ID DYN1_RAT Reviewed; 864 AA.
AC P21575;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Dynamin-1 {ECO:0000303|PubMed:16141317, ECO:0000303|PubMed:2144893};
DE EC=3.6.5.5 {ECO:0000269|PubMed:16141317};
DE AltName: Full=B-dynamin;
DE AltName: Full=D100;
DE AltName: Full=Dynamin I {ECO:0000303|PubMed:17376771};
DE AltName: Full=Dynamin, brain {ECO:0000305|PubMed:2144893};
GN Name=Dnm1; Synonyms=Dnm;
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] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=2144893; DOI=10.1038/347256a0;
RA Obar R.A., Collins C.A., Hammarback J.A., Shpetner H.S., Vallee R.B.;
RT "Molecular cloning of the microtubule-associated mechanochemical enzyme
RT dynamin reveals homology with a new family of GTP-binding proteins.";
RL Nature 347:256-261(1990).
RN [2]
RP PROTEIN SEQUENCE OF 5-15; 45-54; 67-87; 91-107; 116-157; 167-188; 257-266;
RP 300-315; 328-342; 400-415; 511-522 AND 584-594 (ISOFORM 1/2/3/4), AND
RP 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 [3]
RP PROTEIN SEQUENCE OF 343-364; 511-522 AND 797-838 (ISOFORM 1/2/4/5/6/8),
RP PROTEIN SEQUENCE OF 847-864 (ISOFORM 1/5), PHOSPHORYLATION AT SER-347;
RP SER-512; SER-774; SER-778; SER-822; SER-851 AND SER-857, IDENTIFICATION BY
RP MASS SPECTROMETRY, MUTAGENESIS OF SER-774; SER-778 AND THR-780, AND
RP INTERACTION WITH AMPH.
RX PubMed=17376771; DOI=10.1074/jbc.m609713200;
RA Graham M.E., Anggono V., Bache N., Larsen M.R., Craft G.E., Robinson P.J.;
RT "The in vivo phosphorylation sites of rat brain dynamin I.";
RL J. Biol. Chem. 282:14695-14707(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-581 (ISOFORM 5/6/7/8).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 668-864 (ISOFORM 1/5).
RC TISSUE=Brain, and Hypothalamus;
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH AMPH; BIN1; SH3GL2 AND SYNJ1.
RX PubMed=9341169; DOI=10.1074/jbc.272.43.27239;
RA Micheva K.D., Kay B.K., McPherson P.S.;
RT "Synaptojanin forms two separate complexes in the nerve terminal.
RT Interactions with endophilin and amphiphysin.";
RL J. Biol. Chem. 272:27239-27245(1997).
RN [7]
RP INTERACTION WITH SNPH.
RX PubMed=12896979; DOI=10.1074/jbc.m304851200;
RA Das S., Gerwin C., Sheng Z.H.;
RT "Syntaphilin binds to dynamin-1 and inhibits dynamin-dependent
RT endocytosis.";
RL J. Biol. Chem. 278:41221-41226(2003).
RN [8]
RP INTERACTION WITH PLCG1.
RX PubMed=15252117; DOI=10.1242/jcs.01220;
RA Choi J.H., Park J.B., Bae S.S., Yun S., Kim H.S., Hong W.P., Kim I.S.,
RA Kim J.H., Han M.Y., Ryu S.H., Patterson R.L., Snyder S.H., Suh P.G.;
RT "Phospholipase C-gamma1 is a guanine nucleotide exchange factor for
RT dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor
RT endocytosis.";
RL J. Cell Sci. 117:3785-3795(2004).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MYO1E.
RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
RA Krendel M., Osterweil E.K., Mooseker M.S.;
RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in
RT endocytosis.";
RL FEBS Lett. 581:644-650(2007).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SH3GL1; SH3GL2 AND SH3GL3.
RC TISSUE=Brain;
RX PubMed=9238017; DOI=10.1073/pnas.94.16.8569;
RA Ringstad N., Nemoto Y., De Camilli P.;
RT "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin
RT and dynamin via a Grb2-like Src homology 3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997).
RN [11]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9725914; DOI=10.1091/mbc.9.9.2595;
RA Cao H., Garcia F., McNiven M.A.;
RT "Differential distribution of dynamin isoforms in mammalian cells.";
RL Mol. Biol. Cell 9:2595-2609(1998).
RN [12]
RP INTERACTION WITH MOB4.
