ID A0A3Q0R2F6_AMPCI Unreviewed; 697 AA.
AC A0A3Q0R2F6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000003585.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000003585.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3Q0R2F6; -.
DR STRING; 61819.ENSACIP00000003585; -.
DR Ensembl; ENSACIT00000003701.1; ENSACIP00000003585.1; ENSACIG00000002828.1.
DR GeneTree; ENSGT00940000155504; -.
DR OMA; CAYINTN; -.
DR Proteomes; UP000261340; 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 Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 22..301
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 605..696
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 525..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 77737 MW; D474D34535201658 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDI LPRGTGIVTR
RPLILQLVHI DQEDRRKTTE ENGIDGEEWG KFLHTKNKIY TDFEEIRQEI EAETERISGN
NKGISDEPIH LKIFSPYVVN LTLVDLPGIT KVPVGDQPKD IEIQIRELIL KYISNPNSII
LAVTAANTDM ATSEALKVAR EVDPDGRRTL AVITKLDLMD AGTDAMDVLM GRVIPVKLGI
IGVVNRSQLD INQKKSVADS IRDEHAFLQK KYPSLANRNG TKYLARTLNR LLMHHIRDCL
PELKTRINVL AAQYQSLLNS YGEPVDDKSA TLLQIITKFA AEYCNTIEGT AKYIETAELC
GGARICYIFH ETFGRTLESV DPLGGLTTID VLTAIRNATG PRPALFVPEV SFELLVKRQV
KRLEEPSLRC VELVHEEMQR IIQHCSNYST QELLRFPKLH DAIVEVVTSL LRKRLPVTNE
MVHNLVAIEL AYINTKHPDF ADACGLMNNN IEEQRRNRLR DLPSAVPRDK AAASGSQSLS
SGDQADGGTG NWRGMLRKGE EGPGGDRAMS QPPVAASPQK GHAVNLLDVP VPVSRKLSAR
EQRDCEVIER LIKSYFLIVR KNIQDSVPKA VMHFLVNHVK DCLQSELVGQ LYKTTLLNDL
LTESEDMAQR RNEAADMLKA LQKASQVIAE IRETHLW
//
