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Protein

Dynamin-1-like protein

Gene

DNM1L

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Plays an important role in mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution (By similarity).By similarity

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 40GTPBy similarity9
Nucleotide bindingi228 – 234GTPBy similarity7
Nucleotide bindingi259 – 262GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Endocytosis, Necrosis

Keywords - Ligandi

GTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-75153. Apoptotic execution phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynamin-1-like protein (EC:3.6.5.5)
Gene namesi
Name:DNM1L
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Coated pit, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002849721 – 749Dynamin-1-like proteinAdd BLAST749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei542PhosphoserineBy similarity1
Cross-linki545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei561PhosphoserineBy similarity1
Cross-linki571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Glycosylationi598O-linked (GlcNAc)By similarity1
Glycosylationi599O-linked (GlcNAc)By similarity1
Cross-linki607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei610N6-acetyllysine; alternateBy similarity1
Cross-linki610Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki619Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei620PhosphoserineBy similarity1
Cross-linki621Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei629Phosphoserine; by CDK1By similarity1
Modified residuei650Phosphoserine; by CAMK1 and PKABy similarity1
Modified residuei657S-nitrosocysteineBy similarity1

Post-translational modificationi

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-650 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-629 also promotes mitochondrial fission (By similarity).By similarity
Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity).By similarity
S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage.By similarity
O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-650 (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiQ2KIA5.
PeptideAtlasiQ2KIA5.
PRIDEiQ2KIA5.

Expressioni

Gene expression databases

BgeeiENSBTAG00000011395.

Interactioni

Subunit structurei

Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern. Can also oligomerize to form multimeric ring-like structures. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria. Interacts with BCL2L1 isoform BCL-X(L) and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with FIS1. Interacts with MIEF2 and MIEF1; this regulates GTP hydrolysis and DNM1L oligomerization. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037777.

Structurei

3D structure databases

ProteinModelPortaliQ2KIA5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 315Dynamin-type GAdd BLAST294
Domaini657 – 748GEDPROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 356GTPase domainBy similarityAdd BLAST356
Regioni1 – 356N-terminal dimerization domainBy similarityAdd BLAST356
Regioni357 – 502Middle domainBy similarityAdd BLAST146
Regioni461 – 698Interaction with GSK3BBy similarityAdd BLAST238
Regioni515 – 582B domainBy similarityAdd BLAST68
Regioni667 – 681Important for homodimerizationBy similarityAdd BLAST15

Domaini

The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization.By similarity

Sequence similaritiesi

Contains 1 GED domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiQ2KIA5.
KOiK17065.
OMAiISSEAIH.
OrthoDBiEOG091G02TQ.
TreeFamiTF352031.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030556. DNM1L.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR003130. GED.
IPR020850. GED_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 2 hits.
PTHR11566:SF39. PTHR11566:SF39. 2 hits.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2KIA5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGIVTR RPLILQLVHV APEDKRKTTG EENDPATWKN SRHLSKGVEA
110 120 130 140 150
EEWGKFLHTK NKLYTDFDEI RQEIENETER ISGNNKGVSP EPIHLKIFSP
160 170 180 190 200
NVVNLTLVDL PGMTKVPVGD QPKDIELQIR ELILRFISNP NSIILAVTAA
210 220 230 240 250
NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM DVLMGRVIPV
260 270 280 290 300
KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR
310 320 330 340 350
TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI
360 370 380 390 400
TKFATEYCNT IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL
410 420 430 440 450
NTIDILTAIR NATGPRPALF VPEVSFELLV KRQIKRLEEP SLRCVELVHE
460 470 480 490 500
EMQRIIQHCS NYSTQELLRF PKLHDAIVEV VTCLLRKRLP VTNEMVHNLV
510 520 530 540 550
AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA VSRDKSSKVP
560 570 580 590 600
SALAPASQEP SPAASAEADG KLIQESRRET KNAASGGGGV GDAVQEPTTG
610 620 630 640 650
NWRGMLKTSK AEELLAEEKS KPIPIMPASP QKGHAVNLLD VPVPVARKLS
660 670 680 690 700
AREQRDCEVI ERLIKSYFLI VRKNIQDSVP KAVMHFLVNH VKDTLQSELV
710 720 730 740
GQLYKSSLLD DLLTESEDMA QRRKEAADML KALQGASQII AEIRETHLW
Length:749
Mass (Da):83,352
Last modified:March 7, 2006 - v1
Checksum:iBA90863E8BC8265B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112710 mRNA. Translation: AAI12711.1.
RefSeqiNP_001039959.1. NM_001046494.2.
UniGeneiBt.87451.

Genome annotation databases

EnsembliENSBTAT00000037956; ENSBTAP00000037777; ENSBTAG00000011395.
GeneIDi540892.
KEGGibta:540892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112710 mRNA. Translation: AAI12711.1.
RefSeqiNP_001039959.1. NM_001046494.2.
UniGeneiBt.87451.

3D structure databases

ProteinModelPortaliQ2KIA5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000037777.

Proteomic databases

PaxDbiQ2KIA5.
PeptideAtlasiQ2KIA5.
PRIDEiQ2KIA5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000037956; ENSBTAP00000037777; ENSBTAG00000011395.
GeneIDi540892.
KEGGibta:540892.

Organism-specific databases

CTDi10059.

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161068.
HOVERGENiHBG107833.
InParanoidiQ2KIA5.
KOiK17065.
OMAiISSEAIH.
OrthoDBiEOG091G02TQ.
TreeFamiTF352031.

Enzyme and pathway databases

ReactomeiR-BTA-75153. Apoptotic execution phase.

Gene expression databases

BgeeiENSBTAG00000011395.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030556. DNM1L.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR003130. GED.
IPR020850. GED_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 2 hits.
PTHR11566:SF39. PTHR11566:SF39. 2 hits.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNM1L_BOVIN
AccessioniPrimary (citable) accession number: Q2KIA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 7, 2006
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.