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Dynamin-1 (EC 3.6.5.5)

 DYN1_MOUSE              Reviewed;         867 AA.
P39053; A2AN50; A2AN51; A2AN54; A2AN55; Q3UNM1; Q5DTN7; Q61358;
Q61359; Q61360; Q6PDM5; Q8JZZ4; Q9CSY7; Q9QXX1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
20-JUN-2003, sequence version 2.
05-DEC-2018, entry version 187.
RecName: Full=Dynamin-1;
EC=3.6.5.5;
Name=Dnm1; Synonyms=Dnm, Kiaa4093;
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] (ISOFORMS 3; 4; 5 AND 6).
STRAIN=NIH Swiss; TISSUE=Brain;
PubMed=9143510; DOI=10.1006/geno.1997.4634;
Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H.,
Jockusch H.;
"Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes
2 and 9, respectively.";
Genomics 41:290-292(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
STRAIN=C57BL/6J; TISSUE=Colon, and Embryo;
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] (ISOFORM 3).
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
PubMed=11042120; DOI=10.1042/bj3510661;
Yoo J., Lee S.S., Jeong M.J., Lee K.I., Kwon B.M., Kim S.H.,
Park Y.M., Han M.Y.;
"Characterization of the mouse dynamin I gene promoter and
identification of sequences that direct expression in neuronal
cells.";
Biochem. J. 351:661-668(2000).
[7]
PROTEIN SEQUENCE OF 5-54; 67-87; 91-107; 114-188; 207-217; 230-237;
247-266; 280-290; 300-309; 328-361; 370-376; 400-414; 511-535;
563-571; 584-594; 664-675 AND 684-694.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3, AND SUBCELLULAR
LOCATION.
PubMed=11082044;
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
"All three PACSIN isoforms bind to endocytic proteins and inhibit
endocytosis.";
J. Cell Sci. 113:4511-4521(2000).
[9]
INTERACTION WITH CAV1, AND PHOSPHORYLATION.
PubMed=11956154; DOI=10.1210/endo.143.5.8814;
Kim Y.N., Bertics P.J.;
"The endocytosis-linked protein dynamin associates with caveolin-1 and
is tyrosine phosphorylated in response to the activation of a
noninternalizing epidermal growth factor receptor mutant.";
Endocrinology 143:1726-1731(2002).
[10]
INTERACTION WITH SH3GLB1.
PubMed=12456676; DOI=10.1074/jbc.M208568200;
Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
"Characterization of endophilin B1b, a brain-specific membrane-
associated lysophosphatidic acid acyl transferase with properties
distinct from endophilin A1.";
J. Biol. Chem. 278:4160-4167(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80; TYR-125 AND TYR-354,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-512,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851 AND SER-857 (ISOFORM
4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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).
[16]
INTERACTION WITH UNC119.
PubMed=19781630; DOI=10.1016/j.cellsig.2009.09.022;
Karim Z., Vepachedu R., Gorska M., Alam R.;
"UNC119 inhibits dynamin and dynamin-dependent endocytic processes.";
Cell. Signal. 22:128-137(2010).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-796, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Microtubule-associated force-producing protein involved
in producing microtubule bundles and able to bind and hydrolyze
GTP. Most probably involved in vesicular trafficking processes.
Involved in receptor-mediated endocytosis (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
-!- SUBUNIT: Binds SH3GL1, SH3GL2 and SH3GL3 (By similarity).
Interacts with SNX9 (By similarity). Interacts with PHOCN.
Interacts with MYO1E (via SH3 domain). Interacts with SNX33 (via
SH3 domain) (By similarity). Interacts with CAV1 and SH3GLB1.
Interacts with PACSIN1, PACSIN2 and PACSIN3. Interacts with
UNC119; leading to a decrease of DNM1 GTPase activity. Interacts
with DIAPH1 (By similarity). Interacts with AMPH, BIN1 AND SYNJ1
(By similarity). {ECO:0000250|UniProtKB:P21575,
ECO:0000250|UniProtKB:Q05193, ECO:0000269|PubMed:11082044,
ECO:0000269|PubMed:11956154, ECO:0000269|PubMed:12456676,
ECO:0000269|PubMed:19781630}.
-!- INTERACTION:
Q7TQF7:Amph; NbExp=3; IntAct=EBI-397785, EBI-775139;
Q5S007:LRRK2 (xeno); NbExp=3; IntAct=EBI-397785, EBI-5323863;
Q9JJV2-1:Pfn2; NbExp=2; IntAct=EBI-397785, EBI-990256;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11082044}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11082044}.
