ID DPTOR_HUMAN Reviewed; 409 AA. AC Q8TB45; B2RCL9; B4DN97; E7EV87; Q96EQ1; Q9H0R7; Q9H894; Q9HA07; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 07-JUL-2009, sequence version 2. DT 24-JAN-2024, entry version 162. DE RecName: Full=DEP domain-containing mTOR-interacting protein {ECO:0000305}; DE Short=hDEPTOR {ECO:0000303|PubMed:33865870}; DE AltName: Full=DEP domain-containing protein 6 {ECO:0000303|PubMed:29382726}; GN Name=DEPTOR {ECO:0000303|PubMed:19446321, GN ECO:0000312|HGNC:HGNC:22953}; GN Synonyms=DEPDC6 {ECO:0000303|PubMed:29382726}; 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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-204. RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP SER-204 AND ASN-389. RC TISSUE=Heart, Mammary gland, and Thyroid; 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=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). 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), AND VARIANTS SER-204 RP AND ASN-389. RC TISSUE=Cervix, and 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 [6] 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 [7] RP FUNCTION, INTERACTION WITH MTOR, INDUCTION, PHOSPHORYLATION AT THR-241; RP SER-244; SER-258; THR-259; SER-263; SER-265; SER-282; SER-283; SER-287; RP SER-293; SER-297; SER-298 AND SER-299, MUTAGENESIS OF THR-241; SER-244; RP SER-258; THR-259; SER-263; SER-265; SER-282; SER-283; SER-287; SER-293; RP SER-297; SER-298 AND SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19446321; DOI=10.1016/j.cell.2009.03.046; RA Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M., RA Gray N.S., Sabatini D.M.; RT "DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma RT cells and required for their survival."; RL Cell 137:873-886(2009). RN [8] 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 [9] RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-265; SER-286; RP SER-287; SER-293; THR-295 AND SER-299, UBIQUITINATION, AND MUTAGENESIS OF RP SER-286; SER-293 AND 295-THR--SER-299. RX PubMed=22017875; DOI=10.1016/j.molcel.2011.08.030; RA Gao D., Inuzuka H., Tan M.K., Fukushima H., Locasale J.W., Liu P., Wan L., RA Zhai B., Chin Y.R., Shaik S., Lyssiotis C.A., Gygi S.P., Toker A., RA Cantley L.C., Asara J.M., Harper J.W., Wei W.; RT "mTOR drives its own activation via SCF(betaTrCP)-dependent degradation of RT the mTOR inhibitor DEPTOR."; RL Mol. Cell 44:290-303(2011). RN [10] RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-286; SER-287 AND RP SER-291, UBIQUITINATION, AND MUTAGENESIS OF SER-286; SER-287 AND SER-291. RX PubMed=22017876; DOI=10.1016/j.molcel.2011.08.029; RA Zhao Y., Xiong X., Sun Y.; RT "DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(betaTrCP) RT E3 ubiquitin ligase and regulates survival and autophagy."; RL Mol. Cell 44:304-316(2011). RN [11] RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-286; SER-287 AND RP SER-291, UBIQUITINATION, AND MUTAGENESIS OF 286-SER--SER-291; SER-286; RP SER-287 AND SER-291. RX PubMed=22017877; DOI=10.1016/j.molcel.2011.09.005; RA Duan S., Skaar J.R., Kuchay S., Toschi A., Kanarek N., Ben-Neriah Y., RA Pagano M.; RT "mTOR generates an auto-amplification loop by triggering the betaTrCP- and RT CK1alpha-dependent degradation of DEPTOR."; RL Mol. Cell 44:317-324(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [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 FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN THE MTORC1 COMPLEX, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-241; SER-244; SER-258; RP THR-259; SER-263; SER-265; SER-282; SER-283; SER-287; SER-293; SER-297; RP SER-298 AND SER-299. RX PubMed=25936805; DOI=10.1016/j.molcel.2015.03.028; RA Yoon M.S., Rosenberger C.L., Wu C., Truong N., Sweedler J.V., Chen J.; RT "Rapid mitogenic regulation of the mTORC1 inhibitor, DEPTOR, by RT phosphatidic acid."; RL Mol. Cell 58:549-556(2015). RN [16] RP FUNCTION, AND DEUBIQUITINATION. RX PubMed=29382726; DOI=10.1074/jbc.m117.809533; RA Zhao L., Wang X., Yu Y., Deng L., Chen L., Peng X., Jiao C., Gao G., RA Tan X., Pan W., Ge X., Wang P.; RT "OTUB1 protein suppresses mTOR complex 1 (mTORC1) activity by RT deubiquitinating the mTORC1 inhibitor DEPTOR."; RL J. Biol. Chem. 293:4883-4892(2018). RN [17] RP INTERACTION WITH MINAR1, AND UBIQUITINATION. RX PubMed=30080879; DOI=10.1371/journal.pgen.1007583; RA Zhang H., Zhang Q., Gao G., Wang X., Wang T., Kong Z., Wang G., Zhang C., RA Wang Y., Peng G.; RT "UBTOR/KIAA1024 regulates neurite outgrowth and neoplasia through mTOR RT signaling."; RL PLoS Genet. 