ID DNM1L_HUMAN Reviewed; 736 AA. AC O00429; A8K4X9; B4DGC9; B4DSU8; G8JLD5; J3KPI2; O14541; O60709; Q59GN9; AC Q7L6B3; Q8TBT7; Q9BWM1; Q9Y5J2; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 29-MAY-2024, entry version 206. DE RecName: Full=Dynamin-1-like protein; DE EC=3.6.5.5 {ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767}; DE AltName: Full=Dnm1p/Vps1p-like protein; DE Short=DVLP; DE AltName: Full=Dynamin family member proline-rich carboxyl-terminal domain less; DE Short=Dymple; DE AltName: Full=Dynamin-like protein; DE AltName: Full=Dynamin-like protein 4; DE AltName: Full=Dynamin-like protein IV; DE Short=HdynIV; DE AltName: Full=Dynamin-related protein 1; GN Name=DNM1L {ECO:0000312|HGNC:HGNC:2973}; Synonyms=DLP1, DRP1; 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 1), AND SUBCELLULAR LOCATION. RC TISSUE=Hepatoma; RX PubMed=9348079; DOI=10.1093/oxfordjournals.jbchem.a021784; RA Shin H.-W., Shinotsuka C., Torii S., Murakami K., Nakayama K.; RT "Identification and subcellular localization of a novel mammalian dynamin- RT related protein homologous to yeast Vps1p and Dnm1p."; RL J. Biochem. 122:525-530(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT THR-71, TISSUE SPECIFICITY, RP INTERACTION WITH GSK3B, AND REGION. RC TISSUE=Liver; RX PubMed=9731200; DOI=10.1006/bbrc.1998.9253; RA Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C.; RT "Human dynamin-like protein interacts with the glycogen synthase kinase RT 3beta."; RL Biochem. Biophys. Res. Commun. 249:697-703(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-71, TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38, AND FUNCTION. RC TISSUE=Brain; RX PubMed=9570752; DOI=10.1242/jcs.111.10.1341; RA Imoto M., Tachibana I., Urrutia R.; RT "Identification and functional characterization of a novel human protein RT highly related to the yeast dynamin-like GTPase Vps1p."; RL J. Cell Sci. 111:1341-1349(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANT THR-71, TISSUE RP SPECIFICITY, AND INTERACTION WITH GSK3B. RC TISSUE=Brain; RX PubMed=10749171; DOI=10.1089/104454900314573; RA Chen C.-H., Howng S.-L., Hwang S.-L., Chou C.-K., Liao C.-H., Hong Y.-R.; RT "Differential expression of four human dynamin-like protein variants in RT brain tumors."; RL DNA Cell Biol. 19:189-194(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6 AND 7). RC TISSUE=Amygdala, and Brain; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 27-736 (ISOFORM 1). RC TISSUE=Lung; 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 [9] RP MUTAGENESIS OF SER-39, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=9422767; DOI=10.1074/jbc.273.2.1044; RA Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.; RT "Dymple, a novel dynamin-like high molecular weight GTPase lacking a RT proline-rich carboxyl-terminal domain in mammalian cells."; RL J. Biol. Chem. 273:1044-1051(1998). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=9472031; DOI=10.1083/jcb.140.4.779; RA Yoon Y., Pitts K.R., Dahan S., McNiven M.A.; RT "A novel dynamin-like protein associates with cytoplasmic vesicles and RT tubules of the endoplasmic reticulum in mammalian cells."; RL J. Cell Biol. 140:779-793(1998). RN [11] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9786947; DOI=10.1083/jcb.143.2.351; RA Smirnova E., Shurland D.-L., Ryazantsev S.N., van der Bliek A.M.; RT "A human dynamin-related protein controls the distribution of RT mitochondria."; RL J. Cell Biol. 143:351-358(1998). RN [12] RP OLIGOMERIZATION. RX PubMed=9915810; DOI=10.1074/jbc.274.5.2780; RA Shin H.-W., Takatsu H., Mukai H., Munekata E., Murakami K., Nakayama K.; RT "Intermolecular and interdomain interactions of a dynamin-related GTP- RT binding protein, Dnm1p/Vps1p-like protein."; RL J. Biol. Chem. 274:2780-2785(1999). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38; VAL-41; THR-59 AND RP GLY-281, AND OLIGOMERIZATION. RX PubMed=11514614; DOI=10.1091/mbc.12.8.2245; RA Smirnova E., Griparic L., Shurland D.-L., van der Bliek A.M.; RT "Dynamin-related protein Drp1 is required for mitochondrial division in RT mammalian cells."; RL Mol. Biol. Cell 12:2245-2256(2001). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-38. RX PubMed=12499366; DOI=10.1074/jbc.m211761200; RA Koch A., Thiemann M., Grabenbauer M., Yoon Y., McNiven M.A., Schrader M.; RT "Dynamin-like protein 1 is involved in peroxisomal fission."; RL J. Biol. Chem. 278:8597-8605(2003). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-39 AND THR-59. RX PubMed=12618434; DOI=10.1074/jbc.m212031200; RA Li X., Gould S.J.; RT "The dynamin-like GTPase DLP1 is essential for peroxisome division and is RT recruited to peroxisomes in part by PEX11."; RL J. Biol. Chem. 278:17012-17020(2003). RN [16] RP OLIGOMERIZATION, SUBCELLULAR LOCATION, DOMAIN, REGION, AND MUTAGENESIS OF RP LYS-38 AND LYS-679. RX PubMed=15208300; DOI=10.1074/jbc.m404105200; RA Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M., Blackstone C.; RT "Intra- and intermolecular domain interactions of the C-terminal GTPase RT effector domain of the multimeric dynamin-like GTPase Drp1."; RL J. Biol. Chem. 279:35967-35974(2004). RN [17] RP UBIQUITINATION BY MARCHF5, AND INTERACTION WITH MARCHF5. RX PubMed=16874301; DOI=10.1038/sj.emboj.7601249; RA Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., RA Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.; RT "A novel mitochondrial ubiquitin ligase plays a critical role in RT mitochondrial dynamics."; RL EMBO J. 25:3618-3626(2006). RN [18] RP UBIQUITINATION BY MARCHF5, AND INTERACTION WITH MARCHF5. RX PubMed=16936636; DOI=10.1038/sj.embor.7400790; RA Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.; RT "MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change RT mitochondrial morphology."; RL EMBO Rep. 7:1019-1022(2006). RN [19] RP FUNCTION. RX PubMed=17015472; DOI=10.1128/mcb.02282-05; RA Parone P.A., James D.I., Da Cruz S., Mattenberger Y., Donze O., Barja F., RA Martinou J.C.; RT "Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak- RT dependent apoptosis."; RL Mol. Cell. Biol. 26:7397-7408(2006). RN [20] RP PHOSPHORYLATION, AND FUNCTION. RX PubMed=17301055; DOI=10.1074/jbc.m607279200; RA Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.; RT "Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in RT mitochondrial fission."; RL J. Biol. Chem. 282:11521-11529(2007). RN [21] RP PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, AND MUTAGENESIS OF SER-637. RX PubMed=17553808; DOI=10.1074/jbc.c700083200; RA Chang C.R., Blackstone C.; RT "Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its RT GTPase activity and mitochondrial morphology."; RL J. Biol. Chem. 282:21583-21587(2007). RN [22] RP SUBCELLULAR LOCATION. RX PubMed=17606867; DOI=10.1083/jcb.200611064; RA Karbowski M., Neutzner A., Youle R.J.; RT "The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 RT dependent mitochondrial division."; RL J. Cell Biol. 178:71-84(2007). RN [23] RP FUNCTION, VARIANT EMPF1 ASP-395, AND CHARACTERIZATION OF VARIANT EMPF1 RP ASP-395. RX PubMed=17460227; DOI=10.1056/nejmoa064436; RA Waterham H.R., Koster J., van Roermund C.W., Mooyer P.A., Wanders R.J., RA Leonard J.V.; RT "A lethal defect of mitochondrial and peroxisomal fission."; RL N. Engl. J. Med. 356:1736-1741(2007). RN [24] RP PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, AND RP MUTAGENESIS OF SER-637. RX PubMed=18695047; DOI=10.1083/jcb.200802164; RA Han X.J., Lu Y.F., Li S.A., Kaitsuka T., Sato Y., Tomizawa K., Nairn A.C., RA Takei K., Matsui H., Matsushita M.; RT "CaM kinase I alpha-induced phosphorylation of Drp1 regulates mitochondrial RT morphology."; RL J. Cell Biol. 182:573-585(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-607 AND SER-616, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [27] RP PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA, RP DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP SER-616 AND SER-637. RX PubMed=18838687; DOI=10.1073/pnas.0808249105; RA Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R., RA Blackstone C., Bernardi P., Scorrano L.; RT "Dephosphorylation by calcineurin regulates translocation of Drp1 to RT mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008). RN [28] 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 [29] RP SUMOYLATION BY MUL1. RX PubMed=19407830; DOI=10.1038/embor.2009.86; RA Braschi E., Zunino R., McBride H.M.; RT "MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial RT fission."; RL EMBO Rep. 10:748-754(2009). RN [30] RP SUMOYLATION AT LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; RP LYS-606 AND LYS-608, INTERACTION WITH UBE2I, FUNCTION, AND MUTAGENESIS OF RP LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; LYS-606 AND RP LYS-608. RX PubMed=19638400; DOI=10.1096/fj.09-136630; RA Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., Arnoult D., RA Keller P.J., Hong Y., Blackstone C., Feldman E.L.; RT "SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple RT nonconsensus sites within the B domain and is linked to its activity RT cycle."; RL FASEB J. 23:3917-3927(2009). RN [31] RP SUMOYLATION, DESUMOYLATION, AND FUNCTION. RX PubMed=19411255; DOI=10.1074/jbc.m901902200; RA Zunino R., Braschi E., Xu L., McBride H.M.; RT "Translocation of SenP5 from the nucleoli to the mitochondria modulates RT DRP1-dependent fission during mitosis."; RL J. Biol. Chem. 284:17783-17795(2009). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [33] RP S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE, RP AND MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367; CYS-431; CYS-446; RP CYS-470; CYS-505 AND CYS-644. RX PubMed=19342591; DOI=10.1126/science.1171091; RA Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., Lipton S.A.; RT "S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial RT fission and neuronal injury."; RL Science 324:102-105(2009). RN [34] RP POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20688057; DOI=10.1016/j.yexcr.2010.07.020; RA Bonekamp N.A., Vormund K., Jacob R., Schrader M.; RT "Dynamin-like protein 1 at the Golgi complex: A novel component of the RT sorting/targeting machinery en route to the plasma membrane."; RL Exp. Cell Res. 316:3454-3467(2010). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY RP MASS 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 [36] 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 [37] RP INTERACTION WITH MIEF2 AND MIEF1. RX PubMed=21508961; DOI=10.1038/embor.2011.54; RA Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., RA Ryan M.T.; RT "MiD49 and MiD51, new components of the mitochondrial fission machinery."; RL EMBO Rep. 12:565-573(2011). RN [38] RP INTERACTION WITH MIEF1. RX PubMed=21701560; DOI=10.1038/emboj.2011.198; RA Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., RA Shupliakov O., Lendahl U., Nister M.; RT "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes RT mitochondrial fusion rather than fission."; RL EMBO J. 30:2762-2778(2011). RN [39] RP INTERACTION WITH RALBP1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT RP SER-616 BY CDK1. RX PubMed=21822277; DOI=10.1038/ncb2310; RA Kashatus D.F., Lim K.H., Brady D.C., Pershing N.L., Cox A.D., Counter C.M.; RT "RALA and RALBP1 regulate mitochondrial fission at mitosis."; RL Nat. Cell Biol. 13:1108-1115(2011). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [41] RP FUNCTION, INTERACTION WITH PGAM5, AND SUBCELLULAR LOCATION. RX PubMed=22265414; DOI=10.1016/j.cell.2011.11.030; RA Wang Z., Jiang H., Chen S., Du F., Wang X.; RT "The mitochondrial phosphatase PGAM5 functions at the convergence point of RT multiple necrotic death pathways."; RL Cell 148:228-243(2012). RN [42] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [43] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23921378; DOI=10.1074/jbc.m113.479873; RA Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., RA Ryan M.T.; RT "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment RT and are specific for mitochondrial fission."; RL J. Biol. Chem. 288:27584-27593(2013). RN [44] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND SER-616, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [45] RP FUNCTION, INTERACTION WITH MIEF2 AND MIEF1, PHOSPHORYLATION AT SER-637, AND RP MUTAGENESIS OF SER-637. RX PubMed=23283981; DOI=10.1091/mbc.e12-10-0721; RA Loson O.C., Song Z., Chen H., Chan D.C.; RT "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial RT fission."; RL Mol. Biol. Cell 24:659-667(2013). RN [46] RP INTERACTION WITH BCL2L1, AND FUNCTION. RX PubMed=23792689; DOI=10.1038/ncb2791; RA Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P., RA Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S., RA Morrison R.S., Jonas E.A.; RT "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during RT endocytosis."; RL Nat. Cell Biol. 15:773-785(2013). RN [47] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY RP 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 [48] RP INTERACTION WITH FIS1; CANX; BCAP31. RX PubMed=24196833; DOI=10.1091/mbc.e13-09-0525; RA Shen Q., Yamano K., Head B.P., Kawajiri S., Cheung J.T., Wang C., Cho J.H., RA Hattori N., Youle R.J., van der Bliek A.M.; RT "Mutations in Fis1 disrupt orderly disposal of defective mitochondria."; RL Mol. Biol. Cell 25:145-159(2014). RN [49] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-616 AND SER-637. RX PubMed=26122121; DOI=10.1093/brain/awv182; RA Shahni R., Cale C.M., Anderson G., Osellame L.D., Hambleton S., RA Jacques T.S., Wedatilake Y., Taanman J.W., Chan E., Qasim W., Plagnol V., RA Chalasani A., Duchen M.R., Gilmour K.C., Rahman S.; RT "Signal transducer and activator of transcription 2 deficiency is a novel RT disorder of mitochondrial fission."; RL Brain 138:2834-2846(2015). RN [50] RP FUNCTION, INTERACTION WITH MIEF2, AND SUBUNIT. RX PubMed=23530241; DOI=10.1073/pnas.1300855110; RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.; RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for RT membrane scission."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013). RN [51] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FUNDC1. RX PubMed=27145933; DOI=10.15252/embj.201593102; RA Wu W., Lin C., Wu K., Jiang L., Wang X., Li W., Zhuang H., Zhang X., RA Chen H., Li S., Yang Y., Lu Y., Wang J., Zhu R., Zhang L., Sui S., Tan N., RA Zhao B., Zhang J., Li L., Feng D.; RT "FUNDC1 regulates mitochondrial dynamics at the ER-mitochondrial contact RT site under hypoxic conditions."; RL EMBO J. 35:1368-1384(2016). RN [52] RP FUNCTION, AND PHOSPHORYLATION AT SER-637. RX PubMed=29478834; DOI=10.1016/j.cmet.2018.01.011; RA Schmitt K., Grimm A., Dallmann R., Oettinghaus B., Restelli L.M., RA Witzig M., Ishihara N., Mihara K., Ripperger J.A., Albrecht U., Frank S., RA Brown S.A., Eckert A.; RT "Circadian control of DRP1 activity regulates mitochondrial dynamics and RT bioenergetics."; RL Cell Metab. 