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Dynamin-1-like protein (EC 3.6.5.5) (Dynamin family member proline-rich carboxyl-terminal domain less) (Dymple) (Dynamin-related protein 1)

 DNM1L_MOUSE             Reviewed;         742 AA.
Q8K1M6; Q8BNQ5; Q8BQ64; Q8CGD0; Q8K1A1;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
20-JUN-2018, entry version 148.
RecName: Full=Dynamin-1-like protein;
EC=3.6.5.5;
AltName: Full=Dynamin family member proline-rich carboxyl-terminal domain less;
Short=Dymple;
AltName: Full=Dynamin-related protein 1;
Name=Dnm1l; Synonyms=Drp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Osteoclast;
PubMed=14592431; DOI=10.1016/j.bbrc.2003.10.008;
Honda S., Hirose S.;
"Stage-specific enhanced expression of mitochondrial fusion and
fission factors during spermatogenesis in rat testis.";
Biochem. Biophys. Res. Commun. 311:424-432(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain, Mammary gland, and Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-659 (ISOFORM 1).
PubMed=11544199; DOI=10.1101/gr.185501;
Piao Y., Ko N.T., Lim M.K., Ko M.S.H.;
"Construction of long-transcript enriched cDNA libraries from
submicrogram amounts of total RNAs by a universal PCR amplification
method.";
Genome Res. 11:1553-1558(2001).
[5]
PROTEIN SEQUENCE OF 626-640 AND 725-737, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
TISSUE SPECIFICITY.
PubMed=9422767; DOI=10.1074/jbc.273.2.1044;
Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.;
"Dymple, a novel dynamin-like high molecular weight GTPase lacking a
proline-rich carboxyl-terminal domain in mammalian cells.";
J. Biol. Chem. 273:1044-1051(1998).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT IN PURKINJE
CELLS.
PubMed=19752021; DOI=10.1083/jcb.200903065;
Wakabayashi J., Zhang Z., Wakabayashi N., Tamura Y., Fukaya M.,
Kensler T.W., Iijima M., Sesaki H.;
"The dynamin-related GTPase Drp1 is required for embryonic and brain
development in mice.";
J. Cell Biol. 186:805-816(2009).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19578372; DOI=10.1038/ncb1907;
Ishihara N., Nomura M., Jofuku A., Kato H., Suzuki S.O., Masuda K.,
Otera H., Nakanishi Y., Nonaka I., Goto Y., Taguchi N., Morinaga H.,
Maeda M., Takayanagi R., Yokota S., Mihara K.;
"Mitochondrial fission factor Drp1 is essential for embryonic
development and synapse formation in mice.";
Nat. Cell Biol. 11:958-966(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT IN PURKINJE
CELLS.
PubMed=22564413; DOI=10.1083/jcb.201110034;
Kageyama Y., Zhang Z., Roda R., Fukaya M., Wakabayashi J.,
Wakabayashi N., Kensler T.W., Reddy P.H., Iijima M., Sesaki H.;
"Mitochondrial division ensures the survival of postmitotic neurons by
suppressing oxidative damage.";
J. Cell Biol. 197:535-551(2012).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23283981; DOI=10.1091/mbc.E12-10-0721;
Loson O.C., Song Z., Chen H., Chan D.C.;
"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
fission.";
Mol. Biol. Cell 24:659-667(2013).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, CATALYTIC
ACTIVITY, AND INTERACTION WITH MIEF1.
PubMed=24508339; DOI=10.1016/j.str.2014.01.001;
Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O.,
Chan D.C.;
"The mitochondrial fission receptor Mid51 requires ADP as a
cofactor.";
Structure 22:367-377(2014).
-!- FUNCTION: Functions in mitochondrial and peroxisomal division.
Mediates membrane fission through oligomerization into membrane-
associated tubular structures that wrap around the scission site
to constrict and sever the mitochondrial membrane through a GTP
hydrolysis-dependent mechanism. Through its function in
mitochondrial division, ensures the survival of at least some
types of postmitotic neurons, including Purkinje cells, by
suppressing oxidative damage. Required for normal brain
development, including that of cerebellum. Facilitates
developmentally regulated apoptosis during neural tube formation.