Note=Microtubule-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P39053-1; Sequence=Displayed;
Name=3; Synonyms=BraDnm8;
IsoId=P39053-3; Sequence=VSP_007643, VSP_007645;
Name=4; Synonyms=BraDnm2;
IsoId=P39053-4; Sequence=VSP_007647;
Note=Contains a phosphoserine at position 857. Contains a
phosphoserine at position 851. {ECO:0000244|PubMed:21183079};
Name=5; Synonyms=BreDnm15;
IsoId=P39053-5; Sequence=VSP_007645;
Name=6;
IsoId=P39053-6; Sequence=VSP_007644, VSP_024845;
Note=Ref.1 (AAA37324) sequence has a frameshift in position 844.
Contains a phosphoserine at position 847.
{ECO:0000244|PubMed:19131326};
-!- PTM: Phosphorylated in response to EGF stimulation in cells
expressing truncated EGFR. {ECO:0000269|PubMed:11956154}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
-!- SEQUENCE CAUTION:
Sequence=BAD90284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; L29457; AAA37319.1; -; mRNA.
EMBL; L31395; AAA37318.1; -; mRNA.
EMBL; L31396; AAA37323.1; -; mRNA.
EMBL; L31397; AAA37324.1; ALT_FRAME; mRNA.
EMBL; AK011651; BAB27759.1; -; mRNA.
EMBL; AK144142; BAE25726.1; -; mRNA.
EMBL; AK220483; BAD90284.1; ALT_INIT; mRNA.
EMBL; AL808027; CAM15852.1; -; Genomic_DNA.
EMBL; AL808027; CAM15853.1; -; Genomic_DNA.
EMBL; AL808027; CAM15855.1; -; Genomic_DNA.
EMBL; AL808027; CAM15857.1; -; Genomic_DNA.
EMBL; BC034679; AAH34679.1; -; mRNA.
EMBL; BC058623; AAH58623.1; -; mRNA.
EMBL; AF170568; AAF24220.1; -; Genomic_DNA.
CCDS; CCDS38102.1; -. [P39053-6]
CCDS; CCDS79772.1; -. [P39053-3]
RefSeq; NP_001288666.1; NM_001301737.1. [P39053-3]
RefSeq; NP_034195.2; NM_010065.3. [P39053-6]
RefSeq; XP_006497718.2; XM_006497655.2. [P39053-4]
RefSeq; XP_006497721.2; XM_006497658.3. [P39053-3]
RefSeq; XP_006497722.2; XM_006497659.3. [P39053-3]
RefSeq; XP_006497723.2; XM_006497660.2. [P39053-3]
RefSeq; XP_006497724.2; XM_006497661.2. [P39053-5]
RefSeq; XP_017170817.1; XM_017315328.1. [P39053-5]
UniGene; Mm.44736; -.
ProteinModelPortal; P39053; -.
SMR; P39053; -.
BioGrid; 199257; 34.
CORUM; P39053; -.
IntAct; P39053; 37.
MINT; P39053; -.
STRING; 10090.ENSMUSP00000088618; -.
iPTMnet; P39053; -.
PhosphoSitePlus; P39053; -.
SwissPalm; P39053; -.
MaxQB; P39053; -.
PaxDb; P39053; -.
PeptideAtlas; P39053; -.
PRIDE; P39053; -.
Ensembl; ENSMUST00000078352; ENSMUSP00000077461; ENSMUSG00000026825. [P39053-3]
Ensembl; ENSMUST00000091089; ENSMUSP00000088618; ENSMUSG00000026825. [P39053-6]
Ensembl; ENSMUST00000113350; ENSMUSP00000108977; ENSMUSG00000026825. [P39053-5]
Ensembl; ENSMUST00000113352; ENSMUSP00000108979; ENSMUSG00000026825. [P39053-5]
Ensembl; ENSMUST00000113365; ENSMUSP00000108992; ENSMUSG00000026825. [P39053-4]
Ensembl; ENSMUST00000139624; ENSMUSP00000122679; ENSMUSG00000026825. [P39053-1]
Ensembl; ENSMUST00000202578; ENSMUSP00000143955; ENSMUSG00000026825. [P39053-3]
GeneID; 13429; -.
KEGG; mmu:13429; -.
UCSC; uc008jfc.2; mouse. [P39053-6]
UCSC; uc008jfd.3; mouse. [P39053-3]
UCSC; uc029twn.1; mouse. [P39053-5]
CTD; 1759; -.
