DNM1L_RAT
ID DNM1L_RAT Reviewed; 755 AA.
AC O35303; O35318; O35319; O35320; O35321; O35322; O35323; Q5U2W1; Q792T7;
AC Q9R234; Q9R277;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dynamin-1-like protein;
DE EC=3.6.5.5;
DE AltName: Full=Dynamin-like protein;
GN Name=Dnm1l; Synonyms=Dlp1, Drp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), PROTEIN SEQUENCE
RP OF 39-48; 62-74; 113-126; 147-160; 174-180 AND 700-710, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5), TISSUE SPECIFICITY, AND
RP INTERACTION WITH GSK3B.
RC TISSUE=Brain;
RX PubMed=10679301; DOI=10.1006/bbrc.2000.2197;
RA Chen C.-H., Hwang S.-L., Howng S.-L., Chou C.-K., Hong Y.-R.;
RT "Three rat brain alternative splicing dynamin-like protein variants:
RT interaction with the glycogen synthase kinase 3beta and action as a
RT substrate.";
RL Biochem. Biophys. Res. Commun. 268:893-898(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP PROTEIN SEQUENCE OF 39-48; 174-180; 252-260; 343-352; 379-389; 472-486 AND
RP 672-678, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP MUTAGENESIS OF LYS-38 AND ASP-231, OLIGOMERIZATION, AND FUNCTION.
RX PubMed=11553726; DOI=10.1091/mbc.12.9.2894;
RA Yoon Y., Pitts K.R., McNiven M.A.;
RT "Mammalian dynamin-like protein DLP1 tubulates membranes.";
RL Mol. Biol. Cell 12:2894-2905(2001).
RN [6]
RP SUBCELLULAR LOCATION, INDUCTION BY BEZAFIBRATE, AND FUNCTION.
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 [7]
RP FUNCTION, INTERACTION WITH FIS1, AND SUBCELLULAR LOCATION.
RX PubMed=12861026; DOI=10.1128/mcb.23.15.5409-5420.2003;
RA Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A.;
RT "The mitochondrial protein hFis1 regulates mitochondrial fission in
RT mammalian cells through an interaction with the dynamin-like protein
RT DLP1.";
RL Mol. Cell. Biol. 23:5409-5420(2003).
RN [8]
RP PHOSPHORYLATION AT SER-635, FUNCTION, AND MUTAGENESIS OF SER-71; SER-139;
RP SER-149 AND SER-635.
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 [9]
RP INTERACTION WITH BCL2L1, FUNCTION, AND MUTAGENESIS OF LYS-38.
RX PubMed=18250306; DOI=10.1073/pnas.0711647105;
RA Li H., Chen Y., Jones A.F., Sanger R.H., Collis L.P., Flannery R.,
RA McNay E.C., Yu T., Schwarzenbacher R., Bossy B., Bossy-Wetzel E.,
RA Bennett M.V., Pypaert M., Hickman J.A., Smith P.J., Hardwick J.M.,
RA Jonas E.A.;
RT "Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal
RT neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2169-2174(2008).
RN [10]
RP GLYCOSYLATION AT THR-604 AND THR-605, AND SUBCELLULAR LOCATION.
RX PubMed=22745122; DOI=10.1074/jbc.m112.390682;
RA Gawlowski T., Suarez J., Scott B., Torres-Gonzalez M., Wang H.,
RA Schwappacher R., Han X., Yates J.R. III, Hoshijima M., Dillmann W.;
RT "Modulation of dynamin-related protein 1 (DRP1) function by increased O-
RT linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac
RT myocytes.";
RL J. Biol. Chem. 287:30024-30034(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH BCL2L1; CLTA AND
RP MFF, AND SUBCELLULAR LOCATION.
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 [13]
RP PHOSPHORYLATION AT SER-656.