14:E1007583-E1007583(2018). RN [18] 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 [19] RP UBIQUITINATION. RX PubMed=33110214; DOI=10.1038/s41418-020-00649-z; RA Cho J.H., Kim K., Kim S.A., Park S., Park B.O., Kim J.H., Kim S.Y., RA Kwon M.J., Han M.H., Lee S.B., Park B.C., Park S.G., Kim J.H., Kim S.; RT "Deubiquitinase OTUD5 is a positive regulator of mTORC1 and mTORC2 RT signaling pathways."; RL Cell Death Differ. 28:900-914(2021). RN [20] RP PHOSPHORYLATION AT TYR-289, AND MUTAGENESIS OF TYR-289 AND TYR-326. RX PubMed=34634301; DOI=10.1016/j.jbc.2021.101291; RA M Gagne L., Morin N., Lavoie N., Bisson N., Lambert J.P., Mallette F.A., RA Huot M.E.; RT "Tyrosine phosphorylation of DEPTOR functions as a molecular switch to RT activate mTOR signaling."; RL J. Biol. Chem. 297:101291-101291(2021). RN [21] RP PHOSPHORYLATION AT SER-235, DEUBIQUITINATION, AND MUTAGENESIS OF SER-235. RX PubMed=35216969; DOI=10.1016/j.jbc.2022.101750; RA Vega M., Chen Y., Shi Y., Gera J., Lichtenstein A.; RT "Turnover of the mTOR inhibitor, DEPTOR, and downstream AKT phosphorylation RT in multiple myeloma cells, is dependent on ERK1-mediated phosphorylation."; RL J. Biol. Chem. 298:101750-101750(2022). RN [22] {ECO:0007744|PDB:7DKL} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 21-235, ACTIVITY REGULATION, AND RP MUTAGENESIS OF ARG-53; ARG-54; LYS-58; ARG-225 AND LEU-231. RX PubMed=33865870; DOI=10.1016/j.jmb.2021.166989; RA Weng Z., Shen X., Zheng J., Liang H., Liu Y.; RT "Structural basis of DEPTOR to recognize phosphatidic acid using its tandem RT DEP domains."; RL J. Mol. Biol. 433:166989-166989(2021). RN [23] {ECO:0007744|PDB:7PE7, ECO:0007744|PDB:7PE8, ECO:0007744|PDB:7PE9, ECO:0007744|PDB:7PEA, ECO:0007744|PDB:7PEB, ECO:0007744|PDB:7PEC, ECO:0007744|PDB:7PED} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-230 IN COMPLEX WITH DEPTOR; RP MLST8; MAPKAP1; RICTOR AND RPTOR, FUNCTION, IDENTIFICATION IN THE MTORC1 RP COMPLEX, AND 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 [24] {ECO:0007744|PDB:7OWG} RP STRUCTURE BY ELECTRON MICROSCOPY (4.70 ANGSTROMS) IN COMPLEX WITH MTOR; RP MLST8 AND RPTOR, FUNCTION, 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). CC -!- FUNCTION: Negative regulator of the mTORC1 and mTORC2 complexes: CC inhibits the protein kinase activity of MTOR, thereby inactivating both CC complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876, CC PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519269, CC PubMed:34519268). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy CC (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to CC AKT1S1/PRAS40, only partially inhibits mTORC1 activity CC (PubMed:34519269, PubMed:34519268). {ECO:0000269|PubMed:19446321, CC ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805, CC ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:34519268, CC ECO:0000269|PubMed:34519269}. CC -!- ACTIVITY REGULATION: Inhibited upon phosphatidic acid-binding: CC phosphatidic acid produced upon mitogenic stimulation promotes DEPTOR CC dissociatiom from the mTORC1 and mTORC2 complexes, leading to their CC activation (PubMed:25936805, PubMed:33865870). Specifically binds CC unsaturated phosphatidic acid, such as 16:0-18:1, 18:0-18:1 and di-18:1 CC (PubMed:25936805). Inhibited when nutrients are present via a feedback CC loop: phosphorylation by MTOR promotes DEPTOR ubiquitination and CC degradation (PubMed:22017875, PubMed:22017876, PubMed:22017877). CC {ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805, CC ECO:0000269|PubMed:33865870}. CC -!