ID A0A3Q1I3Q4_ANATE Unreviewed; 643 AA.
AC A0A3Q1I3Q4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dynamin-1-like protein {ECO:0000256|ARBA:ARBA00018833};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
DE AltName: Full=Interferon-induced GTP-binding protein Mx {ECO:0000256|ARBA:ARBA00015210};
DE AltName: Full=Interferon-inducible Mx protein {ECO:0000256|ARBA:ARBA00031810};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000014825.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000014825.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001837};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004432}.
CC Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004600}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004450}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR AlphaFoldDB; A0A3Q1I3Q4; -.
DR Ensembl; ENSATET00000015060.2; ENSATEP00000014825.2; ENSATEG00000018248.2.
DR GeneTree; ENSGT00940000155504; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 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 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 PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF39; DYNAMIN-1-LIKE PROTEIN; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003932};
KW Membrane {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003932}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 22..301
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 551..642
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
SQ SEQUENCE 643 AA; 72444 MW; B4CACD9A23758FF8 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDI LPRGTGIVTR
RPLILQLVHI DQEDRRKTNE ENGIDGEEWG KFLHTKNKIY TDFEEIRQEI EAETERMSGN
NKGISDEPIH LKIFSPHVVN LTLVDLPGIT KVPVGDQPRD IEIQIRELIL KYISNPNSII
LAVTAANTDM ATSESLKVAR EVDPDGRRTL AVVTKLDLMD AGTDAMDVLM GRVIPVKLGI
IGVVNRSQLD INQKKLVADS IRDECAFLQK RYPSLANRNG TKYLAKTLNR LLMHHIRDCL
PELKTRINVL AAQYQSLLSS YGEPVEDKSS TLLQLITKFA TEYCNTIEGT AKYIETAELC
GGARICYIFH ETFGRTLESV DPLGGLTTID VLTAIRNATG PRPALFVPEV SFELLVKRQV
KRLEEPSLRC VELVHEEMQR IIQHCSNYST QELLRFPKLH DAIVEVVTSL LRKRLPVTND
MVHNLVAIEL AYINTKHPDF ADACEFNLSL CCCLQATEPL SYQCLWLDFT ITSHLPVPVS
RKLSSREQRD CEVIERLIKS YFLIVRKNIQ DSVPKAVMHF LVNHVKESLQ SELVGQLYKT
ALLSDLLTES EDMAQRRNEA ADMLKALQKA SQVIAEIRET HMW
//