RX PubMed=28463107; DOI=10.7554/elife.21374;
RA Monterisi S., Lobo M.J., Livie C., Castle J.C., Weinberger M., Baillie G.,
RA Surdo N.C., Musheshe N., Stangherlin A., Gottlieb E., Maizels R.,
RA Bortolozzi M., Micaroni M., Zaccolo M.;
RT "PDE2A2 regulates mitochondria morphology and apoptotic cell death via
RT local modulation of cAMP/PKA signalling.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Functions in mitochondrial and peroxisomal division
CC (PubMed:11553726, PubMed:12499366, PubMed:12861026, PubMed:17301055,
CC PubMed:18250306). Mediates membrane fission through oligomerization
CC into membrane-associated tubular structures that wrap around the
CC scission site to constrict and sever the mitochondrial membrane through
CC a GTP hydrolysis-dependent mechanism (PubMed:11553726). The specific
CC recruitment at scission sites is mediated by membrane receptors like
CC MFF, MIEF1 and MIEF2 for mitochondrial membranes (By similarity). While
CC the recruitment by the membrane receptors is GTP-dependent, the
CC following hydrolysis of GTP induces the dissociation from the receptors
CC and allows DNM1L filaments to curl into closed rings that are probably
CC sufficient to sever a double membrane (By similarity). Acts downstream
CC of PINK1 to promote mitochondrial fission in a PRKN-dependent manner.
CC Plays an important role in mitochondrial fission during mitosis (By
CC similarity). Through its function in mitochondrial division, ensures
CC the survival of at least some types of postmitotic neurons, including
CC Purkinje cells, by suppressing oxidative damage (By similarity).
CC Required for normal brain development, including that of cerebellum (By
CC similarity). Facilitates developmentally regulated apoptosis during
CC neural tube formation (By similarity). Required for a normal rate of
CC cytochrome c release and caspase activation during apoptosis; this
CC requirement may depend upon the cell type and the physiological
CC apoptotic cues (By similarity). Required for formation of endocytic
CC vesicles (PubMed:18250306, PubMed:23792689). Proposed to regulate
CC synaptic vesicle membrane dynamics through association with BCL2L1
CC isoform Bcl-X(L) which stimulates its GTPase activity in synaptic
CC vesicles; the function may require its recruitment by MFF to clathrin-
CC containing vesicles (PubMed:18250306, PubMed:23792689). Required for
CC programmed necrosis execution (By similarity). Rhythmic control of its
CC activity following phosphorylation at Ser-656 is essential for the
CC circadian control of mitochondrial ATP production (By similarity).
CC {ECO:0000250|UniProtKB:O00429, ECO:0000250|UniProtKB:Q8K1M6,
CC ECO:0000269|PubMed:11553726, ECO:0000269|PubMed:12499366,
CC ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:17301055,
CC ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:23792689}.
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 -!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle
CC region of one molecule binding to the GED domain of another DNM1L
CC molecule. Oligomerizes in a GTP-dependent manner to form membrane-
CC associated tubules with a spiral pattern. Interacts with GSK3B and
CC MARCHF5 (PubMed:10679301). Interacts (via the GTPase and B domains)
CC with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in
CC its B domain. Interacts with PPP3CA; the interaction dephosphorylates
CC DNM1L and regulates its transition to mitochondria. Interacts with
CC BCL2L1 isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may
CC form a complex in synaptic vesicles that also contains clathrin and MFF
CC (PubMed:23792689, PubMed:18250306). Interacts with MFF; the interaction
CC is inhinited by C11orf65/MFI (By similarity). Interacts with FIS1
CC (PubMed:12861026). Interacts with MIEF2 and MIEF1; GTP-dependent this
CC regulates GTP hydrolysis and DNM1L oligomerization. Interacts with
CC PGAM5; this interaction leads to dephosphorylation at Ser-656 and
CC activation of GTPase activity and eventually to mitochondria
CC fragmentation. Interacts with RALBP1; during mitosis, recruits DNM1L to
CC the mitochondrion and mediates its activation by the mitotic kinase
CC cyclin B-CDK1 (By similarity). {ECO:0000250|UniProtKB:O00429,
CC ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:10679301,
CC ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:18250306,
CC ECO:0000269|PubMed:23792689}.