- SUBUNIT: Associated component of the mechanistic target of rapamycin CC complex 1 (mTORC1) which contains MTOR, MLST8 and RPTOR CC (PubMed:19446321, PubMed:25936805, PubMed:34519269, PubMed:34519268). CC Associated component of the mechanistic target of rapamycin complex 2 CC (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and CC DEPTOR (PubMed:19446321, PubMed:34519268). Interacts (via PDZ domain) CC with MTOR; interacts with MTOR within both mTORC1 and mTORC2 CC (PubMed:19446321). Interacts (via PDZ domain) with MINAR1 (via N- CC terminus) (PubMed:30080879). Interacts with SIK3 (PubMed:30232230). CC {ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:25936805, CC ECO:0000269|PubMed:30080879, ECO:0000269|PubMed:30232230, CC ECO:0000269|PubMed:34519268, ECO:0000269|PubMed:34519269}. CC -!- INTERACTION: CC Q8TB45; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2359040, EBI-17183751; CC Q8TB45; Q8TBZ0: CCDC110; NbExp=3; IntAct=EBI-2359040, EBI-2837012; CC Q8TB45; P42345: MTOR; NbExp=5; IntAct=EBI-2359040, EBI-359260; CC Q8TB45; Q13077: TRAF1; NbExp=3; IntAct=EBI-2359040, EBI-359224; CC Q8TB45; P42346: Mtor; Xeno; NbExp=2; IntAct=EBI-2359040, EBI-1571489; CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000305|PubMed:25936805}. CC Note=Localizes to the lysosomal membrane when associated with the CC mTORC1 and mTORC2 complexes. {ECO:0000305|PubMed:25936805}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TB45-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TB45-2; Sequence=VSP_054681; CC -!- INDUCTION: Expression is negatively regulated by both mTORC1 and mTORC2 CC (at protein level). {ECO:0000269|PubMed:19446321}. CC -!- PTM: Phosphorylation weakens interaction with MTOR within mTORC1 and CC mTORC2 (PubMed:19446321). Phosphorylated at Ser-286, Ser-287 and Ser- CC 291 in response to mitogenic stimulation by MTOR: DEPTOR is either CC directly phosphorylated by MTOR or indirectly via proteins kinases that CC are activated by MTOR, such as CK1/CSNK1A1 (PubMed:22017875, CC PubMed:22017876, PubMed:22017877). Phosphorylation at Ser-286, Ser-287 CC and Ser-291 promotes ubiquitination by the SCF(BTRC) complex, followed CC by degradation (PubMed:22017875, PubMed:22017876, PubMed:22017877). CC Phosphorylation at Ser-235 by MAPK3/ERK1 promotes deubiquitination by CC USP7, enhancing its stability (PubMed:35216969). Phosphorylation at CC Tyr-289 by SYK impairs its interaction with MTOR, promoting mTORC1 and CC mTORC2 signaling (PubMed:34634301). {ECO:0000269|PubMed:19446321, CC ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:34634301, CC ECO:0000269|PubMed:35216969}. CC -!- PTM: Ubiquitinated; leading to proteasomal degradation CC (PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:30080879, CC PubMed:33110214). Ubiquitination by the SCF(BTRC) and SCF(FBXW11) CC complexes following phosphorylation at Ser-286, Ser-287 and Ser-291 by CC MTOR, leads to its degradation by the proteasome (PubMed:22017875, CC PubMed:22017876, PubMed:22017877, PubMed:33110214). Deubiquitinated by CC OTUB1 in response to amino acid via a non-canonical mechanism, leading CC to DEPTOR stability (PubMed:29382726). Deubiquitinated by USP7 CC following phosphorylation at Ser-235, promoting its stability CC (PubMed:35216969). {ECO:0000269|PubMed:22017875, CC ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877, CC ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:30080879, CC ECO:0000269|PubMed:33110214, ECO:0000269|PubMed:35216969}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AL136678; CAB66613.1; -; mRNA. DR EMBL; AK022490; BAB14054.1; -; mRNA. DR EMBL; AK023916; BAB14723.1; ALT_INIT; mRNA. DR EMBL; AK297822; BAG60159.1; -; mRNA. DR EMBL; AK315175; BAG37616.1; -; mRNA. DR EMBL; AC091563; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471060; EAW91997.1; -; Genomic_DNA. DR