MGI; MGI:107384; Dnm1.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00940000155214; -.
HOVERGEN; HBG107833; -.
InParanoid; P39053; -.
KO; K01528; -.
OMA; KIKEPCL; -.
OrthoDB; EOG091G0EIQ; -.
PhylomeDB; P39053; -.
TreeFam; TF300362; -.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-190873; Gap junction degradation.
Reactome; R-MMU-196025; Formation of annular gap junctions.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
ChiTaRS; Dnm1; mouse.
PRO; PR:P39053; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026825; Expressed in 249 organ(s), highest expression level in prefrontal cortex.
CleanEx; MM_DNM1; -.
ExpressionAtlas; P39053; baseline and differential.
Genevisible; P39053; MM.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
GO; GO:0044327; C:dendritic spine head; IBA:GO_Central.
GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0030117; C:membrane coat; IDA:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0098844; C:postsynaptic endocytic zone membrane; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
GO; GO:0043196; C:varicosity; ISO:MGI.
GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
GO; GO:0006897; P:endocytosis; ISO:MGI.
GO; GO:0007032; P:endosome organization; ISO:MGI.
GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:MGI.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISO:MGI.
GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IBA:GO_Central.
GO; GO:0031623; P:receptor internalization; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:1904645; P:response to amyloid-beta; IEA:Ensembl.
GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IGI:SynGO.
GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
GO; GO:1901998; P:toxin transport; IMP:MGI.
CDD; cd08771; DLP_1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027741; DNM1.
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.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF32; PTHR11566:SF32; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Endocytosis; GTP-binding; Hydrolase;
Methylation; Microtubule; Motor protein; Nitration;
Nucleotide-binding; Phosphoprotein; Reference proteome.
CHAIN 1 867 Dynamin-1.
/FTId=PRO_0000206564.
DOMAIN 28 294 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 515 625 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 659 750 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 38 45 GTP. {ECO:0000250}.
NP_BIND 136 140 GTP. {ECO:0000250}.
NP_BIND 205 208 GTP. {ECO:0000250}.
REGION 38 45 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 64 66 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 136 139 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 205 208 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 235 238 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
MOD_RES 80 80 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 125 125 Nitrated tyrosine; alternate.
{ECO:0000244|PubMed:16800626}.
MOD_RES 125 125 Phosphotyrosine; alternate.
{ECO:0000244|PubMed:18034455}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 354 354 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 796 796 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
VAR_SEQ 407 444 MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK ->
LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE
(in isoform 3).
{ECO:0000303|PubMed:9143510,
ECO:0000303|Ref.3}.
/FTId=VSP_007643.
VAR_SEQ 516 519 Missing (in isoform 6).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9143510}.
/FTId=VSP_007644.
VAR_SEQ 845 867 SLGAWRLNSPQGKHENRAGKARL -> RITISDP (in
isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9143510,
ECO:0000303|Ref.3}.
/FTId=VSP_007645.
VAR_SEQ 846 867 LGAWRLNSPQGKHENRAGKARL -> RSGQASPSRPESPRP
PFDL (in isoform 4).
{ECO:0000303|PubMed:9143510}.
/FTId=VSP_007647.
VAR_SEQ 846 867 LGAWRLNSPQGKHENRAGKARL -> RKGPASPTRPAAPRP
TEAPLLDL (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024845.
CONFLICT 135 135 V -> A (in Ref. 1; AAA37318).
{ECO:0000305}.
CONFLICT 450 450 P -> R (in Ref. 1; AAA37318).
{ECO:0000305}.
CONFLICT 531 531 I -> S (in Ref. 1; AAA37318).
{ECO:0000305}.
CONFLICT 573 573 R -> H (in Ref. 2; BAE25726).
{ECO:0000305}.
CONFLICT 600 600 Y -> N (in Ref. 1; AAA37318).
{ECO:0000305}.
CONFLICT 703 703 A -> V (in Ref. 5; AAH58623).
{ECO:0000305}.
CONFLICT 722 722 A -> R (in Ref. 1; AAA37319/AAA37323/
AAA37324). {ECO:0000305}.
SEQUENCE 867 AA; 97803 MW; F48EC3DF5F39A08B CRC64;
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVNSTTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI
REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE
YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE
TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE
QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT
PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP
PGVPSLGAWR LNSPQGKHEN RAGKARL


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