CC -!- INTERACTION:
CC O35303; P53563-1: Bcl2l1; NbExp=4; IntAct=EBI-1767447, EBI-287204;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12861026,
CC ECO:0000269|PubMed:22745122}. Golgi apparatus {ECO:0000250}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q8K1M6}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8K1M6}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Peroxisome
CC {ECO:0000269|PubMed:12499366}. Membrane, clathrin-coated pit.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000269|PubMed:23792689}. Note=Mainly cytosolic. Recruited by RALA
CC and RALBP1 to mitochondrion during mitosis. Translocated to the
CC mitochondrial membrane through O-GlcNAcylation and interaction with
CC FIS1. Colocalized with MARCHF5 at mitochondrial membrane. Localizes to
CC mitochondria at sites of division. Localizes to mitochondria following
CC necrosis induction. Recruited to the mitochondrial outer membrane by
CC interaction with MIEF1. Mitochondrial recruitment is inhibited by
CC C11orf65/MFI (By similarity). Associated with peroxisomal membranes,
CC partly recruited there by PEX11B. May also be associated with
CC endoplasmic reticulum tubules and cytoplasmic vesicles and found to be
CC perinuclear (PubMed:23792689). In some cell types, localizes to the
CC Golgi complex (By similarity). Binds to phospholipid membranes (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8K1M6,
CC ECO:0000269|PubMed:23792689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O35303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35303-2; Sequence=VSP_013697, VSP_013701;
CC Name=3; Synonyms=DLP1-37;
CC IsoId=O35303-3; Sequence=VSP_013698, VSP_013699;
CC Name=4;
CC IsoId=O35303-4; Sequence=VSP_013696;
CC Name=5; Synonyms=DLP1-11;
CC IsoId=O35303-5; Sequence=VSP_013702;
CC Name=6;
CC IsoId=O35303-6; Sequence=VSP_013700;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested (at protein level).
CC Longer isoforms are preferentially expressed in brain.
CC {ECO:0000269|PubMed:10679301, ECO:0000269|PubMed:9472031}.
CC -!- INDUCTION: By bezafibrate. {ECO:0000269|PubMed:12499366}.
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:0000250|UniProtKB:O00429}.
CC -!- PTM: Phosphorylation/dephosphorylation events on two sites near the GED
CC domain regulate mitochondrial fission (By similarity). Phosphorylation
CC on Ser-656 by CAMK1 and PKA inhibits the GTPase activity, leading to a
CC defect in mitochondrial fission promoting mitochondrial elongation (By
CC similarity). Dephosphorylated on this site by PPP3CA which promotes
CC mitochondrial fission (By similarity). Phosphorylation on Ser-635 by
CC PINK1 activates the GTPase activity and promotes mitochondrial fission
CC (By similarity). Phosphorylation on Ser-635 by CDK1 also promotes
CC mitochondrial fission (PubMed:17301055). Phosphorylated in a circadian
CC manner at Ser-656 (By similarity). {ECO:0000250|UniProtKB:O00429,
CC ECO:0000269|PubMed:17301055}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial
CC fission and causes neuronal damage. {ECO:0000250}.
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-656.
CC {ECO:0000269|PubMed:17301055}.
CC -!- PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology.
CC {ECO:0000250|UniProtKB:O00429}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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; AF019043; AAB72197.1; -; mRNA.
DR EMBL; AF020207; AAB71232.1; -; mRNA.
DR EMBL; AF020208; AAB71233.1; -; mRNA.
DR EMBL; AF020209; AAB71234.1; -; mRNA.
DR EMBL; AF020210; AAB71235.1; -; mRNA.