EMBL; BC012040; AAH12040.1; -; mRNA. DR EMBL; BC024746; AAH24746.1; -; mRNA. DR CCDS; CCDS6331.1; -. [Q8TB45-1] DR CCDS; CCDS64960.1; -. [Q8TB45-2] DR RefSeq; NP_001269941.1; NM_001283012.1. [Q8TB45-2] DR RefSeq; NP_073620.2; NM_022783.3. [Q8TB45-1] DR PDB; 7DKL; X-ray; 1.50 A; A=21-235. DR PDB; 7OWG; EM; 4.70 A; O=1-409. DR PDB; 7PE7; EM; 3.41 A; I/J=1-409. DR PDB; 7PE8; EM; 3.20 A; I=1-409. DR PDB; 7PE9; EM; 3.70 A; I=1-409. DR PDB; 7PEA; EM; 4.07 A; I/J=1-409. DR PDB; 7PEB; EM; 3.67 A; I=1-409. DR PDB; 7PEC; EM; 4.24 A; I=1-409. DR PDB; 7PED; X-ray; 1.93 A; A/B=1-230. DR PDBsum; 7DKL; -. DR PDBsum; 7OWG; -. DR PDBsum; 7PE7; -. DR PDBsum; 7PE8; -. DR PDBsum; 7PE9; -. DR PDBsum; 7PEA; -. DR PDBsum; 7PEB; -. DR PDBsum; 7PEC; -. DR PDBsum; 7PED; -. DR AlphaFoldDB; Q8TB45; -. 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 SMR; Q8TB45; -. DR BioGRID; 122304; 82. DR IntAct; Q8TB45; 11. DR MINT; Q8TB45; -. DR STRING; 9606.ENSP00000286234; -. DR BindingDB; Q8TB45; -. DR ChEMBL; CHEMBL4105866; -. DR GlyGen; Q8TB45; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TB45; -. DR PhosphoSitePlus; Q8TB45; -. DR BioMuta; DEPTOR; -. DR DMDM; 251757257; -. DR EPD; Q8TB45; -. DR jPOST; Q8TB45; -. DR MassIVE; Q8TB45; -. DR MaxQB; Q8TB45; -. DR PaxDb; 9606-ENSP00000286234; -. DR PeptideAtlas; Q8TB45; -. DR ProteomicsDB; 18583; -. DR ProteomicsDB; 73961; -. [Q8TB45-1] DR Pumba; Q8TB45; -. DR Antibodypedia; 13704; 331 antibodies from 32 providers. DR DNASU; 64798; -. DR Ensembl; ENST00000286234.6; ENSP00000286234.5; ENSG00000155792.10. [Q8TB45-1] DR Ensembl; ENST00000523492.5; ENSP00000430457.1; ENSG00000155792.10. [Q8TB45-2] DR GeneID; 64798; -. DR KEGG; hsa:64798; -. DR MANE-Select; ENST00000286234.6; ENSP00000286234.5; NM_022783.4; NP_073620.2. DR UCSC; uc003yow.6; human. [Q8TB45-1] DR AGR; HGNC:22953; -. DR CTD; 64798; -. DR DisGeNET; 64798; -. DR GeneCards; DEPTOR; -. DR HGNC; HGNC:22953; DEPTOR. DR HPA; ENSG00000155792; Tissue enhanced (skeletal muscle, tongue). DR MIM; 612974; gene. DR neXtProt; NX_Q8TB45; -. DR OpenTargets; ENSG00000155792; -. DR PharmGKB; PA134897957; -. DR VEuPathDB; HostDB:ENSG00000155792; -. DR eggNOG; ENOG502QS4Y; Eukaryota. DR GeneTree; ENSGT00520000055667; -. DR HOGENOM; CLU_042535_0_0_1; -. DR InParanoid; Q8TB45; -. DR OMA; HVCDDHL; -. DR OrthoDB; 2953750at2759; -. DR PhylomeDB; Q8TB45; -. DR PathwayCommons; Q8TB45; -. DR SignaLink; Q8TB45; -. DR SIGNOR; Q8TB45; -. DR BioGRID-ORCS; 64798; 10 hits in 1146 CRISPR screens. DR ChiTaRS; DEPTOR; human. DR GeneWiki; DEPTOR; -. DR GenomeRNAi; 64798; -. DR Pharos; Q8TB45; Tchem. DR PRO; PR:Q8TB45; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8TB45; Protein. DR Bgee; ENSG00000155792; Expressed in parotid gland and 203 other cell types or tissues. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB. DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB. DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:UniProt. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0045792; P:negative regulation of cell size; IMP:UniProtKB. DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB. DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:1903940; P:negative regulation of TORC2 signaling; IDA:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB. DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR CDD; cd04442; DEP_1_DEP6; 1. DR CDD; cd04441; DEP_2_DEP6; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR000591; DEP_dom. DR InterPro; IPR037335; DEPTOR_DEP_1. DR InterPro; IPR037336; DEPTOR_DEP_2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR22829; DEP DOMAIN PROTEIN; 1. DR PANTHER; PTHR22829:SF18; DEP DOMAIN-CONTAINING MTOR-INTERACTING PROTEIN; 1. DR Pfam; PF00610; DEP; 2. DR SMART; SM00049; DEP; 2. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. DR PROSITE; PS50186; DEP; 2. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q8TB45; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Lipid-binding; Lysosome; KW Membrane; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..409 FT /note="DEP domain-containing mTOR-interacting protein" FT /id="PRO_0000284784" FT DOMAIN 36..119 FT /note="DEP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT DOMAIN 145..219 FT /note="DEP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT DOMAIN 330..407 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 217..235 FT /note="DDEX motif" FT /evidence="ECO:0000269|PubMed:33865870" FT MOTIF 286..291 FT /note="BetaTrCP degron motif" FT /evidence="ECO:0000269|PubMed:22017877" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 235 FT /note="Phosphoserine; by MAPK3" FT /evidence="ECO:0000269|PubMed:35216969" FT MOD_RES 241 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0007744|PubMed:23186163" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 259 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017875" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q570Y9" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 286 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000269|PubMed:22017875, FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877" FT MOD_RES 287 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876, FT ECO:0000269|PubMed:22017877" FT MOD_RES 289 FT /note="Phosphotyrosine; by SYK" FT /evidence="ECO:0000269|PubMed:34634301" FT MOD_RES 291 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000269|PubMed:22017876, FT ECO:0000269|PubMed:22017877" FT MOD_RES 293 FT /note="Phosphoserine; by MTOR" FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017875" FT MOD_RES 295 FT /note="Phosphothreonine; by MTOR" FT /evidence="ECO:0000269|PubMed:22017875" FT MOD_RES 297 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19446321" FT MOD_RES 299 FT /note="Phosphoserine; by MTOR" FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017875" FT VAR_SEQ 42..142 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054681" FT VARIANT 148 FT /note="N -> S (in dbSNP:rs34057546)" FT /id="VAR_031816" FT VARIANT 204 FT /note="N -> S (in dbSNP:rs2271900)" FT /evidence="ECO:0000269|PubMed:11230166, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_031817" FT VARIANT 389 FT /note="S -> N (in dbSNP:rs4871827)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_031818" FT MUTAGEN 53 FT /note="R->A: Decreased phosphatidic acid-binding." FT /evidence="ECO:0000269|PubMed:33865870" FT MUTAGEN 54 FT /note="R->A: Decreased phosphatidic acid-binding." FT /evidence="ECO:0000269|PubMed:33865870" FT MUTAGEN 58 FT /note="K->A: Decreased phosphatidic acid-binding." FT /evidence="ECO:0000269|PubMed:33865870" FT MUTAGEN 225 FT /note="R->A: Decreased phosphatidic acid-binding." FT /evidence="ECO:0000269|PubMed:33865870" FT MUTAGEN 231 FT /note="L->D: Decreased phosphatidic acid-binding." FT /evidence="ECO:0000269|PubMed:33865870" FT MUTAGEN 235 FT /note="S->A: Decreased phosphorylation, leading to impaired FT deubiquitination by USP7." FT /evidence="ECO:0000269|PubMed:35216969" FT MUTAGEN 235 FT /note="S->D: Mimics phosphorylation, leading to slightly FT increased stability." FT /evidence="ECO:0000269|PubMed:35216969" FT MUTAGEN 241 FT /note="T->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 244 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-258, A-259, A-263, A-265, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 258 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-259, A-263, A-265, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 259 FT /note="T->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-263, A-265, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 263 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-265, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 265 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-282, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 282 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-283, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 