RX PubMed=11872741; DOI=10.1074/jbc.m108818200;
RA Baillat G., Gaillard S., Castets F., Monneron A.;
RT "Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and
RT Dynamin I.";
RL J. Biol. Chem. 277:18961-18966(2002).
RN [13]
RP PHOSPHORYLATION AT SER-774 AND SER-778 BY CDK5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12855954; DOI=10.1038/ncb1020;
RA Tan T.C., Valova V.A., Malladi C.S., Graham M.E., Berven L.A., Jupp O.J.,
RA Hansra G., McClure S.J., Sarcevic B., Boadle R.A., Larsen M.R.,
RA Cousin M.A., Robinson P.J.;
RT "Cdk5 is essential for synaptic vesicle endocytosis.";
RL Nat. Cell Biol. 5:701-710(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-851 AND SER-857, AND
RP IDENTIFICATION BY 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 [15]
RP INTERACTION WITH SYT1.
RX PubMed=25964652; DOI=10.1242/jcs.161505;
RA McAdam R.L., Varga K.T., Jiang Z., Young F.B., Blandford V.,
RA McPherson P.S., Gong L.W., Sossin W.S.;
RT "The juxtamembrane region of synaptotagmin 1 interacts with dynamin 1 and
RT regulates vesicle fission during compensatory endocytosis in endocrine
RT cells.";
RL J. Cell Sci. 128:2229-2235(2015).
RN [16] {ECO:0007744|PDB:2AKA}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-304, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-59.
RX PubMed=16141317; DOI=10.1073/pnas.0506491102;
RA Reubold T.F., Eschenburg S., Becker A., Leonard M., Schmid S.L.,
RA Vallee R.B., Kull F.J., Manstein D.J.;
RT "Crystal structure of the GTPase domain of rat dynamin 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13093-13098(2005).
RN [17] {ECO:0007744|PDB:3ZVR}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-752.
RX PubMed=21927001; DOI=10.1038/nature10441;
RA Ford M.G., Jenni S., Nunnari J.;
RT "The crystal structure of dynamin.";
RL Nature 477:561-566(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP and utilizes this energy to
CC mediate vesicle scission and participates in many forms of endocytosis,
CC such as clathrin-mediated endocytosis or synaptic vesicle endocytosis
CC as well as rapid endocytosis (RE). Associates to the membrane, through
CC lipid binding, and self-assembles into rings and stacks of
CC interconnected rings through oligomerization to form a helical polymer
CC around the vesicle membrane leading to constriction of invaginated
CC coated pits around their necks. Self-assembly of the helical polymer
CC induces membrane tubules narrowing until the polymer reaches a length
CC sufficient to trigger GTP hydrolysis. Depending on the curvature
CC imposed on the tubules, membrane detachment from the helical polymer
CC upon GTP hydrolysis can cause spontaneous hemifission followed by
CC complete fission. May play a role in regulating early stages of
CC clathrin-mediated endocytosis in non-neuronal cells through its
CC activation by dephosphorylation via the signaling downstream of EGFR
CC (By similarity). Controls vesicle size at a step before fission, during
CC formation of membrane pits, at hippocampal synapses. Controls plastic
CC adaptation of the synaptic vesicle recycling machinery to high levels
CC of activity (By similarity). Mediates rapid endocytosis (RE), a Ca(2+)-
CC dependent and clathrin- and K(+)-independent process in chromaffin
CC cells. Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP (By
CC similarity). Through its interaction with DNAJC6, acts during the early
CC steps of clathrin-coated vesicle (CCV) formation (By similarity).
CC {ECO:0000250|UniProtKB:P39053, ECO:0000250|UniProtKB:Q05193,
CC ECO:0000250|UniProtKB:Q08DF4}.
