DYN3_MOUSE
ID DYN3_MOUSE Reviewed; 863 AA.
AC Q8BZ98; B2RUH0; Q3UGY9; Q80TR2; Q8BWW6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Dynamin-3;
DE EC=3.6.5.5;
GN Name=Dnm3; Synonyms=Kiaa0820;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-863 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Most
CC probably involved in vesicular trafficking processes, in particular
CC endocytosis (By similarity). {ECO:0000250}.
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 -!- INTERACTION:
CC Q8BZ98; Q7TQF7: Amph; NbExp=2; IntAct=EBI-6880033, EBI-775139;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Microtubule-associated. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZ98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZ98-2; Sequence=VSP_031548;
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; AK036199; BAC29343.1; -; mRNA.
DR EMBL; AK049724; BAC33895.1; -; mRNA.
DR EMBL; AK147678; BAE28068.1; -; mRNA.
DR EMBL; BC141143; AAI41144.1; -; mRNA.
DR EMBL; BC141144; AAI41145.1; -; mRNA.
DR EMBL; AK122379; BAC65661.1; -; Transcribed_RNA.
DR CCDS; CCDS48417.1; -. [Q8BZ98-2]
DR RefSeq; NP_001033708.1; NM_001038619.1. [Q8BZ98-1]
DR RefSeq; NP_766234.1; NM_172646.2. [Q8BZ98-2]
DR AlphaFoldDB; Q8BZ98; -.
DR SMR; Q8BZ98; -.
DR BioGRID; 222243; 12.
DR IntAct; Q8BZ98; 8.
DR MINT; Q8BZ98; -.
DR STRING; 10090.ENSMUSP00000064538; -.
DR iPTMnet; Q8BZ98; -.
DR PhosphoSitePlus; Q8BZ98; -.
DR SwissPalm; Q8BZ98; -.
DR EPD; Q8BZ98; -.
DR jPOST; Q8BZ98; -.
DR MaxQB; Q8BZ98; -.
DR PaxDb; Q8BZ98; -.
DR PeptideAtlas; Q8BZ98; -.
DR PRIDE; Q8BZ98; -.
DR ProteomicsDB; 275421; -. [Q8BZ98-1]
DR ProteomicsDB; 275422; -. [Q8BZ98-2]
DR Antibodypedia; 34382; 223 antibodies from 32 providers.
DR DNASU; 103967; -.
DR Ensembl; ENSMUST00000070330; ENSMUSP00000064538; ENSMUSG00000040265. [Q8BZ98-2]
DR GeneID; 103967; -.
DR KEGG; mmu:103967; -.
DR UCSC; uc007dga.2; mouse. [Q8BZ98-1]
DR UCSC; uc007dgb.2; mouse. [Q8BZ98-2]
DR CTD; 26052; -.
DR MGI; MGI:1341299; Dnm3.
DR VEuPathDB; HostDB:ENSMUSG00000040265; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000158056; -.
DR HOGENOM; CLU_008964_1_1_1; -.
DR InParanoid; Q8BZ98; -.
DR OMA; XVLLLID; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q8BZ98; -.
DR TreeFam; TF300362; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 103967; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dnm3; mouse.
DR PRO; PR:Q8BZ98; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BZ98; protein.
DR Bgee; ENSMUSG00000040265; Expressed in facial nucleus and 171 other tissues.
DR ExpressionAtlas; Q8BZ98; baseline and differential.
DR Genevisible; Q8BZ98; MM.
DR GO; GO:0061828; C:apical tubulobulbar complex; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0061829; C:basal tubulobulbar complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098844; C:postsynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
DR GO; GO:0099186; F:structural constituent of postsynapse; ISO:MGI.
DR GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0046847; P:filopodium assembly; ISO:MGI.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISO:MGI.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IGI:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11566; 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; SSF52540; 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 Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Endocytosis;
KW GTP-binding; Hydrolase; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..863
FT /note="Dynamin-3"
FT /id="PRO_0000319951"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 515..621
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 653..744
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 626..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ16"
FT BINDING 205..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ16"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ16"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39054"
FT MOD_RES 593
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 594
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08877"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08877"
FT VAR_SEQ 628..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031548"
FT CONFLICT 139
FT /note="G -> A (in Ref. 1; BAE28068)"
FT /evidence="ECO:0000305"
FT CONFLICT 532..549
FT /note="Missing (in Ref. 3; BAC65661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 97190 MW; 8BDBB091CB10D264 CRC64;
MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVTSKAEY AEFLHCKGKK FTDFDEVRHE IEAETDRVTG MNKGISSIPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIRDMI MQFITRENCL ILAVTPANTD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YVGVVNRSQK
DIDGKKDIKA AMLAERKFFL SHPAYRHIAD RMGTPHLQKV LNQQLTNHIR DTLPNFRNKL
QGQLLSIEHE VEAFKNFKPE DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA
KINRIFHERF PFEIVKMEFN EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL
KGPSLKSVDL VMQELINTVK KCTKRLANFP RLCEETERIV ANHIREREGK TKDQVLLLID
IQVSYINTNH EDFIGFANAQ QRSSQVHKKS TIGNQVIRKG WLTVSNIGIM KGGSKGYWFV
LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKGFMSSKH VFALFNTEQR NVYKDYRFLE
LACDSQEDVD SWKASLLRAG VYPDKSVGSN KTENDENGQA ENFSMDPQLE RQVETIRNLV
DSYMSIINKC IRDLIPKTIM HLMINNVKDF INSELLAQLY SSEDQNTLME ESAEQAQRRD
EMLRMYQALK EALAIIGDIN TATVSTPAPP PVDDSWLQHS RRSPPPSPTT QRRLTISAPL
PRPTSGRGPA PAIPSPGPHS GAPPVPFRPG PLPPFPNSSD SFGAPPQVPS RPTRAPPSVP
SRRPPPSPTR PTIIRPLESS LLD
