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Dynamin-3 (EC 3.6.5.5) (Dynamin, testicular) (T-dynamin)

 DYN3_RAT                Reviewed;         869 AA.
Q08877; Q9QXL9;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 2.
28-MAR-2018, entry version 152.
RecName: Full=Dynamin-3;
EC=3.6.5.5;
AltName: Full=Dynamin, testicular;
AltName: Full=T-dynamin;
Name=Dnm3; Synonyms=Dyn3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=8360266;
Nakata T., Takamura R., Hirokawa N.;
"A novel member of the dynamin family of GTP-binding proteins is
expressed specifically in the testis.";
J. Cell Sci. 105:1-5(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
TISSUE=Brain;
PubMed=8752097;
Cook T., Mesa K., Urrutia R.;
"Three dynamin-encoding genes are differentially expressed in
developing rat brain.";
J. Neurochem. 67:927-931(1996).
[3]
PROTEIN SEQUENCE OF 839-859 (ISOFORM 1/3/5/7/9/11), PHOSPHORYLATION AT
SER-769; SER-773 AND SER-853, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17376771; DOI=10.1074/jbc.M609713200;
Graham M.E., Anggono V., Bache N., Larsen M.R., Craft G.E.,
Robinson P.J.;
"The in vivo phosphorylation sites of rat brain dynamin I.";
J. Biol. Chem. 282:14695-14707(2007).
[4]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9725914; DOI=10.1091/mbc.9.9.2595;
Cao H., Garcia F., McNiven M.A.;
"Differential distribution of dynamin isoforms in mammalian cells.";
Mol. Biol. Cell 9:2595-2609(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 AND SER-773, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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, in
particular endocytosis.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9725914}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9725914}.
Note=Microtubule-associated. Isoform-specific localization.
{ECO:0000269|PubMed:9725914}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle
{ECO:0000269|PubMed:9725914}.
-!- SUBCELLULAR LOCATION: Isoform 8: Cytoplasm. Golgi apparatus
{ECO:0000269|PubMed:9725914}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Name=1; Synonyms=bab, DynIIIbb;
IsoId=Q08877-1; Sequence=Displayed;
Note=Expressed in lung, brain, heart.;
Name=2; Synonyms=baa, DynIIIba;
IsoId=Q08877-2; Sequence=VSP_034043;
Note=Expressed in lung, brain, heart, testis. Localized to
vesicular-like punctate spots, neither at the plasma membrane
nor the Golgi area.;
Name=3; Synonyms=bbb;
IsoId=Q08877-3; Sequence=VSP_034041;
Note=Expressed in lung, brain, heart, testis.;
Name=4; Synonyms=bba;
IsoId=Q08877-4; Sequence=VSP_034041, VSP_034043;
Note=Expressed in lung, brain, heart.;
Name=5; Synonyms=bcb;
IsoId=Q08877-5; Sequence=VSP_034042;
Note=Expressed in lung.;
Name=6; Synonyms=bca;
IsoId=Q08877-6; Sequence=VSP_034042, VSP_034043;
Note=Expressed in lung.;
Name=7; Synonyms=aab, DynIIIab;
IsoId=Q08877-7; Sequence=VSP_034038;
Note=Expressed in lung, brain, heart, testis.;
Name=8; Synonyms=aaa, DynIIIaa;
IsoId=Q08877-9; Sequence=VSP_034038, VSP_034043;
Note=Expressed in lung, brain, heart, testis. Diffuse
cytoplasmic distribution and some modest association with the
Golgi apparatus.;
Name=9; Synonyms=abb;
IsoId=Q08877-10; Sequence=VSP_034038, VSP_034041;
Note=Expressed in lung, brain, heart.;
Name=10; Synonyms=aba;
IsoId=Q08877-11; Sequence=VSP_034038, VSP_034041, VSP_034043;
Note=Expressed in lung, brain, heart.;
Name=11; Synonyms=acb;
IsoId=Q08877-12; Sequence=VSP_034038, VSP_034042;
Note=Expressed in lung.;
Name=12; Synonyms=aca;
IsoId=Q08877-13; Sequence=VSP_034038, VSP_034042, VSP_034043;
Note=Expressed in lung.;
Name=13; Synonyms=c;
IsoId=Q08877-8; Sequence=VSP_034039, VSP_034040;
Note=Expressed in lung, brain, heart, testis.;
-!- TISSUE SPECIFICITY: Isoform-specific expression in germ-cell-
depleted testis (Sertoli cells), brain (peripheral sensory
neurons), lung and heart. {ECO:0000269|PubMed:8360266,
ECO:0000269|PubMed:9725914}.
-!- DEVELOPMENTAL STAGE: Up-regulated expression throughout
development. {ECO:0000269|PubMed:8752097}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D14076; BAA03161.1; -; mRNA.
EMBL; AF201839; AAF07848.1; -; mRNA.