27:657-666(2018). RN [53] RP FUNCTION, PHOSPHORYLATION AT SER-616, AND MUTAGENESIS OF SER-616. RX PubMed=32484300; DOI=10.15252/embr.201948686; RA Han H., Tan J., Wang R., Wan H., He Y., Yan X., Guo J., Gao Q., Li J., RA Shang S., Chen F., Tian R., Liu W., Liao L., Tang B., Zhang Z.; RT "PINK1 phosphorylates Drp1S616 to regulate mitophagy-independent RT mitochondrial dynamics."; RL EMBO Rep. 21:48686-48686(2020). RN [54] RP FUNCTION, DEPHOSPHORYLATION BY PGAM5, MUTAGENESIS OF LYS-38 AND SER-637, RP AND PHOSPHORYLATION AT SER-637. RX PubMed=32439975; DOI=10.1038/s41467-020-16312-7; RA Yu B., Ma J., Li J., Wang D., Wang Z., Wang S.; RT "Mitochondrial phosphatase PGAM5 modulates cellular senescence by RT regulating mitochondrial dynamics."; RL Nat. Commun. 11:2549-2549(2020). RN [55] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=33850055; DOI=10.1126/scisignal.abc7931; RA Huang S., Li Z., Wu Z., Liu C., Yu M., Wen M., Zhang L., Wang X.; RT "DDAH2 suppresses RLR-MAVS-mediated innate antiviral immunity by RT stimulating nitric oxide-activated, Drp1-induced mitochondrial fission."; RL Sci. Signal. 14:0-0(2021). RN [56] RP X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, MUTAGENESIS OF 401-GLY--PRO-404; GLU-490 AND LYS-668, RP LIPID-BINDING, AND REGION. RX PubMed=23584531; DOI=10.1038/emboj.2013.74; RA Frohlich C., Grabiger S., Schwefel D., Faelber K., Rosenbaum E., Mears J., RA Rocks O., Daumke O.; RT "Structural insights into oligomerization and mitochondrial remodelling of RT dynamin 1-like protein."; RL EMBO J. 32:1280-1292(2013). RN [57] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-327 AND 711-736 IN COMPLEX WITH RP GTP ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-34; LYS-38; SER-39; RP THR-59; ASP-146; GLY-149; LYS-216 AND ASP-218, ACTIVITY REGULATION, AND RP SUBUNIT. RX PubMed=23977156; DOI=10.1371/journal.pone.0071835; RA Wenger J., Klinglmayr E., Frohlich C., Eibl C., Gimeno A., Hessenberger M., RA Puehringer S., Daumke O., Goettig P.; RT "Functional mapping of human dynamin-1-like GTPase domain based on x-ray RT structure analyses."; RL PLoS ONE 8:E71835-E71835(2013). RN [58] {ECO:0007744|PDB:5WP9} RP STRUCTURE BY ELECTRON MICROSCOPY (4.22 ANGSTROMS) (ISOFORM 2) IN COMPLEX RP WITH MIEF2, MUTAGENESIS OF ASP-190; ASP-221 AND SER-637, AND RP CHARACTERIZATION OF VARIANT EMPF1 ASP-362. RX PubMed=29899447; DOI=10.1038/s41586-018-0211-2; RA Kalia R., Wang R.Y., Yusuf A., Thomas P.V., Agard D.A., Shaw J.M., RA Frost A.; RT "Structural basis of mitochondrial receptor binding and constriction by RT DRP1."; RL Nature 558:401-405(2018). RN [59] RP VARIANT EMPF1 ASP-362, AND CHARACTERIZATION OF VARIANT EMPF1 ASP-362. RX PubMed=26604000; DOI=10.1038/ejhg.2015.243; RG Care4Rare Consortium; RA Vanstone J.R., Smith A.M., McBride S., Naas T., Holcik M., Antoun G., RA Harper M.E., Michaud J., Sell E., Chakraborty P., Tetreault M., RA Majewski J., Baird S., Boycott K.M., Dyment D.A., MacKenzie A., Lines M.A.; RT "DNM1L-related mitochondrial fission defect presenting as refractory RT epilepsy."; RL Eur. J. Hum. Genet. 24:1084-1088(2016). RN [60] RP VARIANT EMPF1 CYS-403, CHARACTERIZATION OF VARIANTS EMPF1 ASP-395 AND RP CYS-403, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=27145208; DOI=10.1002/ajmg.a.37721; RA Fahrner J.A., Liu R., Perry M.S., Klein J., Chan D.C.; RT "A novel de novo dominant negative mutation in DNM1L impairs mitochondrial RT fission and presents as childhood epileptic encephalopathy."; RL Am. J. Med. Genet. A 170:2002-2011(2016). RN [61] RP VARIANT EMPF1 SER-362, CHARACTERIZATION OF VARIANT EMPF1 SER-362, AND RP FUNCTION. RX PubMed=26992161; DOI=10.1002/ajmg.a.37624; RA Sheffer R., Douiev L., Edvardson S., Shaag A., Tamimi K., Soiferman D., RA Meiner V., Saada A.; RT "Postnatal microcephaly and pain insensitivity due to a de novo RT heterozygous DNM1L mutation causing impaired mitochondrial fission and RT function."; RL Am. J. Med. Genet. A 170:1603-1607(2016). RN [62] RP VARIANT EMPF1 SER-406, CHARACTERIZATION OF VARIANT EMPF1 SER-406, AND RP FUNCTION. RX PubMed=27301544; DOI=10.1111/cge.12805; RA Zaha K., Matsumoto H., Itoh M., Saitsu H., Kato K., Kato M., Ogata S., RA Murayama K., Kishita Y., Mizuno Y., Kohda M., Nishino I., Ohtake A., RA Okazaki Y., Matsumoto N., Nonoyama S.; RT "DNM1L-related encephalopathy in infancy with Leigh syndrome-like phenotype RT and suppression-burst."; RL Clin. Genet. 90:472-474(2016). RN [63] RP VARIANT EMPF1 GLY-36, CHARACTERIZATION OF VARIANT EMPF1 GLY-36, AND RP FUNCTION. RX PubMed=27328748; DOI=10.1002/humu.23033; RA Nasca A., Legati A., Baruffini E., Nolli C., Moroni I., Ardissone A., RA Goffrini P., Ghezzi D.; RT "Biallelic Mutations in DNM1L are Associated with a Slowly Progressive RT Infantile Encephalopathy."; RL Hum. Mutat. 37:898-903(2016). RN [64] RP INVOLVEMENT IN OPA5, VARIANTS OPA5 ALA-2 AND GLU-192, CHARACTERIZATION OF RP VARIANTS OPA5 ALA-2 AND GLU-192, AND SUBCELLULAR LOCATION. RX PubMed=28969390; DOI=10.1093/brain/awx219; RA Gerber S., Charif M., Chevrollier A., Chaumette T., Angebault C., RA Kane M.S., Paris A., Alban J., Quiles M., Delettre C., Bonneau D., RA Procaccio V., Amati-Bonneau P., Reynier P., Leruez S., Calmon R., RA Boddaert N., Funalot B., Rio M., Bouccara D., Meunier I., Sesaki H., RA Kaplan J., Hamel C.P., Rozet J.M., Lenaers G.; RT "Mutations in DNM1L, as in OPA1, result indominant optic atrophy despite RT opposite effectson mitochondrial fusion and fission."; RL Brain 140:2586-2596(2017). CC -!- FUNCTION: Functions in mitochondrial and peroxisomal division CC (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, CC PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, CC PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, CC PubMed:23921378, PubMed:26992161, PubMed:27145208, PubMed:27145933, CC PubMed:27301544, PubMed:27328748, PubMed:29478834, PubMed:32439975, CC PubMed:32484300, PubMed:9570752, PubMed:9786947). Mediates membrane CC fission through oligomerization into membrane-associated tubular CC structures that wrap around the scission site to constrict and sever CC the mitochondrial membrane through a GTP hydrolysis-dependent mechanism CC (PubMed:23530241, PubMed:23584531, PubMed:33850055). The specific CC recruitment at scission sites is mediated by membrane receptors like CC MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, CC PubMed:23921378, PubMed:29899447). While the recruitment by the CC membrane receptors is GTP-dependent, the following hydrolysis of GTP CC induces the dissociation from the receptors and allows DNM1L filaments CC to curl into closed rings that are probably sufficient to sever a CC double membrane (PubMed:29899447). Acts downstream of PINK1 to promote CC mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). CC Plays an important role in mitochondrial fission during mitosis CC (PubMed:19411255, PubMed:26992161, PubMed:27301544, PubMed:27328748). CC Through its function in