DYN3_RAT
ID DYN3_RAT Reviewed; 869 AA.
AC Q08877; Q9QXL9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dynamin-3;
DE EC=3.6.5.5;
DE AltName: Full=Dynamin, testicular;
DE AltName: Full=T-dynamin;
GN Name=Dnm3; Synonyms=Dyn3;
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 8), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8360266; DOI=10.1242/jcs.105.1.1;
RA Nakata T., Takamura R., Hirokawa N.;
RT "A novel member of the dynamin family of GTP-binding proteins is expressed
RT specifically in the testis.";
RL J. Cell Sci. 105:1-5(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=8752097; DOI=10.1046/j.1471-4159.1996.67030927.x;
RA Cook T., Mesa K., Urrutia R.;
RT "Three dynamin-encoding genes are differentially expressed in developing
RT rat brain.";
RL J. Neurochem. 67:927-931(1996).
RN [3]
RP PROTEIN SEQUENCE OF 839-859 (ISOFORM 1/3/5/7/9/11), PHOSPHORYLATION AT
RP SER-769; SER-773 AND SER-853, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 AND SER-773, 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).
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.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9725914}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9725914}. Note=Microtubule-
CC associated. Isoform-specific localization.
CC {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:9725914}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm. Golgi apparatus
CC {ECO:0000269|PubMed:9725914}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1; Synonyms=bab, DynIIIbb;
CC IsoId=Q08877-1; Sequence=Displayed;
CC Name=2; Synonyms=baa, DynIIIba;
CC IsoId=Q08877-2; Sequence=VSP_034043;
CC Name=3; Synonyms=bbb;
CC IsoId=Q08877-3; Sequence=VSP_034041;
CC Name=4; Synonyms=bba;
CC IsoId=Q08877-4; Sequence=VSP_034041, VSP_034043;
CC Name=5; Synonyms=bcb;
CC IsoId=Q08877-5; Sequence=VSP_034042;
CC Name=6; Synonyms=bca;
CC IsoId=Q08877-6; Sequence=VSP_034042, VSP_034043;
CC Name=7; Synonyms=aab, DynIIIab;
CC IsoId=Q08877-7; Sequence=VSP_034038;
CC Name=8; Synonyms=aaa, DynIIIaa;
CC IsoId=Q08877-9; Sequence=VSP_034038, VSP_034043;
CC Name=9; Synonyms=abb;
CC IsoId=Q08877-10; Sequence=VSP_034038, VSP_034041;
CC Name=10; Synonyms=aba;
CC IsoId=Q08877-11; Sequence=VSP_034038, VSP_034041, VSP_034043;
CC Name=11; Synonyms=acb;
CC IsoId=Q08877-12; Sequence=VSP_034038, VSP_034042;
CC Name=12; Synonyms=aca;
CC IsoId=Q08877-13; Sequence=VSP_034038, VSP_034042, VSP_034043;
CC Name=13; Synonyms=c;
CC IsoId=Q08877-8; Sequence=VSP_034039, VSP_034040;
CC -!- TISSUE SPECIFICITY: Isoform-specific expression in germ-cell-depleted
CC testis (Sertoli cells), brain (peripheral sensory neurons), lung and
CC heart. {ECO:0000269|PubMed:8360266, ECO:0000269|PubMed:9725914}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated expression throughout development.
CC {ECO:0000269|PubMed:8752097}.
CC -!- MISCELLANEOUS: [Isoform 1]: Expressed in lung, brain, heart.
CC -!- MISCELLANEOUS: [Isoform 2]: Expressed in lung, brain, heart, testis.
CC Localized to vesicular-like punctate spots, neither at the plasma
CC membrane nor the Golgi area. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Expressed in lung, brain, heart, testis.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Expressed in lung, brain, heart.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Expressed in lung. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Expressed in lung. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Expressed in lung, brain, heart, testis.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Expressed in lung, brain, heart, testis.
CC Diffuse cytoplasmic distribution and some modest association with the
CC Golgi apparatus. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Expressed in lung, brain, heart.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: Expressed in lung, brain, heart.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 11]: Expressed in lung. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 12]: Expressed in lung. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 13]: Expressed in lung, brain, heart, testis.
CC {ECO:0000305}.
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; D14076; BAA03161.1; -; mRNA.
DR EMBL; AF201839; AAF07848.1; -; mRNA.
DR PIR; I55498; I55498.
