ID W5MWQ7_LEPOC Unreviewed; 843 AA.
AC W5MWQ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012816.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012816.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01000158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MWQ7; -.
DR STRING; 7918.ENSLOCP00000012816; -.
DR Ensembl; ENSLOCT00000012841.1; ENSLOCP00000012816.1; ENSLOCG00000010434.1.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR HOGENOM; CLU_008964_1_0_1; -.
DR InParanoid; W5MWQ7; -.
DR OMA; ISANTEY; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000010434; Expressed in camera-type eye and 11 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd08771; DLP_1; 1.
DR CDD; cd01256; PH_dynamin; 1.
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:SF54; DYNAMIN-3; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003932};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 519..625
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 653..744
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 742..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95124 MW; 2C4EE1C51AF691D4 CRC64;
MGNRGMEELI PLVNRLQDAF STIGQSCNLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLISANTEY AEFLQCKGKK FTDFDEVRQE IEAETDRLTG ANKGISPVPI
NLRVYSPYVL NLTLIDLPGI TKVPVGDQPP DIEYQIRDMI MQFICRENCL ILAVTPANTD
LANSDALKLA KDVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDIKA ALAAERKFFL SHPSYRHMAD NMGTPYLQKV LNQQLTNHIR DTLPAFRSKL
QAQLLSLDKE AEEYRHFRPD DPSRKTKALL QMVQQFSVDF EKRIEGSGDQ VDTVELSGGA
KINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL
KEPCLKCVDM VIQELINTVR QCTIKLGTFP RLREETERIV TTHIRDRESR AKDQVLLLIE
VQLSYINTNH EDFIGFANAQ QRSSQMSKKS SAGNQQTLLV IRKGWLTINN ISIIKGGAKE
YWFVLTAESL SWFKDDEEKE KKYMLPLDNL KVRDVEKGFM SSKHIFALFN TEQRNVYKDY
RYLELACDSQ EEVDSWKASL LRAGVYPEKS FVDSEDSGPS DNFSMDPQLE RQVETIRNLV
DSYMAIVNKC IRDLMPKTIM HLMINNVKEF INAELLAQLY STGDQSALMD ESQEQAQRRD
EVLRTHHALK EALAIIGDIS TTTITTPLPP PVDSSWLQAG QGGSRRSPPP SPTAPRRMQL
GSRAPAPPVP SRPGPLPPFN NSADALPPQV PSRPNRAPPS IPSVRQKKTN PESVKIPLSS
VKK
//