mitochondrial division, ensures the survival of CC at least some types of postmitotic neurons, including Purkinje cells, CC by suppressing oxidative damage (By similarity). Required for normal CC brain development, including that of cerebellum (PubMed:17460227, CC PubMed:26992161, PubMed:27145208, PubMed:27301544, PubMed:27328748). CC Facilitates developmentally regulated apoptosis during neural tube CC formation (By similarity). Required for a normal rate of cytochrome c CC release and caspase activation during apoptosis; this requirement may CC depend upon the cell type and the physiological apoptotic cues (By CC similarity). Required for formation of endocytic vesicles CC (PubMed:20688057, PubMed:23792689, PubMed:9570752). Proposed to CC regulate synaptic vesicle membrane dynamics through association with CC BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in CC synaptic vesicles; the function may require its recruitment by MFF to CC clathrin-containing vesicles (PubMed:17015472, PubMed:23792689). CC Required for programmed necrosis execution (PubMed:22265414). Rhythmic CC control of its activity following phosphorylation at Ser-637 is CC essential for the circadian control of mitochondrial ATP production CC (PubMed:29478834). {ECO:0000250|UniProtKB:Q8K1M6, CC ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366, CC ECO:0000269|PubMed:17015472, ECO:0000269|PubMed:17301055, CC ECO:0000269|PubMed:17460227, ECO:0000269|PubMed:17553808, CC ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, CC ECO:0000269|PubMed:19342591, ECO:0000269|PubMed:19411255, CC ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:20688057, CC ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:23283981, CC ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531, CC ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:23921378, CC ECO:0000269|PubMed:26992161, ECO:0000269|PubMed:27145208, CC ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:27301544, CC ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29478834, CC ECO:0000269|PubMed:29899447, ECO:0000269|PubMed:32439975, CC ECO:0000269|PubMed:32484300, ECO:0000269|PubMed:33850055, CC ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9786947}. CC -!- FUNCTION: [Isoform 1]: Inhibits peroxisomal division when CC overexpressed. {ECO:0000269|PubMed:12618434}. CC -!- FUNCTION: [Isoform 4]: Inhibits peroxisomal division when CC overexpressed. {ECO:0000269|PubMed:12618434}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; CC Evidence={ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767}; CC -!- ACTIVITY REGULATION: GTPase activity is increased by binding to CC phospholipid membranes. {ECO:0000269|PubMed:23977156}. CC -!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle CC region of one molecule binding to the GED domain of another DNM1L CC molecule (PubMed:17553808, PubMed:23530241, PubMed:23584531, CC PubMed:23977156). Oligomerizes in a GTP-dependent manner to form CC membrane-associated tubules with a spiral pattern (PubMed:23584531). CC Interacts with GSK3B and MARCHF5 (PubMed:10749171, PubMed:16874301, CC PubMed:16936636, PubMed:9731200). Interacts (via the GTPase and B CC domains) with UBE2I; the interaction promotes sumoylation of DNM1L, CC mainly in its B domain (PubMed:19638400). Interacts with PPP3CA; the CC interaction dephosphorylates DNM1L and regulates its transition to CC mitochondria (PubMed:18838687). Interacts with BCL2L1 isoform BCL-X(L) CC and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in CC synaptic vesicles that also contains clathrin and MFF CC (PubMed:23792689). Interacts with MFF; the interaction is inhibited by CC C11orf65/MFI (By similarity). Interacts with FIS1; may form part of a CC larger protein complex at the endoplasmic reticulum-mitochondrial CC interface during mitochondrial fission (PubMed:18695047, CC PubMed:24196833). Interacts with CANX (PubMed:24196833). Interacts with CC BCAP31 (PubMed:24196833). Interacts with MIEF2 and MIEF1; GTP- CC dependent, regulates GTP hydrolysis and DNM1L oligomerization CC (PubMed:21508961). Interacts with PGAM5; this interaction leads to CC dephosphorylation at Ser-656 and activation of GTPase activity and CC eventually to mitochondria fragmentation (PubMed:22265414). Interacts CC with RALBP1; during mitosis, recruits DNM1L to the mitochondrion and CC mediates its activation by the mitotic kinase cyclin B-CDK1 CC (PubMed:21822277). Interacts with FUNDC1; this interaction recruits CC DNM1L/DRP1 at ER-mitochondria contact sites (PubMed:27145933). CC {ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:10749171, CC ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636, CC ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, CC ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19638400, CC ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, CC ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:22265414, CC ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, CC ECO:0000269|PubMed:23584531, ECO:0000269|PubMed:23792689, CC ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:27145208, CC ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:9731200}. CC -!- INTERACTION: CC O00429; Q9NVI7: ATAD3A; NbExp=4; IntAct=EBI-724571, EBI-352007; CC O00429; Q9NVI7-2: ATAD3A; NbExp=5; IntAct=EBI-724571, EBI-5456381; CC O00429; O00429: DNM1L; NbExp=2; IntAct=EBI-724571, EBI-724571; CC O00429; P03372: ESR1; NbExp=2; IntAct=EBI-724571, EBI-78473; CC O00429; Q9Y3D6: FIS1; NbExp=2; IntAct=EBI-724571, EBI-3385283; CC O00429; Q5S007: LRRK2; NbExp=16; IntAct=EBI-724571, EBI-5323863; CC O00429; Q9GZY8: MFF; NbExp=3; IntAct=EBI-724571, EBI-11420856; CC O00429; Q9NQG6: MIEF1; NbExp=11; IntAct=EBI-724571, EBI-740987; CC O00429; Q96C03: MIEF2; NbExp=5; IntAct=EBI-724571, EBI-750153; CC O00429; Q9Y512: SAMM50; NbExp=3; IntAct=EBI-724571, EBI-748409; CC O00429; Q14160: SCRIB; NbExp=2; IntAct=EBI-724571, EBI-357345; CC O00429-3; O00429-3: DNM1L; NbExp=8; IntAct=EBI-6896746, EBI-6896746; CC O00429-3; Q5S007: LRRK2; NbExp=2; IntAct=EBI-6896746, EBI-5323863; CC O00429-3; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-6896746, EBI-6447163; CC O00429-3; O95563: MPC2; NbExp=3; IntAct=EBI-6896746, EBI-719403; CC O00429-3; P21980-2: TGM2; NbExp=3; IntAct=EBI-6896746, EBI-25842075; CC O00429-3; O43257: ZNHIT1; NbExp=3; IntAct=EBI-6896746, EBI-347522; CC O00429-4; O00429-4: DNM1L; NbExp=2; IntAct=EBI-4420450, EBI-4420450; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11514614, CC ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:9786947}. Golgi CC apparatus {ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:9348079, CC ECO:0000269|PubMed:9570752}. Endomembrane system CC {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:9348079, CC ECO:0000269|PubMed:9472031, ECO:0000269|PubMed:9570752}; Peripheral CC membrane protein. Mitochondrion outer membrane CC {ECO:0000269|PubMed:26122121, ECO:0000269|PubMed:27145208, CC ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:28969390}; Peripheral CC membrane protein. Peroxisome {ECO:0000269|PubMed:12499366, CC ECO:0000269|PubMed:12618434}. Membrane, clathrin-coated pit CC {ECO:0000250|UniProtKB:O35303}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane {ECO:0000250|UniProtKB:O35303}. Note=Mainly