Required for a normal rate of cytochrome c release and caspase
activation during apoptosis; this requirement may depend upon the
cell type and the physiological apoptotic cues. Plays an important
role in mitochondrial fission during mitosis. Required for
formation of endocytic vesicles. Proposed to regulate synaptic
vesicle membrane dynamics through association with BCL2L1 isoform
Bcl-X(L) which stimulates its GTPase activity in synaptic
vesicles; the function may require its recruitment by MFF to
clathrin-containing vesicles. Required for programmed necrosis
execution. {ECO:0000269|PubMed:19578372,
ECO:0000269|PubMed:19752021, ECO:0000269|PubMed:22564413,
ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
{ECO:0000269|PubMed:24508339}.
-!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle
region of one molecule binding to the GED domain of another DNM1L
molecule. Oligomerizes in a GTP-dependent manner to form membrane-
associated tubules with a spiral pattern. Can also oligomerize to
form multimeric ring-like structures. Interacts with GSK3B and
MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the
interaction promotes sumoylation of DNM1L, mainly in its B domain.
Interacts with PPP3CA; the interaction dephosphorylates DNM1L and
regulates its transition to mitochondria. Interacts with BCL2L1
isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may
form a complex in synaptic vesicles that also contains clathrin
and MFF. Interacts with FIS1. Interacts with MIEF2. Interacts with
PGAM5; this interaction leads to dephosphorylation at Ser-656 and
activation of GTPase activity and eventually to mitochondria
fragmentation (By similarity). Interacts with MIEF1; this
regulates GTP hydrolysis and DNM1L oligomerization
(PubMed:24508339). {ECO:0000250|UniProtKB:O00429,
ECO:0000269|PubMed:24508339}.
-!- INTERACTION:
Q5S006:Lrrk2; NbExp=4; IntAct=EBI-2365792, EBI-2693710;
Q8BGV8:Mief1; NbExp=5; IntAct=EBI-16092613, EBI-16092561;
Q5NCS9:Mief2; NbExp=2; IntAct=EBI-16092613, EBI-16092669;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus
{ECO:0000250}. Endomembrane system; Peripheral membrane protein.
Mitochondrion outer membrane; Peripheral membrane protein.
Peroxisome {ECO:0000250}. Membrane, clathrin-coated pit
{ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic
vesicle membrane {ECO:0000250}. Note=Mainly cytosolic.
Translocated to the mitochondrial membrane through O-GlcNAcylation
and interaction with FIS1. Colocalized with MARCH5 at
mitochondrial membrane. Localizes to mitochondria at sites of
division. Localizes to mitochondria following necrosis induction.
Associated with peroxisomal membranes, partly recruited there by
PEX11B. May also be associated with endoplasmic reticulum tubules
and cytoplasmic vesicles and found to be perinuclear. In some cell
types, localizes to the Golgi complex (By similarity). Recruited
to the mitochondrial outer membrane by interaction with MIEF1.
Binds to phospholipid membranes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8K1M6-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q8K1M6-2; Sequence=VSP_013695;
Name=3;
IsoId=Q8K1M6-3; Sequence=VSP_013690, VSP_013694;
Name=4;
IsoId=Q8K1M6-4; Sequence=VSP_013689, VSP_013691, VSP_013695;
Name=5;
IsoId=Q8K1M6-5; Sequence=VSP_013690, VSP_013692, VSP_013693;
-!- TISSUE SPECIFICITY: Expressed in the cerebellum and in several
regions of the cerebrum and diencephalon. Strongly expressed in
the cerebellar Purkinje cells and in the pontile giant neurons.
{ECO:0000269|PubMed:9422767}.
-!- DOMAIN: The GED domain folds back to interact, in cis, with the
GTP-binding domain and middle domain, and interacts, in trans,
with the GED domains of other DNM1L molecules, and is thus
critical for activating GTPase activity and for DNM1L
dimerization. {ECO:0000250}.
-!- PTM: Phosphorylation/dephosphorylation events on two sites near
the GED domain regulate mitochondrial fission. Phosphorylation on
Ser-643 inhibits mitochondrial fission probably through preventing
intramolecular interaction. Dephosphorylated on this site by
PPP3CA which promotes mitochondrial fission. Phosphorylation on
Ser-622 also promotes mitochondrial fission (By similarity).
{ECO:0000250}.
-!- PTM: Sumoylated on various lysine residues within the B domain,
probably by MUL1. Sumoylation positively regulates mitochondrial
fission. Desumoylated by SENP5 during G2/M transition of mitosis.