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:16141317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:16141317};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for GTP (for basal GTPase activity)
CC {ECO:0000269|PubMed:16141317};
CC KM=30 uM for GTP (for assembly-stimulated GTPase activity)
CC {ECO:0000269|PubMed:16141317};
CC -!- SUBUNIT: Homodimer; homodimerization is mediated by the dynamin-type G
CC domain which promotes assembly-stimulated GTPase activity. Homo-
CC tetramer formed from two dimers in the absence of lipid. Oligomerizes
CC into a helical polymer that self-assembles around the vesicle membrane,
CC when associated to the menbrane through lipid binding. Interacts (via
CC C-terminal proline-rich domain (PRD)) with SNX9 (via SH3 domain); this
CC interaction allows regulation of DNM1 self-assembly during late stages
CC of endocytic vesicle formation and supports DNM1's early functions in
CC accelerating clathrin-coated pits (CCPs) maturation in non neuronals
CC cell. Interacts (via C-terminal proline-rich domain (PRD)) with MYO1E
CC (via SH3 domain); this interaction regulates receptor-mediated
CC endocytosis. Interacts with SNX33 (via SH3 domain); this interaction
CC decreases DNM1-dependent endocytosis. Interacts with DIAPH1. Interacts
CC with GRB2 (via SH3 domain); this interaction mediates disassembly of
CC DNM1 polymers, therefore modulates self-assembly (By similarity). Forms
CC a complex with BIN1 (via SH3 domain) and SH3GL2 (via SH3 domain)
CC (PubMed:9341169). Forms a complex with SH3GL2 (via SH3 domain) and AMPH
CC (via SH3 domain) (PubMed:9341169). Forms a complex with SH3GL2 (via SH3
CC domain) and SYNJ1 (PubMed:9341169). Interacts with AMPH
CC (PubMed:17376771). Interacts (via C-terminal proline-rich domain (PRD))
CC with SYT1; this interaction facilitates vesicle fission during
CC clathrin-mediated endocytosis (CME) (PubMed:25964652). Interacts (via
CC C-terminal proline-rich domain (PRD)) with PLCG1 (via SH3 domain); this
CC interaction stimulates the release of GDP from DNM1 and enhances DNM1-
CC dependent endocytosis (PubMed:15252117). Interacts with SNPH; this
CC interaction inhibits the binding of DNM1 to AMPH and DNM1-receptor-
CC mediated endocytosis (PubMed:12896979). Interacts with CAV1. Interacts
CC with SH3GLB1 (via SH3 domain). Interacts with PACSIN1 (via SH3 domain),
CC PACSIN2 (via SH3 domain) and PACSIN3 (via SH3 domain). Interacts with
CC UNC119; this interaction decreases DNM1's GTPase activity and affects
CC DNM1's interaction with AMPH (By similarity). Interacts (GTP-bound
CC form) with DNAJC6; this interaction allows clathrin-coated vesicle
CC (CCV) formation at the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P39053, ECO:0000250|UniProtKB:Q05193,
CC ECO:0000269|PubMed:12896979, ECO:0000269|PubMed:15252117,
CC ECO:0000269|PubMed:17376771, ECO:0000269|PubMed:25964652,
CC ECO:0000269|PubMed:9341169}.
CC -!- INTERACTION:
CC P21575; O08838: Amph; NbExp=3; IntAct=EBI-80070, EBI-80080;
CC P21575; O08839: Bin1; NbExp=2; IntAct=EBI-80070, EBI-80095;
CC P21575; P21575: Dnm1; NbExp=7; IntAct=EBI-80070, EBI-80070;
CC P21575; P62994: Grb2; NbExp=3; IntAct=EBI-80070, EBI-401775;
CC P21575; Q9Z0W5: Pacsin1; NbExp=4; IntAct=EBI-80070, EBI-1550185;
CC P21575; Q63787: Pik3r1; NbExp=2; IntAct=EBI-80070, EBI-518443;
CC P21575; O35179: Sh3gl2; NbExp=6; IntAct=EBI-80070, EBI-1149197;
CC P21575; O35180: Sh3gl3; NbExp=2; IntAct=EBI-80070, EBI-1149266;
CC P21575; Q9WV48: Shank1; NbExp=2; IntAct=EBI-80070, EBI-80909;
CC P21575; Q6IN36: Wipf1; NbExp=2; IntAct=EBI-80070, EBI-6986245;
CC P21575; Q6XZF7: DNMBP; Xeno; NbExp=3; IntAct=EBI-80070, EBI-2483419;
CC P21575; Q12965: MYO1E; Xeno; NbExp=2; IntAct=EBI-80070, EBI-4279548;
CC P21575; Q5TCZ1-2; Xeno; NbExp=2; IntAct=EBI-80070, EBI-7014859;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:9725914}. Note=Strongly associated with
CC clathrin-coated vesicles at the plasma membrane.
CC {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Golgi apparatus
CC {ECO:0000269|PubMed:9725914}. Note=Diffuse cytoplasmic distribution.
CC {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05193}.
CC Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q05193}.
CC Cytoplasmic vesicle {ECO:0000305|PubMed:17257598}. Presynapse
CC {ECO:0000269|PubMed:9238017}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule {ECO:0000250|UniProtKB:Q08DF4}. Note=Associated to
CC the membrane in an helical polymer shape in a GTP bound state.
CC Transiently recruited to endocytic clathrin-coated pits (CCPs) at a
CC late stage of clathrin-coated vesicle (CCV) formation.