CC cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis CC (PubMed:21822277). Translocated to the mitochondrial membrane through CC O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at CC mitochondrial membrane (PubMed:17606867). Localizes to mitochondria at CC sites of division (PubMed:15208300). Localizes to mitochondria CC following necrosis induction. Recruited to the mitochondrial outer CC membrane by interaction with MIEF1. Mitochondrial recruitment is CC inhibited by C11orf65/MFI (By similarity). Associated with peroxisomal CC membranes, partly recruited there by PEX11B. May also be associated CC with endoplasmic reticulum tubules and cytoplasmic vesicles and found CC to be perinuclear (PubMed:9422767, PubMed:9570752). In some cell types, CC localizes to the Golgi complex (By similarity). Binds to phospholipid CC membranes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8K1M6, CC ECO:0000269|PubMed:15208300, ECO:0000269|PubMed:17606867, CC ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:9422767, CC ECO:0000269|PubMed:9570752}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=HdynIV-WT, DLP1F; CC IsoId=O00429-1; Sequence=Displayed; CC Name=4; Synonyms=HdynIV-11, DLP1c; CC IsoId=O00429-2; Sequence=VSP_013688; CC Name=2; Synonyms=DLP1a; CC IsoId=O00429-3; Sequence=VSP_013686; CC Name=3; Synonyms=HdynIV-37, DLP1b; CC IsoId=O00429-4; Sequence=VSP_013685; CC Name=5; Synonyms=HdynIV-26; CC IsoId=O00429-5; Sequence=VSP_013687; CC Name=6; CC IsoId=O00429-6; Sequence=VSP_039097; CC Name=7; CC IsoId=O00429-7; Sequence=VSP_054544, VSP_054545; CC Name=8; CC IsoId=O00429-8; Sequence=VSP_039097, VSP_013688; CC Name=9; CC IsoId=O00429-9; Sequence=VSP_039097, VSP_013685; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels found in CC skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. CC Isoform 2 and isoform 3 are predominantly expressed in testis and CC skeletal muscles respectively. Isoform 4 is weakly expressed in brain, CC heart and kidney. Isoform 5 is dominantly expressed in liver, heart and CC kidney. Isoform 6 is expressed in neurons. CC {ECO:0000269|PubMed:10749171, ECO:0000269|PubMed:9422767, CC ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9731200, CC ECO:0000269|PubMed:9786947}. CC -!- DOMAIN: The GED domain folds back to interact, in cis, with the GTP- CC binding domain and middle domain, and interacts, in trans, with the GED CC domains of other DNM1L molecules, and is thus critical for activating CC GTPase activity and for DNM1L dimerization. CC {ECO:0000269|PubMed:15208300}. CC -!- PTM: Phosphorylation/dephosphorylation events on two sites near the GED CC domain regulate mitochondrial fission (PubMed:17301055, CC PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:23283981, CC PubMed:29478834, PubMed:33850055). Phosphorylation on Ser-637 by CAMK1 CC and PKA inhibits the GTPase activity, leading to a defect in CC mitochondrial fission promoting mitochondrial elongation CC (PubMed:17553808, PubMed:18695047, PubMed:23283981, PubMed:29478834). CC Dephosphorylated on this site by PPP3CA which promotes mitochondrial CC fission (PubMed:18838687). Phosphorylation on Ser-616 by CDK1 and PINK1 CC activates the GTPase activity and promotes mitochondrial fission CC (PubMed:18838687, PubMed:21822277, PubMed:32484300). Phosphorylated in CC a circadian manner at Ser-637 (PubMed:29478834). Dephosphorylated by CC PGAM5 (PubMed:32439975). {ECO:0000269|PubMed:17301055, CC ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, CC ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:21822277, CC ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:29478834, CC ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:32484300, CC ECO:0000269|PubMed:33850055}. CC -!- PTM: Sumoylated on various lysine residues within the B domain, CC probably by MUL1. Sumoylation positively regulates mitochondrial CC fission. Desumoylated by SENP5 during G2/M transition of mitosis. CC Appears to be linked to its catalytic activity. CC {ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:19411255, CC ECO:0000269|PubMed:19638400}. CC -!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial CC fission and causes neuronal damage. {ECO:0000269|PubMed:19342591}. CC -!- PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology. CC {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636}. CC -!- PTM: O-GlcNAcylation augments the level of the GTP-bound active form of CC DNM1L and induces translocation from the cytoplasm to mitochondria in CC cardiomyocytes. It also decreases phosphorylation at Ser-637 (By CC similarity). {ECO:0000250|UniProtKB:O35303}. CC -!- DISEASE: Note=May be associated with Alzheimer disease through amyloid- CC beta-induced increased S-nitrosylation of DNM1L, which triggers, CC directly or indirectly, excessive mitochondrial fission, synaptic loss CC and neuronal damage. {ECO:0000269|PubMed:19342591}. CC -!- DISEASE: Encephalopathy due to defective mitochondrial and peroxisomal CC fission 1 (EMPF1) [MIM:614388]: A rare autosomal dominant systemic CC disorder resulting in lack of neurologic development and death in CC infancy. After birth, infants present in the first week of life with CC poor feeding and neurologic impairment, including hypotonia, little CC spontaneous movement, no tendon reflexes, no response to light CC stimulation, and poor visual fixation. Other features include mildly CC elevated plasma concentration of very-long-chain fatty acids, lactic CC acidosis, microcephaly, deep-set eyes, optic atrophy and hypoplasia, CC and an abnormal gyral pattern in both frontal lobes associated with CC dysmyelination. {ECO:0000269|PubMed:17460227, CC ECO:0000269|PubMed:26604000, ECO:0000269|PubMed:26992161, CC ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27301544, CC ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29899447}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Optic atrophy 5 (OPA5) [MIM:610708]: A form of optic atrophy, CC a disease characterized by progressive visual loss in association with CC a deficiency in the number of nerve fibers which arise in the retina CC and converge to form the optic disk, optic nerve, optic chiasm and CC optic tracts. OPA5 is an autosomal dominant non-syndromic form that CC manifests as slowly progressive visual loss with variable onset from CC the first to third decades. Additional ocular abnormalities may include CC central scotoma and dyschromatopsia. {ECO:0000269|PubMed:28969390}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE- CC ProRule:PRU01055}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92307.1; Type=Erroneous initiation; Note=Extended 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; AB006965; BAA22193.1; -; mRNA. DR EMBL; AF061795; AAC35283.1; -; mRNA. DR EMBL; AF000430; AAC23724.1; -; mRNA. DR EMBL; AF151685; AAD39541.1; -; mRNA. DR EMBL; AK299926; BAG61760.1; -; mRNA. DR EMBL; AK291094; BAF83783.1; -; mRNA. DR EMBL; AK294533; BAG57740.1; -; mRNA. DR EMBL; AB209070; BAD92307.1; ALT_INIT; mRNA. DR EMBL; AC084824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087588; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC024590; AAH24590.1; -; mRNA. DR CCDS; CCDS61095.1; -. [O00429-6] DR CCDS; CCDS61096.1; -. [O00429-8] DR CCDS; CCDS61098.1; -. [O00429-2] DR