DR RefSeq; NP_612547.1; NM_138538.1. [Q08877-1]
DR RefSeq; XP_006250203.1; XM_006250141.3. [Q08877-7]
DR RefSeq; XP_006250204.1; XM_006250142.3. [Q08877-9]
DR AlphaFoldDB; Q08877; -.
DR SMR; Q08877; -.
DR BioGRID; 251309; 4.
DR ELM; Q08877; -.
DR IntAct; Q08877; 3.
DR MINT; Q08877; -.
DR STRING; 10116.ENSRNOP00000063767; -.
DR iPTMnet; Q08877; -.
DR PhosphoSitePlus; Q08877; -.
DR jPOST; Q08877; -.
DR PaxDb; Q08877; -.
DR PRIDE; Q08877; -.
DR Ensembl; ENSRNOT00000067653; ENSRNOP00000063767; ENSRNOG00000026490. [Q08877-1]
DR Ensembl; ENSRNOT00000075938; ENSRNOP00000068044; ENSRNOG00000026490. [Q08877-2]
DR GeneID; 171574; -.
DR KEGG; rno:171574; -.
DR UCSC; RGD:727949; rat. [Q08877-1]
DR CTD; 26052; -.
DR RGD; 727949; Dnm3.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000158056; -.
DR HOGENOM; CLU_008964_1_1_1; -.
DR InParanoid; Q08877; -.
DR OMA; XVLLLID; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q08877; -.
DR BRENDA; 3.6.5.5; 5301.
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 PRO; PR:Q08877; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000026490; Expressed in cerebellum and 16 other tissues.
DR Genevisible; Q08877; RN.
DR GO; GO:0061828; C:apical tubulobulbar complex; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0061829; C:basal tubulobulbar complex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098844; C:postsynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043083; C:synaptic cleft; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IDA:RGD.
DR GO; GO:0099186; F:structural constituent of postsynapse; IDA:SynGO.
DR GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IDA:UniProtKB.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IDA:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:RGD.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IMP:RGD.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IMP:SynGO.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0042713; P:sperm ejaculation; NAS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
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 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; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Endocytosis; Golgi apparatus;
KW GTP-binding; Hydrolase; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..869
FT /note="Dynamin-3"
FT /id="PRO_0000206574"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 525..631
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 752..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..858
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 603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 604
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17376771"
FT VAR_SEQ 516..525
FT /note="Missing (in isoform 7, isoform 8, isoform 9, isoform
FT 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:8360266"
FT /id="VSP_034038"
FT VAR_SEQ 526..564
FT /note="VIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEE -> VRAKFCDSE
FT GLADRQQHWHHERRLEGLLVCPHGRKLVLV (in isoform 13)"
FT /evidence="ECO:0000305"
FT /id="VSP_034039"
FT VAR_SEQ 565..869
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000305"
FT /id="VSP_034040"
FT VAR_SEQ 636..640
FT /note="SFTEN -> SFGSNKTEM (in isoform 3, isoform 4, isoform
FT 9 and isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_034041"
FT VAR_SEQ 636..640
FT /note="SFTEN -> DQAENEDGAQENTF (in isoform 5, isoform 6,
FT isoform 11 and isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_034042"
FT VAR_SEQ 847..869
FT /note="SRRPPPSPTRPTIIRPLESSLLD -> RFGAVKEEAVEP (in isoform
FT 2, isoform 4, isoform 6, isoform 8, isoform 10 and isoform
FT 12)"
FT /evidence="ECO:0000303|PubMed:8360266"
FT /id="VSP_034043"
SQ SEQUENCE 869 AA; 97914 MW; 00B41E41E5425BAD CRC64;
MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVTSKAEY AEFLHCKGKK FTDFDEVRHE IEAETDRVTG MNKGISSVPI
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 TIGNQGTNLP PSRQIVIRKG WLTVSNIGIM
KGGSKGYWFV LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKGFMSSKH VFALFNTEQR
NVYKDYRSLE LACDSQEDVD SWKASLLRAG VYPDKSFTEN DENGQAENFS MDPQLERQVE
TIRNLVDSYM SIINKCIRDL IPKTIMHLMI NNVKDFINSE LLAQLYSSED QNTLMEESVE
QAQRRDEMLR MYQALKEALA IIGDINTVTV STPAPPPVDD SWLQHSRRSP PPSPTTQRRL
TLSAPLPRPA SSRGPAPAIP SPGPHSGAPP VPFRPGPLPP FPNSSDSYGA PPQVPSRPTR
APPSVPSRRP PPSPTRPTII RPLESSLLD