CC {ECO:0000250|UniProtKB:Q05193}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=aa {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-1; Sequence=Displayed;
CC Name=2; Synonyms=ab {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-2; Sequence=VSP_034037;
CC Name=3; Synonyms=ac {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-3; Sequence=VSP_034034, VSP_034035;
CC Name=4; Synonyms=ad {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-4; Sequence=VSP_034036;
CC Name=5; Synonyms=ba {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-5; Sequence=VSP_034033;
CC Name=6; Synonyms=bb {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-6; Sequence=VSP_034033, VSP_034037;
CC Name=7; Synonyms=bc {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-7; Sequence=VSP_034033, VSP_034034, VSP_034035;
CC Name=8; Synonyms=bd {ECO:0000303|PubMed:9725914};
CC IsoId=P21575-8; Sequence=VSP_034033, VSP_034036;
CC -!- TISSUE SPECIFICITY: Brain-specific (peripheral sensory neurons).
CC {ECO:0000269|PubMed:9725914}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neurons after maturation.
CC -!- DOMAIN: The dynamin-type G mediates homodimerization and plays a role
CC in self-assembly. {ECO:0000250|UniProtKB:Q05193}.
CC -!- DOMAIN: The C-terminal proline-rich domain (PRD) mediates interaction
CC with SH3-binding partners (PubMed:9341169). Is required for DNM1 self-
CC assembly (By similarity). {ECO:0000250|UniProtKB:Q05193,
CC ECO:0000269|PubMed:9341169}.
CC -!- DOMAIN: The PH domain binds phosphoinositides such as 1-phosphatidyl-
CC 1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-
CC bisphosphate and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate,
CC and mediates receptor-mediated endocytosis.
CC {ECO:0000250|UniProtKB:Q05193}.
CC -!- PTM: Phosphorylation at Ser-774 by GSK3B/GSK3-beta leads to
CC inactivation of receptor-mediated endocytosis in non-neuronal cells.
CC Dephosphorylation at Ser-774, through the EGFR downstream signaling,
CC leads to activation and regulates early stages of clathrin-mediated
CC endocytosis (CME) (By similarity). Phosphorylated by CDK5 leading to
CC synaptic vesicle endocytosis (SVE) activation (PubMed:12855954).
CC {ECO:0000250|UniProtKB:Q05193, ECO:0000269|PubMed:12855954}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- CAUTION: Absence of tyrosine and threonine phosphorylation is
CC demonstrated in PubMed:17376771. However, tyrosine and threonine
CC phosphorylation may still occur in different experimental conditions.
CC {ECO:0000305}.
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DR EMBL; X54531; CAA38397.1; -; mRNA.
DR EMBL; CO398357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB583951; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB708564; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S11508; S11508.
DR RefSeq; NP_542420.1; NM_080689.4. [P21575-2]
DR PDB; 2AKA; X-ray; 1.90 A; B=6-304.
DR PDB; 3ZVR; X-ray; 3.10 A; A=1-752.
DR PDBsum; 2AKA; -.
DR PDBsum; 3ZVR; -.
DR AlphaFoldDB; P21575; -.
DR BMRB; P21575; -.
DR SMR; P21575; -.
DR BioGRID; 250837; 31.
DR CORUM; P21575; -.
DR DIP; DIP-30978N; -.
DR IntAct; P21575; 22.
DR MINT; P21575; -.
DR STRING; 10116.ENSRNOP00000041582; -.
DR BindingDB; P21575; -.
DR ChEMBL; CHEMBL1075191; -.
DR GlyGen; P21575; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P21575; -.
DR PhosphoSitePlus; P21575; -.
DR World-2DPAGE; 0004:P21575; -.
DR jPOST; P21575; -.
DR PaxDb; 10116-ENSRNOP00000047444; -.
DR Ensembl; ENSRNOT00000064039.5; ENSRNOP00000060845.3; ENSRNOG00000033835.7. [P21575-2]
DR Ensembl; ENSRNOT00000102787.1; ENSRNOP00000091634.1; ENSRNOG00000033835.7. [P21575-6]
DR GeneID; 140694; -.
DR KEGG; rno:140694; -.
DR UCSC; RGD:71096; rat. [P21575-1]
DR AGR; RGD:71096; -.
DR CTD; 1759; -.
DR RGD; 71096; Dnm1.
DR VEuPathDB; HostDB:ENSRNOG00000033835; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR HOGENOM; CLU_008964_1_0_1; -.