DR EMBL; AF020211; AAB71236.1; -; mRNA.
DR EMBL; AF020212; AAB71237.1; -; mRNA.
DR EMBL; AF020213; AAB71238.1; -; mRNA.
DR EMBL; AF107048; AAD22412.1; -; mRNA.
DR EMBL; AF132727; AAD31278.1; -; mRNA.
DR EMBL; BC085843; AAH85843.1; -; mRNA.
DR RefSeq; NP_446107.2; NM_053655.3. [O35303-2]
DR RefSeq; XP_006248785.1; XM_006248723.3. [O35303-6]
DR RefSeq; XP_008767063.1; XM_008768841.2. [O35303-1]
DR RefSeq; XP_008767064.1; XM_008768842.2. [O35303-4]
DR RefSeq; XP_008767065.1; XM_008768843.2. [O35303-5]
DR AlphaFoldDB; O35303; -.
DR SMR; O35303; -.
DR BioGRID; 250292; 6.
DR CORUM; O35303; -.
DR DIP; DIP-29699N; -.
DR ELM; O35303; -.
DR IntAct; O35303; 9.
DR MINT; O35303; -.
DR STRING; 10116.ENSRNOP00000002478; -.
DR GlyGen; O35303; 2 sites.
DR iPTMnet; O35303; -.
DR PhosphoSitePlus; O35303; -.
DR SwissPalm; O35303; -.
DR jPOST; O35303; -.
DR PaxDb; O35303; -.
DR PeptideAtlas; O35303; -.
DR PRIDE; O35303; -.
DR Ensembl; ENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813. [O35303-2]
DR Ensembl; ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813. [O35303-1]
DR Ensembl; ENSRNOT00000094355; ENSRNOP00000090570; ENSRNOG00000001813. [O35303-6]
DR Ensembl; ENSRNOT00000101129; ENSRNOP00000078603; ENSRNOG00000001813. [O35303-5]
DR GeneID; 114114; -.
DR KEGG; rno:114114; -.
DR CTD; 10059; -.
DR RGD; 620416; Dnm1l.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155504; -.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; O35303; -.
DR OMA; IMATQFQ; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; O35303; -.
DR TreeFam; TF352031; -.
DR BRENDA; 3.6.5.5; 5301.
DR Reactome; R-RNO-75153; Apoptotic execution phase.
DR PRO; PR:O35303; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001813; Expressed in cerebellum and 19 other tissues.
DR Genevisible; O35303; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0099503; C:secretory vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0051433; F:BH2 domain binding; IPI:CAFA.
DR GO; GO:0030276; F:clathrin binding; IPI:CAFA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
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; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEP:RGD.
DR GO; GO:1904579; P:cellular response to thapsigargin; IMP:RGD.
DR GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD.
DR GO; GO:0061025; P:membrane fusion; ISO:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
DR GO; GO:0090149; P:mitochondrial membrane fission; ISO:RGD.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:CAFA.
DR GO; GO:0016559; P:peroxisome fission; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:RGD.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:CAFA.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:1903578; P:regulation of ATP metabolic process; ISO:RGD.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
DR GO; GO:1900063; P:regulation of peroxisome organization; ISO:RGD.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:1905395; P:response to flavonoid; IEP:RGD.
DR GO; GO:1990910; P:response to hypobaric hypoxia; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:CAFA.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030556; DNM1L.
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; PTHR11566; 1.