Appears to be linked to its catalytic activity (By similarity).
{ECO:0000250}.
-!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial
fission and causes neuronal damage. {ECO:0000250}.
-!- PTM: O-GlcNAcylation augments the level of the GTP-bound active
form of DRP1 and induces translocation from the cytoplasm to
mitochondria in cardiomyocytes. It also decreases phosphorylation
at Ser-643 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mutant mice show severe developmental
abnormalities and die between 10.5 and 12.5 dpc. Compared to wild-
type littermates, mutant embryos at 9.5-11.5 dpc have a
significantly smaller body size, pulsing, but less developed
cardiac structures, a poorly developed liver and a thinner neural
tube cell layer. They lack trophoblastic giant cell layer in the
placenta. Primary cultures of mutant neuronal cells have severe
defects in synapse formation and high sensitivity to Ca(2+)-
dependent apoptosis. Within cerebellar neurons, Purkinje cells are
particularly sensitive to Dnm1l ablation. Conditional knockout in
postmitotic Purkinje cells leads to 40% neuronal degeneration
after 3 months and 90% after 6 months.
{ECO:0000269|PubMed:19578372, ECO:0000269|PubMed:19752021,
ECO:0000269|PubMed:22564413}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
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EMBL; AB079133; BAC06576.1; -; mRNA.
EMBL; AK051443; BAC34640.1; -; mRNA.
EMBL; AK080871; BAC38054.1; -; mRNA.
EMBL; BC027538; AAH27538.1; -; mRNA.
EMBL; BC040777; AAH40777.1; -; mRNA.
EMBL; BC079635; AAH79635.1; -; mRNA.
EMBL; CF914619; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS27984.1; -. [Q8K1M6-3]
CCDS; CCDS70689.1; -. [Q8K1M6-2]
RefSeq; NP_001021118.1; NM_001025947.2. [Q8K1M6-3]
RefSeq; NP_001263269.1; NM_001276340.1. [Q8K1M6-2]
RefSeq; NP_001263270.1; NM_001276341.1. [Q8K1M6-4]
RefSeq; NP_690029.2; NM_152816.3.
RefSeq; XP_006522694.1; XM_006522631.3. [Q8K1M6-1]
UniGene; Mm.218820; -.
ProteinModelPortal; Q8K1M6; -.
SMR; Q8K1M6; -.
BioGrid; 216417; 9.
CORUM; Q8K1M6; -.
DIP; DIP-54818N; -.
IntAct; Q8K1M6; 10.
MINT; Q8K1M6; -.
ChEMBL; CHEMBL2331072; -.
iPTMnet; Q8K1M6; -.
PhosphoSitePlus; Q8K1M6; -.
SwissPalm; Q8K1M6; -.
PeptideAtlas; Q8K1M6; -.
PRIDE; Q8K1M6; -.
Ensembl; ENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789. [Q8K1M6-3]
Ensembl; ENSMUST00000230022; ENSMUSP00000155429; ENSMUSG00000022789. [Q8K1M6-4]
Ensembl; ENSMUST00000230038; ENSMUSP00000155605; ENSMUSG00000022789. [Q8K1M6-5]
Ensembl; ENSMUST00000230980; ENSMUSP00000155155; ENSMUSG00000022789. [Q8K1M6-2]
GeneID; 74006; -.
KEGG; mmu:74006; -.
UCSC; uc007yij.2; mouse. [Q8K1M6-1]
UCSC; uc007yik.2; mouse. [Q8K1M6-4]
UCSC; uc007yim.2; mouse. [Q8K1M6-3]
UCSC; uc007yin.2; mouse. [Q8K1M6-2]
UCSC; uc007yio.2; mouse. [Q8K1M6-5]
CTD; 10059; -.
MGI; MGI:1921256; Dnm1l.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161068; -.
HOVERGEN; HBG107833; -.
InParanoid; Q8K1M6; -.
KO; K17065; -.
OMA; HHIPNRR; -.
OrthoDB; EOG091G02TQ; -.
PhylomeDB; Q8K1M6; -.
TreeFam; TF352031; -.
Reactome; R-MMU-75153; Apoptotic execution phase.
PRO; PR:Q8K1M6; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022789; -.
CleanEx; MM_DNM1L; -.
ExpressionAtlas; Q8K1M6; baseline and differential.