PIR; I55498; I55498.
RefSeq; NP_612547.1; NM_138538.1. [Q08877-1]
RefSeq; XP_006250203.1; XM_006250141.3. [Q08877-7]
RefSeq; XP_006250204.1; XM_006250142.3. [Q08877-9]
UniGene; Rn.11191; -.
ProteinModelPortal; Q08877; -.
SMR; Q08877; -.
BioGrid; 251309; 3.
ELM; Q08877; -.
IntAct; Q08877; 2.
STRING; 10116.ENSRNOP00000060160; -.
iPTMnet; Q08877; -.
PhosphoSitePlus; Q08877; -.
PaxDb; Q08877; -.
PRIDE; Q08877; -.
Ensembl; ENSRNOT00000067653; ENSRNOP00000063767; ENSRNOG00000026490. [Q08877-1]
Ensembl; ENSRNOT00000075938; ENSRNOP00000068044; ENSRNOG00000026490. [Q08877-9]
GeneID; 171574; -.
KEGG; rno:171574; -.
UCSC; RGD:727949; rat. [Q08877-1]
CTD; 26052; -.
RGD; 727949; Dnm3.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161069; -.
HOVERGEN; HBG107833; -.
InParanoid; Q08877; -.
KO; K01528; -.
OMA; FISRENC; -.
OrthoDB; EOG091G0EIQ; -.
PhylomeDB; Q08877; -.
BRENDA; 3.6.5.5; 5301.
Reactome; R-RNO-2132295; MHC class II antigen presentation.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
PRO; PR:Q08877; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000026490; -.
Genevisible; Q08877; RN.
GO; GO:0061828; C:apical tubulobulbar complex; IDA:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0061829; C:basal tubulobulbar complex; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; NAS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0044327; C:dendritic spine head; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0098844; C:postsynaptic endocytic zone membrane; IDA:SynGO.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0043083; C:synaptic cleft; IDA:RGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0050998; F:nitric-oxide synthase binding; IDA:RGD.
GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; IPI:RGD.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:RGD.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0046847; P:filopodium assembly; IDA:UniProtKB.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IDA:RGD.
GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:RGD.
GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IMP:RGD.
GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IMP:SynGO.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:0042713; P:sperm ejaculation; NAS:UniProtKB.
GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; ISO:RGD.
CDD; cd08771; DLP_1; 1.
Gene3D; 2.30.29.30; -; 1.
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.
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;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
Endocytosis; Golgi apparatus; GTP-binding; Hydrolase; Methylation;
Microtubule; Motor protein; Nitration; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 869 Dynamin-3.
/FTId=PRO_0000206574.
DOMAIN 28 294 Dynamin-type G.
DOMAIN 525 631 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 659 750 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 38 46 GTP. {ECO:0000250|UniProtKB:Q9UQ16}.
NP_BIND 205 211 GTP. {ECO:0000250|UniProtKB:Q9UQ16}.
NP_BIND 236 239 GTP. {ECO:0000250|UniProtKB:Q9UQ16}.
COMPBIAS 753 862 Pro-rich.
MOD_RES 80 80 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 125 125 Nitrated tyrosine; alternate.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 125 125 Phosphotyrosine; alternate.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 231 231 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39052}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000250|UniProtKB:P39054}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:P21575}.
MOD_RES 603 603 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39052}.
MOD_RES 604 604 N6-acetyllysine.
{ECO:0000250|UniProtKB:P50570}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:17376771}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:17376771}.
MOD_RES 793 793 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P39053}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000269|PubMed:17376771}.
VAR_SEQ 516 525 Missing (in isoform 7, isoform 8, isoform
9, isoform 10, isoform 11 and isoform
12). {ECO:0000303|PubMed:8360266}.
/FTId=VSP_034038.
VAR_SEQ 526 564 VIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEE
-> VRAKFCDSEGLADRQQHWHHERRLEGLLVCPHGRKLVL
V (in isoform 13). {ECO:0000305}.
/FTId=VSP_034039.
VAR_SEQ 565 869 Missing (in isoform 13). {ECO:0000305}.
/FTId=VSP_034040.
VAR_SEQ 636 640 SFTEN -> SFGSNKTEM (in isoform 3, isoform
4, isoform 9 and isoform 10).
{ECO:0000305}.
/FTId=VSP_034041.
VAR_SEQ 636 640 SFTEN -> DQAENEDGAQENTF (in isoform 5,
isoform 6, isoform 11 and isoform 12).
{ECO:0000305}.
/FTId=VSP_034042.
VAR_SEQ 847 869 SRRPPPSPTRPTIIRPLESSLLD -> RFGAVKEEAVEP
(in isoform 2, isoform 4, isoform 6,
isoform 8, isoform 10 and isoform 12).
{ECO:0000303|PubMed:8360266}.
/FTId=VSP_034043.
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


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