DR PANTHER; PTHR11566:SF39; PTHR11566:SF39; 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; SSF52540; 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 Acetylation; Alternative splicing; Biological rhythms; Coated pit;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; 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..755
FT /note="Dynamin-1-like protein"
FT /id="PRO_0000206568"
FT DOMAIN 22..315
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 663..754
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 159..162
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 228..231
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 258..261
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 357..502
FT /note="Middle domain"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT REGION 461..704
FT /note="Interaction with GSK3B"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT REGION 515..582
FT /note="B domain"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT REGION 536..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..687
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 32..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 228..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 259..262
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 616
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K1M6"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 635
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:17301055,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 656
FT /note="Phosphoserine; by CAMK1 and PKA"
FT /evidence="ECO:0000269|PubMed:28463107"
FT MOD_RES 663
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT CARBOHYD 604
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:22745122"
FT CARBOHYD 605
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:22745122"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 627
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 84..97
FT /note="DPATWKNSRHLSKG -> GKFQSWR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9472031"
FT /id="VSP_013696"
FT VAR_SEQ 84..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9472031"
FT /id="VSP_013697"
FT VAR_SEQ 84
FT /note="D -> GKFQSWN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10679301,
FT ECO:0000303|PubMed:9472031"
FT /id="VSP_013698"
FT VAR_SEQ 546..596
FT /note="SSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRI
FT -> VASGGGGV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10679301,
FT ECO:0000303|PubMed:9472031"
FT /id="VSP_013699"
FT VAR_SEQ 546..582
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9472031"
FT /id="VSP_013700"
FT VAR_SEQ 546..571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9472031"
FT /id="VSP_013701"
FT VAR_SEQ 572..582
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10679301,
FT ECO:0000303|PubMed:9472031"
FT /id="VSP_013702"
FT MUTAGEN 38
FT /note="K->A: Defective in GTP hydrolysis. Tubulates
FT spherical liposomes. Impairs mitochondrial division.
FT Decreases the BCL2L1-mediated induction of synapse number
FT and size of synaptic vesicle clusters."
FT /evidence="ECO:0000269|PubMed:11553726,
FT ECO:0000269|PubMed:18250306"
FT MUTAGEN 71
FT /note="S->A: No effect on mitotic phosphorylation."
FT /evidence="ECO:0000269|PubMed:17301055"
FT MUTAGEN 139
FT /note="S->A: No effect on mitotic phosphorylation."
FT /evidence="ECO:0000269|PubMed:17301055"
FT MUTAGEN 149
FT /note="S->A: No effect on mitotic phosphorylation."
FT /evidence="ECO:0000269|PubMed:17301055"
FT MUTAGEN 231
FT /note="D->N: Defective in GTP-binding."
FT /evidence="ECO:0000269|PubMed:11553726"
FT MUTAGEN 635
FT /note="S->A: Abolishes mitotic phosphorylation. Reduced
FT mitotic mitochondrial fragmentation."
FT /evidence="ECO:0000269|PubMed:17301055"
FT CONFLICT 517
FT /note="A -> V (in Ref. 1; AAB71237)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="G -> V (in Ref. 2; AAD31278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 83908 MW; 0568353907794C43 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR
RPLILQLVHV SPEDKRKTTG EENDPATWKN SRHLSKGVEA EEWGKFLHTK NKLYTDFDEI
RQEIENETER ISGNNKGVSP EPIHLKVFSP NVVNLTLVDL PGMTKVPVGD QPKDIELQIR
ELILRFISNP NSIILAVTAA NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM
DVLMGRVIPV KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR
TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI TKFATEYCNT
IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL NTIDILTAIR NATGPRPALF
VPEVSFELLV KRQIKRLEEP SLRCVELVHE EMQRIIQHCS NYSTQELLRF PKLHDAIVEV
VTCLLRKRLP VTNEMVHNLV AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA
VSRDKSSKVP SALAPASQEP SPAASAEADG KLIQDNRRET KNVASAGGGI GDGGRIGDGG
QEPTTGNWRG MLKTSKAEEL LAEEKSKPIP IMPASPQKGH AVNLLDVPVP VARKLSAREQ
RDCEVIERLI KSYFLIVRKN IQDSVPKAVM HFLVNHVKDT LQSELVGQLY KSSLLDDLLT
ESEDMAQRRK EAADMLKALQ GASQIIAEIR ETHLW