Genevisible; Q8K1M6; MM.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IMP:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0099503; C:secretory vesicle; ISO:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051433; F:BH2 domain binding; ISO:MGI.
GO; GO:0030276; F:clathrin binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:1904579; P:cellular response to thapsigargin; ISO:MGI.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060047; P:heart contraction; IMP:ParkinsonsUK-UCL.
GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
GO; GO:0061025; P:membrane fusion; ISO:MGI.
GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
GO; GO:0090149; P:mitochondrial membrane fission; ISO:MGI.
GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
GO; GO:0070266; P:necroptotic process; IMP:UniProtKB.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISO:MGI.
GO; GO:0016559; P:peroxisome fission; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISO:MGI.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0070585; P:protein localization to mitochondrion; IMP:MGI.
GO; GO:1903578; P:regulation of ATP metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:MGI.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1900063; P:regulation of peroxisome organization; IMP:ParkinsonsUK-UCL.
GO; GO:0032459; P:regulation of protein oligomerization; ISO:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0036466; P:synaptic vesicle recycling via endosome; ISO:MGI.
CDD; cd08771; DLP_1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR030556; DNM1L.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH-like_dom_sf.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF39; PTHR11566:SF39; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Coated pit;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Endocytosis; Glycoprotein; Golgi apparatus;
GTP-binding; Hydrolase; Isopeptide bond; Lipid-binding; Membrane;
Mitochondrion; Mitochondrion outer membrane; Necrosis;
Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
S-nitrosylation; Synapse; Ubl conjugation.
CHAIN 1 742 Dynamin-1-like protein.
/FTId=PRO_0000206567.
DOMAIN 22 308 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 650 741 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 32 40 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 221 227 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 252 255 GTP. {ECO:0000250|UniProtKB:O00429}.
REGION 1 349 N-terminal dimerization domain.
{ECO:0000250}.
REGION 32 39 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 58 60 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 152 155 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 221 224 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 251 254 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 350 495 Middle domain. {ECO:0000250}.
REGION 454 691 Interaction with GSK3B. {ECO:0000250}.
REGION 454 654 Interaction with GSK3B. {ECO:0000250}.
REGION 508 575 B domain. {ECO:0000250}.
REGION 548 742 C-terminal dimerization domain.
{ECO:0000250}.
REGION 660 674 Important for homodimerization.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 603 603 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 643 643 Phosphoserine; by CAMK1 and PKA.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 650 650 S-nitrosocysteine.
{ECO:0000250|UniProtKB:O00429}.
CARBOHYD 591 591 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 592 592 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 541 541 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 564 564 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 574 574 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 600 600 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 603 603 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 612 612 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 614 614 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 104 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013689.
VAR_SEQ 85 90 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_013690.
VAR_SEQ 105 105 K -> M (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013691.
VAR_SEQ 214 227 RRTLAVITKLDLMD -> KGRCLYLMDVDLQW (in
isoform 5). {ECO:0000305}.
/FTId=VSP_013692.
VAR_SEQ 228 742 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_013693.
VAR_SEQ 539 575 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_013694.
VAR_SEQ 539 564 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14592431,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_013695.
MUTAGEN 59 59 T->A: Abolishes GTP hydrolysis.
{ECO:0000269|PubMed:24508339}.
CONFLICT 165 165 P -> L (in Ref. 1; BAC06576).
{ECO:0000305}.
CONFLICT 320 320 Q -> R (in Ref. 1; BAC06576).
{ECO:0000305}.
CONFLICT 519 519 E -> A (in Ref. 2; BAC34640).
{ECO:0000305}.
SEQUENCE 742 AA; 82658 MW; 5A8679B61A444847 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR
RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL HTKNKLYTDF DEIRQEIENE
TERISGNNKG VSPEPIHLKV FSPNVVNLTL VDLPGMTKVP VGDQPKDIEL QIRELILRFI
SNPNSIILAV TAANTDMATS EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV
IPVKLGIIGV VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM
HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY CNTIEGTAKY
IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT AIRNATGPRP ALFVPEVSFE
LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK
RLPVTNEMVH NLVAIELAYI NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS
KVPSALAPAS QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK
TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC EVIERLIKSY
FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS LLDDLLTESE DMAQRRKEAA
DMLKALQGAS QIIAEIRETH LW


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