DNM1L_DANRE
ID DNM1L_DANRE Reviewed; 691 AA.
AC Q7SXN5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Dynamin-1-like protein;
DE EC=3.6.5.5;
GN Name=dnm1l; ORFNames=zgc:66163;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates
CC membrane fission through oligomerization into membrane-associated
CC tubular structures that wrap around the scission site to constrict and
CC sever the mitochondrial membrane through a GTP hydrolysis-dependent
CC mechanism. The specific recruitment at scission sites is mediated by
CC membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial
CC membranes. While the recruitment by the membrane receptors is GTP-
CC dependent, the following hydrolysis of GTP induces the dissociation
CC from the receptors and allows DNM1L filaments to curl into closed rings
CC that are probably sufficient to sever a double membrane (By
CC similarity). May play a role in the circadian control of mitochondrial
CC ATP production (By similarity). {ECO:0000250|UniProtKB:O00429}.
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: Homotetramer; dimerizes through the N-terminal GTP-middle
CC region of one molecule binding to the GED domain of another DNM1L
CC molecule. Oligomerizes in a GTP-dependent manner to form membrane-
CC associated tubules with a spiral pattern.
CC {ECO:0000250|UniProtKB:O00429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Endomembrane system {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O00429}; Peripheral membrane protein
CC {ECO:0000250}. Peroxisome {ECO:0000250}. Membrane, clathrin-coated pit
CC {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250}.
CC -!- DOMAIN: The GED domain folds back to interact, in cis, with the GTP-
CC binding domain and middle domain, and interacts, in trans, with the GED
CC domains of other DNM1L molecules, and is thus critical for activating
CC GTPase activity and for DNM1L dimerization.
CC {ECO:0000250|UniProtKB:O00429}.
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; BC055521; AAH55521.1; -; mRNA.
DR RefSeq; NP_957216.1; NM_200922.1.
DR AlphaFoldDB; Q7SXN5; -.
DR SMR; Q7SXN5; -.
DR STRING; 7955.ENSDARP00000006315; -.
DR PaxDb; Q7SXN5; -.
DR Ensembl; ENSDART00000006840; ENSDARP00000006315; ENSDARG00000015006.
DR GeneID; 393896; -.
DR KEGG; dre:393896; -.
DR CTD; 10059; -.
DR ZFIN; ZDB-GENE-040426-1556; dnm1l.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155504; -.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q7SXN5; -.
DR OMA; IMATQFQ; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q7SXN5; -.
DR TreeFam; TF352031; -.
DR Reactome; R-DRE-75153; Apoptotic execution phase.
DR PRO; PR:Q7SXN5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000015006; Expressed in testis and 27 other tissues.
DR ExpressionAtlas; Q7SXN5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0016559; P:peroxisome fission; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030556; DNM1L.
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; PTHR11566; 2.
DR PANTHER; PTHR11566:SF39; PTHR11566:SF39; 2.
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; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 2: Evidence at transcript level;
KW Biological rhythms; Coated pit; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; GTP-binding; Hydrolase; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Peroxisome; Reference proteome; Synapse.
FT CHAIN 1..691
FT /note="Dynamin-1-like protein"
FT /id="PRO_0000206569"
FT DOMAIN 22..301
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 599..690
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 32..39
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 58..60
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 145..148
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 214..217
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 244..247
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 343..488
FT /note="Middle domain"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT REGION 522..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..623
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 32..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 214..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 245..248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
SQ SEQUENCE 691 AA; 77263 MW; FF3B9A167B2420C7 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIAV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR
RPLILQLVHV DPEDRRKTSE ENGVDGEEWG KFLHTKNKIY TDFDEIRQEI ENETERVSGN
NKGISDEPIH LKIFSPHVVN LTLVDLPGIT KVPVGDQPKD IELQIRELIL KYISNPNSII
LAVTAANTDM ATSEALKVAR EVDPDGRRTL AVVTKLDLMD AGTDAMDVLM GRVIPVKLGL
IGVVNRSQLD INNKKSVADS IRDEHGFLQK KYPSLANRNG TKYLARTLNR LLMHHIRDCL
PELKTRINVL SAQYQSLLSS YGEPVEDMSA TLLQLITKFA TEYCNTIEGT AKYIETAELC
GGARICYIFH ETFGRTLESV DPLGGLTTID VLTAIRNATG PRPALFVPEV SFELLVKRQV
KRLEEPSLRC VELVHEEMQR IIQHCSNYST QELLRFPKLH DAIVEVVTSL LRKRLPVTNE
MVHNLVAIEL AYINTKHPDF ADACGLMNNN IEEQRRNRMR ELPTSVPRDK MAGGAQAEQE
GGTGTWRGML KKGDEGQGEE KTKLQSSIPA SPQKGHAVNL LDVPVPVARK LSAREQRDCE
VIERLIKSYF LIVRKNIQDS VPKAVMHFLV NHVKDSLQSE LVGQLYKPAL LDDLLTESED
MAQRRNEAAD MLKALQKASQ VIAEIRETHL W