283 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-287, FT A-293, A-297, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 286..291 FT /note="SSGYFS->DDGYFD: Mimics phosphorylation; promoting FT association with the SCF(BTRC) complex." FT /evidence="ECO:0000269|PubMed:22017877" FT MUTAGEN 286 FT /note="S->A: Reduced ubiquitination by the SCF(BTRC) FT complex." FT /evidence="ECO:0000269|PubMed:22017875, FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877" FT MUTAGEN 287 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, FT A-293, A-297, A-298 and A-299. Reduced ubiquitination by FT the SCF(BTRC) complex." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 289 FT /note="Y->E: Mimics phosphorylation, leading to slightly FT decreased interaction with MTOR." FT /evidence="ECO:0000269|PubMed:34634301" FT MUTAGEN 289 FT /note="Y->F: Decreased phosphorylation, leading to FT increased interaction with MTOR." FT /evidence="ECO:0000269|PubMed:34634301" FT MUTAGEN 291 FT /note="S->A: Reduced ubiquitination by the SCF(BTRC) FT complex." FT /evidence="ECO:0000269|PubMed:22017876, FT ECO:0000269|PubMed:22017877" FT MUTAGEN 293 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, FT A-287, A-297, A-298 and A-299. Reduced ubiquitination by FT the SCF(BTRC) complex." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:25936805" FT MUTAGEN 295..299 FT /note="TLSSS->ALSSA: Reduced ubiquitination by the FT SCF(BTRC) complex." FT /evidence="ECO:0000269|PubMed:22017875" FT MUTAGEN 297 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, FT A-287, A-293, A-298 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 298 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, FT A-287, A-293, A-297 and A-299." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 299 FT /note="S->A: In mutant 13A; abolished phosphorylation, FT leading to promote interaction with MTOR without affecting FT ability to bind phosphatidic acid; when associated with FT A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, FT A-287, A-293, A-297 and A-298." FT /evidence="ECO:0000269|PubMed:19446321, FT ECO:0000269|PubMed:25936805" FT MUTAGEN 326 FT /note="Y->F: Does not affect phosphorylation." FT /evidence="ECO:0000269|PubMed:34634301" FT CONFLICT 166 FT /note="M -> V (in Ref. 2; BAB14054)" FT /evidence="ECO:0000305" FT CONFLICT 249 FT /note="R -> G (in Ref. 1; CAB66613)" FT /evidence="ECO:0000305" FT HELIX 22..46 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 66..75 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:7PED" FT HELIX 82..94 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 118..121 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 128..143 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 167..176 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 183..195 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 198..204 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7DKL" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:7DKL" FT HELIX 316..320 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:7PE7" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 351..355 FT /evidence="ECO:0007829|PDB:7PE8" FT HELIX 360..363 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 371..375 FT /evidence="ECO:0007829|PDB:7PE7" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:7PE8" FT HELIX 385..394 FT /evidence="ECO:0007829|PDB:7PE8" FT STRAND 397..403 FT /evidence="ECO:0007829|PDB:7PE8" SQ SEQUENCE 409 AA; 46294 MW; AD132F0E9AFFB90C CRC64; MEEGGSTGSA GSDSSTSGSG GAQQRELERM AEVLVTGEQL RLRLHEEKVI KDRRHHLKTY PNCFVAKELI DWLIEHKEAS DRETAIKLMQ KLADRGIIHH VCDEHKEFKD VKLFYRFRKD DGTFPLDNEV KAFMRGQRLY EKLMSPENTL LQPREEEGVK YERTFMASEF LDWLVQEGEA TTRKEAEQLC HRLMEHGIIQ HVSNKHPFVD SNLLYQFRMN FRRRRRLMEL LNEKSPSSQE THDSPFCLRK QSHDNRKSTS FMSVSPSKEI KIVSAVRRSS MSSCGSSGYF SSSPTLSSSP PVLCNPKSVL KRPVTSEELL TPGAPYARKT FTIVGDAVGW GFVVRGSKPC HIQAVDPSGP AAAAGMKVCQ FVVSVNGLNV LHVDYRTVSN LILTGPRTIV MEVMEELEC //