DR InParanoid; P21575; -.
DR OrthoDB; 1052588at2759; -.
DR PhylomeDB; P21575; -.
DR BRENDA; 3.6.5.5; 5301.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; P21575; -.
DR PRO; PR:P21575; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000033835; Expressed in Ammon's horn and 20 other cell types or tissues.
DR Genevisible; P21575; RN.
DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030117; C:membrane coat; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0099049; P:clathrin coat assembly involved in endocytosis; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IMP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IMP:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0097494; P:regulation of vesicle size; ISS:UniProtKB.
DR GO; GO:1904645; P:response to amyloid-beta; IEP:RGD.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0099050; P:vesicle scission; ISS:UniProtKB.
DR CDD; cd08771; DLP_1; 1.
DR CDD; cd01256; PH_dynamin; 1.
DR DisProt; DP02617; -.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF32; DYNAMIN-1; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coated pit; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis;
KW Golgi apparatus; GTP-binding; Hydrolase; Membrane; Methylation;
KW Microtubule; Motor protein; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..864
FT /note="Dynamin-1"
FT /id="PRO_0000206565"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 519..625
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 659..750
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 64..66
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 136..139
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 205..208
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 235..238
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 767..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 43
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 44
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 45
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 46
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 59
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 60
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 206
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 208
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 211
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 236
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 237
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT BINDING 239
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q05193"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 125
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 774
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:12855954,
FT ECO:0000269|PubMed:17376771"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12855954,
FT ECO:0000269|PubMed:17376771"
FT MOD_RES 796
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P39053"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT VAR_SEQ 407..444
FT /note="LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE -> MAFETIVKKQ
FT VKKIREPCLKCVDMVISELISTVRQCTK (in isoform 5, isoform 6,
FT isoform 7 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_034033"
FT VAR_SEQ 766..814
FT /note="QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPP ->
FT AHVQPHAAAPSPRRAPSPARVAGPCSWASACWIRPGGGSPRALQAGGFP (in
FT isoform 3 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_034034"
FT VAR_SEQ 815..864
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_034035"
FT VAR_SEQ 845..864
FT /note="SRSGQASPSRPESPRPPFDL -> RITISDP (in isoform 2 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:2144893"
FT /id="VSP_034037"
FT VAR_SEQ 845..864
FT /note="SRSGQASPSRPESPRPPFDL -> SQPIGSGKSVPS (in isoform 4
FT and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_034036"
FT MUTAGEN 59
FT /note="R->A: Decreases of 32% the basal GTPase activity.
FT Decreases of 44% the assembly-stimulated GTPase activity."
FT /evidence="ECO:0000269|PubMed:16141317"
FT MUTAGEN 59
FT /note="R->K: Decreases of 67% the basal GTPase activity.
FT Decreases of 80% the assembly-stimulated GTPase activity."
FT /evidence="ECO:0000269|PubMed:16141317"
FT MUTAGEN 774
FT /note="S->A: Does not affect phosphorylation by CDK5.
FT Significantly reduces phosphorylation by CDK5; when
FT associated with A-778 and A-780."
FT /evidence="ECO:0000269|PubMed:17376771"
FT MUTAGEN 778
FT /note="S->A: Does not affect phosphorylation by CDK5.
FT Significantly reduces phosphorylation by CDK5; when
FT associated with A-774 and A-780."
FT /evidence="ECO:0000269|PubMed:17376771"
FT MUTAGEN 780
FT /note="T->A: Does not affect phosphorylation by CDK5.
FT Significantly reduces phosphorylation by CDK5; when
FT associated with A-774 and A-778."
FT /evidence="ECO:0000269|PubMed:17376771"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2AKA"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:2AKA"
FT HELIX 274..303
FT /evidence="ECO:0007829|PDB:2AKA"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 326..344
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 404..418
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 421..442
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 450..483
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 520..531
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 540..555
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:3ZVR"
FT STRAND 600..609
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 610..622
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 654..688
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 690..699
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 701..707
FT /evidence="ECO:0007829|PDB:3ZVR"
FT TURN 711..715
FT /evidence="ECO:0007829|PDB:3ZVR"
FT HELIX 719..742
FT /evidence="ECO:0007829|PDB:3ZVR"
SQ SEQUENCE 864 AA; 97295 MW; 02EC9B533CC2EC83 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 GLFTPDLAFE ATVKKQVQKL
KEPSIKCVDM VVSELTSTIR KCSEKLQQYP 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
PGVPSRSGQA SPSRPESPRP PFDL
//