CCDS; CCDS81680.1; -. [O00429-9] DR CCDS; CCDS8728.1; -. [O00429-4] DR CCDS; CCDS8729.1; -. [O00429-1] DR CCDS; CCDS8730.1; -. [O00429-3] DR PIR; JC5695; JC5695. DR RefSeq; NP_001265392.1; NM_001278463.1. [O00429-2] DR RefSeq; NP_001265393.1; NM_001278464.1. [O00429-6] DR RefSeq; NP_001265394.1; NM_001278465.1. [O00429-8] DR RefSeq; NP_001265395.1; NM_001278466.1. [O00429-7] DR RefSeq; NP_001317309.1; NM_001330380.1. [O00429-9] DR RefSeq; NP_005681.2; NM_005690.4. [O00429-4] DR RefSeq; NP_036192.2; NM_012062.4. [O00429-1] DR RefSeq; NP_036193.2; NM_012063.3. [O00429-3] DR PDB; 3W6N; X-ray; 2.00 A; A/B=1-329, A/B=709-736. DR PDB; 3W6O; X-ray; 1.90 A; A/B=1-329, A/B=709-736. DR PDB; 3W6P; X-ray; 1.70 A; A/B=1-329, A/B=709-736. DR PDB; 4BEJ; X-ray; 3.48 A; A/B/C/D=1-736. DR PDB; 4H1U; X-ray; 2.30 A; A=1-327, A=711-736. DR PDB; 4H1V; X-ray; 2.30 A; A=1-327, A=711-736. DR PDB; 5WP9; EM; 4.22 A; A/C/E/G/I/K/M/O=1-736. DR PDB; 8T1H; EM; 5.97 A; A/B=1-736. DR PDBsum; 3W6N; -. DR PDBsum; 3W6O; -. DR PDBsum; 3W6P; -. DR PDBsum; 4BEJ; -. DR PDBsum; 4H1U; -. DR PDBsum; 4H1V; -. DR PDBsum; 5WP9; -. DR PDBsum; 8T1H; -. DR AlphaFoldDB; O00429; -. DR EMDB; EMD-8874; -. DR SMR; O00429; -. DR BioGRID; 115370; 358. DR CORUM; O00429; -. DR DIP; DIP-42704N; -. DR IntAct; O00429; 236. DR MINT; O00429; -. DR STRING; 9606.ENSP00000449089; -. DR BindingDB; O00429; -. DR ChEMBL; CHEMBL4523118; -. DR TCDB; 1.N.6.1.2; the mitochondrial inner/outer membrane fusion (mmf) family. DR GlyCosmos; O00429; 4 sites, 1 glycan. DR GlyGen; O00429; 4 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O00429; -. DR MetOSite; O00429; -. DR PhosphoSitePlus; O00429; -. DR SwissPalm; O00429; -. DR BioMuta; DNM1L; -. DR CPTAC; CPTAC-57; -. DR EPD; O00429; -. DR jPOST; O00429; -. DR MassIVE; O00429; -. DR MaxQB; O00429; -. DR PaxDb; 9606-ENSP00000449089; -. DR PeptideAtlas; O00429; -. DR ProteomicsDB; 34194; -. DR ProteomicsDB; 4122; -. DR ProteomicsDB; 47884; -. [O00429-1] DR ProteomicsDB; 47885; -. [O00429-2] DR ProteomicsDB; 47886; -. [O00429-3] DR ProteomicsDB; 47887; -. [O00429-4] DR ProteomicsDB; 47888; -. [O00429-5] DR ProteomicsDB; 47889; -. [O00429-6] DR Pumba; O00429; -. DR Antibodypedia; 4096; 869 antibodies from 38 providers. DR DNASU; 10059; -. DR Ensembl; ENST00000266481.10; ENSP00000266481.6; ENSG00000087470.21. [O00429-4] DR Ensembl; ENST00000358214.9; ENSP00000350948.5; ENSG00000087470.21. [O00429-9] DR Ensembl; ENST00000381000.8; ENSP00000370388.4; ENSG00000087470.21. [O00429-8] DR Ensembl; ENST00000452533.6; ENSP00000415131.2; ENSG00000087470.21. [O00429-3] DR Ensembl; ENST00000547312.5; ENSP00000448610.1; ENSG00000087470.21. [O00429-2] DR Ensembl; ENST00000549701.6; ENSP00000450399.1; ENSG00000087470.21. [O00429-1] DR Ensembl; ENST00000553257.6; ENSP00000449089.1; ENSG00000087470.21. [O00429-6] DR GeneID; 10059; -. DR KEGG; hsa:10059; -. DR MANE-Select; ENST00000549701.6; ENSP00000450399.1; NM_012062.5; NP_036192.2. DR UCSC; uc001rld.4; human. [O00429-1] DR AGR; HGNC:2973; -. DR CTD; 10059; -. DR DisGeNET; 10059; -. DR GeneCards; DNM1L; -. DR HGNC; HGNC:2973; DNM1L. DR HPA; ENSG00000087470; Low tissue specificity. DR MalaCards; DNM1L; -. DR MIM; 603850; gene. DR MIM; 610708; phenotype. DR MIM; 614388; phenotype. DR neXtProt; NX_O00429; -. DR NIAGADS; ENSG00000087470; -. DR OpenTargets; ENSG00000087470; -. DR Orphanet; 98673; Autosomal dominant optic atrophy, classic form. DR Orphanet; 330050; DNM1L-related encephalopathy due to mitochondrial and peroxisomal fission defect. DR PharmGKB; PA27441; -. DR VEuPathDB; HostDB:ENSG00000087470; -. DR eggNOG; KOG0446; Eukaryota. DR GeneTree; ENSGT00940000155504; -. DR HOGENOM; CLU_008964_5_4_1; -. DR InParanoid; O00429; -. DR OMA; KICHNCG; -. DR OrthoDB; 1052588at2759; -. DR PhylomeDB; O00429; -. DR TreeFam; TF352031; -. DR BRENDA; 3.6.5.5; 2681. DR PathwayCommons; O00429; -. DR Reactome; R-HSA-75153; Apoptotic execution phase. DR SignaLink; O00429; -. DR SIGNOR; O00429; -. DR BioGRID-ORCS; 10059; 516 hits in 1170 CRISPR screens. DR ChiTaRS; DNM1L; human. DR GeneWiki; DNM1L; -. DR GenomeRNAi; 10059; -. DR Pharos; O00429; Tchem. DR PRO; PR:O00429; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; O00429; Protein. DR Bgee; ENSG00000087470; Expressed in lateral nuclear group of thalamus and 209 other cell types or tissues. DR ExpressionAtlas; O00429; baseline and differential. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0005096; F:GTPase activator activity; IC:ParkinsonsUK-UCL. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR GO; GO:0060047; P:heart contraction; IEA:Ensembl. DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:ParkinsonsUK-UCL. DR GO; GO:0061025; P:membrane fusion; IDA:UniProtKB. DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0090149; P:mitochondrial membrane fission; IDA:UniProtKB. DR GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL. DR GO; GO:0160040; P:mitocytosis; IEA:Ensembl. DR GO; GO:0070266; P:necroptotic process; IMP:UniProtKB. DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL. DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:CACAO. DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:UniProtKB. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB. DR GO; GO:0051259; P:protein complex oligomerization; IMP:UniProtKB. DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:DisProt. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:1903578; P:regulation of ATP metabolic process; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR GO; GO:1901524; P:regulation of mitophagy; IGI:ParkinsonsUK-UCL. DR GO; GO:1900063; P:regulation of peroxisome organization; IMP:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR CDD; cd08771; DLP_1; 1. DR DisProt; DP01537; -. [O00429-3] DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR022812; Dynamin. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR045063; Dynamin_N. DR InterPro; IPR000375; Dynamin_stalk. DR InterPro; IPR030381; G_DYNAMIN_dom. DR InterPro; IPR003130; GED. DR InterPro; IPR020850; GED_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11566; DYNAMIN; 1. DR PANTHER; PTHR11566:SF39; DYNAMIN-1-LIKE PROTEIN; 1. DR Pfam; PF01031; Dynamin_M; 1. DR Pfam; PF00350; Dynamin_N; 1. DR Pfam; PF02212; GED; 1. DR PRINTS; PR00195; DYNAMIN. DR SMART; SM00053; DYNc; 1. DR SMART; SM00302; GED; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00410; G_DYNAMIN_1; 1. DR PROSITE; PS51718; G_DYNAMIN_2; 1. DR PROSITE; PS51388; GED; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms; KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Disease variant; Endocytosis; KW Glycoprotein; Golgi apparatus; GTP-binding; Hydrolase; Isopeptide bond; KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Necrosis; Nucleotide-binding; Peroxisome; Phosphoprotein; KW Reference proteome; S-nitrosylation; Synapse; Ubl conjugation. FT CHAIN 1..736 FT /note="Dynamin-1-like protein" FT /id="PRO_0000206566" FT DOMAIN 22..302 FT /note="Dynamin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT DOMAIN 644..735 FT /note="GED" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720" FT REGION 32..39 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 58..60 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 146..149 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 