DYN2_BOVIN
ID DYN2_BOVIN Reviewed; 866 AA.
AC A6H7I5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dynamin-2;
DE EC=3.6.5.5;
GN Name=DNM2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Plays
CC a role in the regulation of neuron morphology, axon growth and
CC formation of neuronal growth cones (By similarity). Plays an important
CC role in vesicular trafficking processes, in particular endocytosis.
CC Involved in cytokinesis. Regulates maturation of apoptotic cell corpse-
CC containing phagosomes by recruiting PIK3C3 to the phagosome membrane.
CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P39054}.
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 -!- SUBUNIT: Interacts with MYOF (By similarity). Interacts with CTTN and
CC ACTN1 (By similarity). Interacts with SHANK1, SHANK2, SH3BP4 and
CC NOSTRIN. Interacts with SNX9. Interacts with SNX18. Interacts with
CC SNX33 (via SH3 domain). Interacts with MYO1E (via SH3 domain).
CC Interacts with PSTPIP1. Interacts with CTNND2 (By similarity). May
CC interact with PIK3C3 (By similarity). May be a component of a complex
CC composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By similarity).
CC Interacts with BIN1 (By similarity). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000250|UniProtKB:P39054, ECO:0000250|UniProtKB:P50570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50570}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cell junction
CC {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:P39052}. Postsynaptic density
CC {ECO:0000250|UniProtKB:P50570}. Synapse {ECO:0000250|UniProtKB:P50570}.
CC Midbody {ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:P39054}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:P39054}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P39054}. Note=Colocalizes with CTTN at the basis
CC of filopodia in hippocampus neuron growth zones. Microtubule-
CC associated. Also found in the postsynaptic density of neuronal cells.
CC Co-localizes with PIK3C3 and RAB5A to the nascent phagosome.
CC {ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570}.
CC -!- PTM: Phosphorylation at Ser-760 by CDK1 is greatly increased upon
CC mitotic entry. It regulates cytokinesis downstream of calcineurin, and
CC does not affect clathrin-mediated endocytosis. Dephosphorylated by
CC calcineurin/PP2 (By similarity). Phosphorylated on tyrosine residues
CC after activation of SRC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P39052}.
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; BC146259; AAI46260.1; -; mRNA.
DR RefSeq; NP_001092839.1; NM_001099369.1.
DR AlphaFoldDB; A6H7I5; -.
DR BMRB; A6H7I5; -.
DR SMR; A6H7I5; -.
DR STRING; 9913.ENSBTAP00000035986; -.
DR PaxDb; A6H7I5; -.
DR PRIDE; A6H7I5; -.
DR GeneID; 511691; -.
DR KEGG; bta:511691; -.
DR CTD; 1785; -.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; A6H7I5; -.
DR OrthoDB; 264244at2759; -.
DR BRENDA; 3.6.5.5; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027188; DNM2.
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 PANTHER; PTHR11566:SF23; PTHR11566:SF23; 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 2: Evidence at transcript level;
KW Acetylation; Cell junction; Cell projection; Coated pit; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; GTP-binding; Hydrolase;
KW Membrane; Microtubule; Motor protein; Nucleotide-binding; Phagocytosis;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..866
FT /note="Dynamin-2"
FT /id="PRO_0000319950"
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 649..740
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 737..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..855
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:O00429"
FT BINDING 205..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
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 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 760
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P39052"
SQ SEQUENCE 866 AA; 97836 MW; 35976F3202391BB7 CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEY AEFLHCKSRK FTDFEEVRQE IEAETDRVTG TNKGISPVPI
NLRIYSPHVL NLTLIDLPGI TKVPVGDQPQ DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIEGKKDIRT ALAAERKFFL SHPAYRHIAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AVPNQVIRRG WLTINNISLM KGGSKEYWFV
LTAESLSWYK DEEEKEKKYM LPLDNLKIRD VEKGFMSNKH VFAIFNTEQR NVYKDLRQIE
LACDSQEDVD SWKASFLRAG VYPEKDQAEN EDGAQENTFS MDPQLERQVE TIRNLVDSYV
AIINKSIRDL MPKTIMHLMI NNTKAFIHYE LLAYLYSSAD QSSLMEESAD QAQRRDDMLR
MYHALKEALN IIGDISTSTV STPVPPPVDD TWIQNTSSHS PTPQRRPVSS VHPPGRPPAV
RGPTPGPPLI PVPVGPASFS APPIPSRPGP HPGVFANNDP FSAPPQIPSR PARIPPGIPP
GVPSRRPPAA PSRPTIIRPA EPSLLD
