrient levels; NAS:ComplexPortal. DR GO; GO:0071470; P:cellular response to osmotic stress; NAS:ComplexPortal. DR GO; GO:0007010; P:cytoskeleton organization; NAS:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; NAS:ComplexPortal. DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0010507; P:negative regulation of autophagy; NAS:ComplexPortal. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0030307; P:positive regulation of cell growth; NAS:ComplexPortal. DR GO; GO:0045821; P:positive regulation of glycolytic process; NAS:ComplexPortal. DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; NAS:ComplexPortal. DR GO; GO:1905857; P:positive regulation of pentose-phosphate shunt; NAS:ComplexPortal. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central. DR GO; GO:0038202; P:TORC1 signaling; IMP:WormBase. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR IDEAL; IID00599; -. 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; IPR019775; WD40_repeat_CS. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19842; G BETA-LIKE PROTEIN GBL; 1. DR PANTHER; PTHR19842:SF0; TARGET OF RAPAMYCIN COMPLEX SUBUNIT LST8; 1. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q9BVC4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Lysosome; KW Membrane; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; KW WD repeat. FT CHAIN 1..326 FT /note="Target of rapamycin complex subunit LST8" FT /id="PRO_0000326499" FT REPEAT 1..37 FT /note="WD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 40..80 FT /note="WD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 83..122 FT /note="WD 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 126..165 FT /note="WD 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 168..207 FT /note="WD 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 218..257 FT /note="WD 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT REPEAT 268..309 FT /note="WD 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221, FT ECO:0000269|PubMed:23636326" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231" FT MOD_RES 51 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:34741373" FT VAR_SEQ 1..66 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_032665" FT VAR_SEQ 1 FT /note="M -> MEHAPWSPGASSRARAGHTM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032666" FT VAR_SEQ 44 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047368" FT VAR_SEQ 192..198 FT /note="GNCYVWN -> APRHLLG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032667" FT VAR_SEQ 199..326 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032668" FT MUTAGEN 51 FT /note="T->A: Reduced ubiquitination by the SCF(FBXW7) FT complex." FT /evidence="ECO:0000269|PubMed:34741373" FT MUTAGEN 55 FT /note="S->A: Does not affect ubiquitination by the FT SCF(FBXW7) complex." FT /evidence="ECO:0000269|PubMed:34741373" FT MUTAGEN 72 FT /note="S->D: Impairs interaction with MTOR." FT /evidence="ECO:0000269|PubMed:12718876" FT MUTAGEN 192 FT /note="G->D: Abolishes interaction with MTOR." FT /evidence="ECO:0000269|PubMed:12718876" FT MUTAGEN 320 FT /note="F->S: Impairs interaction with MTOR." FT /evidence="ECO:0000269|PubMed:12718876" FT CONFLICT 56 FT /note="M -> V (in Ref. 2; BAB13990)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="H -> Y (in Ref. 5; AAH88354)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="R -> G (in Ref. 1; AAO73410)" FT /evidence="ECO:0000305" FT STRAND 10..27 FT /evidence="ECO:0007829|PDB:8ERA" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 62..68 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 78..88 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 97..115 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 122..126 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:7UXC" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:8ERA" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:6ZWM" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:8ERA" FT TURN 203..206 FT /evidence="ECO:0007829|PDB:6ZWO" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 240..248 FT /evidence="ECO:0007829|PDB:8ERA" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 254..259 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:5WBY" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:6ZWO" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:6ZWO" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:8ERA" FT TURN 299..301 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:8ERA" FT STRAND 315..322 FT /evidence="ECO:0007829|PDB:8ERA" FT MOD_RES Q9BVC4-4:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES Q9BVC4-4:7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" SQ SEQUENCE 326 AA; 35876 MW; 43A600D4EF2B6543 CRC64; MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG AIHIWDLKTD HNEQLIPEPE VSITSAHIDP DASYMAAVNS TGNCYVWNLT GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE TGEIKREYGG HQKAVVCLAF NDSVLG //