215..218 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 245..248 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055" FT REGION 344..489 FT /note="Middle domain" FT /evidence="ECO:0000269|PubMed:15208300" FT REGION 448..685 FT /note="Interaction with GSK3B" FT /evidence="ECO:0000269|PubMed:9731200" FT REGION 502..569 FT /note="B domain" FT /evidence="ECO:0000269|PubMed:15208300" FT REGION 523..590 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 654..668 FT /note="Important for homodimerization" FT /evidence="ECO:0000269|PubMed:23584531" FT BINDING 32..40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:23977156" FT BINDING 215..221 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:23977156" FT BINDING 246..249 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:23977156" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 529 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 548 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 597 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8K1M6" FT MOD_RES 607 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 616 FT /note="Phosphoserine; by CDK1 and PINK1" FT /evidence="ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:26122121, FT ECO:0000269|PubMed:32484300, ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 637 FT /note="Phosphoserine; by CAMK1 and PKA" FT /evidence="ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:26122121, FT ECO:0000269|PubMed:32439975" FT MOD_RES 644 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:19342591" FT CARBOHYD 585 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 586 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CROSSLNK 532 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 535 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 558 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 568 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 594 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 597 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 606 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT CROSSLNK 608 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:19638400" FT VAR_SEQ 1..43 FT /note="MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLE -> MFHKK FT INGKQQEKKMTLLHGKTQDTFLKGWKQKNGVNFFTPKI (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054544" FT VAR_SEQ 44..246 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054545" FT VAR_SEQ 83 FT /note="N -> NDPATWKNSRHLSK (in isoform 6, isoform 8 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.6" FT /id="VSP_039097" FT VAR_SEQ 533..569 FT /note="Missing (in isoform 3 and isoform 9)" FT /evidence="ECO:0000303|PubMed:10749171, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9731200" FT /id="VSP_013685" FT VAR_SEQ 533..558 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013686" FT VAR_SEQ 544..569 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10749171" FT /id="VSP_013687" FT VAR_SEQ 559..569 FT /note="Missing (in isoform 4 and isoform 8)" FT /evidence="ECO:0000303|PubMed:10749171, ECO:0000303|Ref.6" FT /id="VSP_013688" FT VARIANT 2 FT /note="E -> A (in OPA5; changed localization to FT mitochondrion; impaired mitochondrial membrane fission; FT dbSNP:rs1555229948)" FT /evidence="ECO:0000269|PubMed:28969390" FT /id="VAR_080869" FT VARIANT 36 FT /note="S -> G (in EMPF1; autosomal recessive; impaired FT mitochondrial membrane fission; hypomorphic mutation FT retaining partial activity in mitochondrial membrane FT fission; dbSNP:rs879255688)" FT /evidence="ECO:0000269|PubMed:27328748" FT /id="VAR_080870" FT VARIANT 71 FT /note="S -> T (in dbSNP:rs1064610)" FT /evidence="ECO:0000269|PubMed:10749171, FT ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9731200" FT /id="VAR_022446" FT VARIANT 192 FT /note="A -> E (in OPA5; changed localization to FT mitochondrion; impaired mitochondrial membrane fission; FT dbSNP:rs1555119216)" FT /evidence="ECO:0000269|PubMed:28969390" FT /id="VAR_080871" FT VARIANT 362 FT /note="G -> D (in EMPF1; uncertain significance; unable to FT associate with MIEF2 into filaments forming the tubular FT structures that wrap around the scission site; presence of FT concentric cristae and/or increased dense granules in some FT mitochondria; dbSNP:rs879255685)" FT /evidence="ECO:0000269|PubMed:26604000, FT ECO:0000269|PubMed:29899447" FT /id="VAR_076316" FT VARIANT 362 FT /note="G -> S (in EMPF1; the mutation acts in a dominant- FT negative manner; defects observed in mitochondrial fission; FT significant decrease in mitochondrial respiratory chain FT complex IV activity; dbSNP:rs886037861)" FT /evidence="ECO:0000269|PubMed:26992161" FT /id="VAR_076317" FT VARIANT 395 FT /note="A -> D (in EMPF1; the mutation acts in a dominant- FT negative manner; defects observed in both mitochondrial and FT peroxisomal fission; reduced oligomerization, decreased FT mitochondrial recruitment; dbSNP:rs121908531)" FT /evidence="ECO:0000269|PubMed:17460227, FT ECO:0000269|PubMed:27145208" FT /id="VAR_063704" FT VARIANT 403 FT /note="R -> C (in EMPF1; the mutation acts in a dominant- FT negative manner; reduced oligomerization; decreased FT mitochondrial recruitment; defects observed in FT mitochondrial fission; dbSNP:rs863223953)" FT /evidence="ECO:0000269|PubMed:27145208" FT /id="VAR_076318" FT VARIANT 406 FT /note="L -> S (in EMPF1; impaired mitochondrial and FT peroxisomal membrane fission)" FT /evidence="ECO:0000269|PubMed:27301544" FT /id="VAR_080872" FT VARIANT 426 FT /note="E -> D (in dbSNP:rs2389105)" FT /id="VAR_030489" FT MUTAGEN 34 FT /note="Q->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:23977156" FT MUTAGEN 38 FT /note="K->A: Loss of GTPase activity. Impairs mitochondrial FT division and induces changes in peroxisome morphology. No FT effect on oligomerization. Increase in sumoylation by FT SUMO3." FT /evidence="ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:15208300, FT ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:9570752" FT MUTAGEN 38 FT /note="K->E: Overexpression delays protein secretion. FT Rescues fragmented or truncated mitochondria in PRKN- or FT PINK1-depleted cells." FT /evidence="ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:15208300, FT ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:23977156, FT ECO:0000269|PubMed:9570752" FT MUTAGEN 39 FT /note="S->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767" FT MUTAGEN 39 FT /note="S->I: Decreased localization to the perinuclear FT region." FT /evidence="ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767" FT MUTAGEN 39 FT /note="S->N: Reduces peroxisomal abundance." FT /evidence="ECO:0000269|PubMed:12618434, FT ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767" FT MUTAGEN 41 FT /note="V->F: Temperature-sensitive. Impairs mitochondrial FT division." FT /evidence="ECO:0000269|PubMed:11514614" FT MUTAGEN 59 FT /note="T->A: Abolishes GTP hydrolysis. Impairs FT mitochondrial division. Reduces peroxisomal abundance." FT /evidence="ECO:0000269|PubMed:11514614, FT ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:23977156" FT MUTAGEN 146 FT /note="D->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:23977156" FT MUTAGEN 149 FT /note="G->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:23977156" FT MUTAGEN 190 FT /note="D->A: Unable to homooligomerize. Unable to associate FT with MIEF2 into filaments forming the tubular structures FT that wrap around the scission site." FT /evidence="ECO:0000269|PubMed:29899447" FT MUTAGEN 216 FT /note="K->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:23977156" FT MUTAGEN 218 FT /note="D->A: Abolishes GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:23977156" FT MUTAGEN 221 FT /note="D->A: Unable to homooligomerize. Unable to associate FT with MIEF2 into filaments forming the tubular structures FT that wrap around the scission site." FT /evidence="ECO:0000269|PubMed:29899447" FT MUTAGEN 281 FT /note="G->D: Temperature-sensitive. Impairs mitochondrial FT division." FT /evidence="ECO:0000269|PubMed:11514614" FT MUTAGEN 300 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 345 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 361 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 367 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 401..404 FT /note="GPRP->AAAA: Impairs formation of higher order FT oligomers, but not homodimerization." FT /evidence="ECO:0000269|PubMed:23584531" FT MUTAGEN 431 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 446 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 470 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 490 FT /note="E->A: Does not impair homodimerization and formation FT of higher order oligomers." FT /evidence="ECO:0000269|PubMed:23584531" FT MUTAGEN 490 FT /note="E->R: Impairs homodimerization and formation of FT higher order oligomers." FT /evidence="ECO:0000269|PubMed:23584531" FT MUTAGEN 505 FT /note="C->A: No effect on S-nitrosylation." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 532 FT /note="K->R: Some loss of sumoylation in B domain. Complete FT loss of sumoylation in B domain; when associated with R- FT 535; R-558 and R-568." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 535 FT /note="K->R: Some loss of sumoylation in B domain. Complete FT loss of sumoylation in B domain; when associated with R- FT 532; R-558 and R-568." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 558 FT /note="K->R: Some loss of sumoylation in B domain. Complete FT loss of sumoylation in B domain; when associated with R- FT 532; R-535 and R-568." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 568 FT /note="K->R: Some loss of sumoylation in B domain. Complete FT loss of sumoylation in B domain; when associated with R- FT 532; R-535 and R-558." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 594 FT /note="K->R: Some loss of sumoylation in the GED domain; FT Complete loss of sumoylation in the GED domain; when FT associated with R-597; R-606 and R-608." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 597 FT /note="K->R: Some loss of sumoylation in the GED domain; FT Complete loss of sumoylation in the GED domain; when FT associated with R-594; R-606 and R-608." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 606 FT /note="K->R: Some loss of sumoylation in the GED domain; FT Complete loss of sumoylation in the GED domain; when FT associated with R-594; R-597 and R-608." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 608 FT /note="K->R: Some loss of sumoylation in the GED domain; FT Complete loss of sumoylation in the GED domain; when FT associated with R-594; R-597 and R-606." FT /evidence="ECO:0000269|PubMed:19638400" FT MUTAGEN 616 FT /note="S->A: Loss of activity. Little effect on FT mitochondrial morphology. Translocated to mitochondria." FT /evidence="ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:32484300" FT MUTAGEN 637 FT /note="S->A: Abolishes phosphorylation. Reduces interaction FT with MIEF1 and MIEF2. Promotes mitochondrial fission and FT cell vulnerability to apoptotic insults. Mostly FT mitochondrial. Disrupts, in vitro, binding to FIS1." FT /evidence="ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981" FT MUTAGEN 637 FT /note="S->D: Impairs intramolecular interactions but not FT homooligomerization. Does not reduce interaction with MIEF1 FT and MIEF2. Impairs formation of higher order oligomers but FT not homodimerization. Unable to associate with MIEF2 into FT filaments forming the tubular structures that wrap around FT the scission site. Slight reduction in GTPase activity. FT Inhibits mitochondrial fission. Retained in the cytoplasm." FT /evidence="ECO:0000269|PubMed:17553808, FT ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, FT ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:29899447, FT ECO:0000269|PubMed:32439975" FT MUTAGEN 644 FT /note="C->A: Abolishes S-nitrosylation. Reduced FT dimerization and no enhancement of GTPase activity." FT /evidence="ECO:0000269|PubMed:19342591" FT MUTAGEN 668 FT /note="K->E: Abolishes homodimerization and formation of FT higher order oligomers." FT /evidence="ECO:0000269|PubMed:23584531" FT MUTAGEN 679 FT /note="K->A: Diminishes intramolecular interaction between FT GTP-middle domain and GED domain but no effect on FT homooligomerization. Marked reduction in GTPase activity, FT in vitro. Decreased mitochondrial division." FT /evidence="ECO:0000269|PubMed:15208300" FT CONFLICT 208 FT /note="R -> C (in Ref. 2; AAC35283 and 4; AAD39541)" FT /evidence="ECO:0000305" FT HELIX 5..18 FT /evidence="ECO:0007829|PDB:3W6P" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:4H1U" FT STRAND 27..31 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 38..44 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:4H1U" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 104..119 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:4H1U" FT HELIX 162..174 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 179..186 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 195..203 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:4H1U" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 227..230 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:3W6P" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4H1V" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 249..253 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 258..272 FT /evidence="ECO:0007829|PDB:3W6P" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 282..317 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 338..355 FT /evidence="ECO:0007829|PDB:3W6P" FT HELIX 363..371 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 373..380 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 389..399 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 409..420 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 421..424 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 425..440 FT /evidence="ECO:0007829|PDB:4BEJ" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 458..493 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 643..673 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 675..690 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 693..699 FT /evidence="ECO:0007829|PDB:4BEJ" FT HELIX 704..727 FT /evidence="ECO:0007829|PDB:4BEJ" SQ SEQUENCE 736 AA; 81877 MW; F9521A376B785B71 CRC64; MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL APASQEPSPA ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL QGASQIIAEI RETHLW //