Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dynamin-1-like protein

Gene

Dnm1l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.6 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409GTPBy similarity
Nucleotide bindingi228 – 2347GTPBy similarity
Nucleotide bindingi259 – 2624GTPBy similarity

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-RNO-75153. Apoptotic execution phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynamin-1-like protein (EC:3.6.5.5)
Alternative name(s):
Dynamin-like protein
Gene namesi
Name:Dnm1l
Synonyms:Dlp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi620416. Dnm1l.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381K → A: Defective in GTP hydrolysis. Tubulates spherical liposomes. Impairs mitochondrial division. Decreases the BCL2L1-mediated induction of synapse number and size of synaptic vesicle clusters. 2 Publications
Mutagenesisi71 – 711S → A: No effect on mitotic phosphorylation. 1 Publication
Mutagenesisi139 – 1391S → A: No effect on mitotic phosphorylation. 1 Publication
Mutagenesisi149 – 1491S → A: No effect on mitotic phosphorylation. 1 Publication
Mutagenesisi231 – 2311D → N: Defective in GTP-binding. 1 Publication
Mutagenesisi635 – 6351S → A: Abolishes mitotic phosphorylation. Reduced mitotic mitochondrial fragmentation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 755755Dynamin-1-like proteinPRO_0000206568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei542 – 5421PhosphoserineBy similarity
Cross-linki545 – 545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki548 – 548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei561 – 5611PhosphoserineBy similarity
Cross-linki571 – 571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki581 – 581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Glycosylationi604 – 6041O-linked (GlcNAc)1 Publication
Glycosylationi605 – 6051O-linked (GlcNAc)1 Publication
Cross-linki613 – 613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei616 – 6161N6-acetyllysine; alternateBy similarity
Cross-linki616 – 616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki625 – 625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei626 – 6261PhosphoserineBy similarity
Cross-linki627 – 627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei635 – 6351Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei656 – 6561Phosphoserine; by CAMK1 and PKABy similarity
Modified residuei663 – 6631S-nitrosocysteineBy similarity

Post-translational modificationi

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-656 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-635 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
Ubiquitinated by MARCH5.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-656.1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiO35303.
PeptideAtlasiO35303.
PRIDEiO35303.

PTM databases

iPTMnetiO35303.
PhosphoSiteiO35303.

Expressioni

Tissue specificityi

Expressed in all tissues tested (at protein level). Longer isoforms are preferentially expressed in brain.2 Publications

Inductioni

By bezafibrate.1 Publication

Gene expression databases

BgeeiENSRNOG00000001813.
GenevisibleiO35303. RN.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bcl2l1P53563-12EBI-1767447,EBI-287204

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250292. 2 interactions.
DIPiDIP-29699N.
IntActiO35303. 3 interactions.
MINTiMINT-4582542.
STRINGi10116.ENSRNOP00000002478.

Structurei

3D structure databases

ProteinModelPortaliO35303.
SMRiO35303. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 315294Dynamin-type GAdd
BLAST
Domaini663 – 75492GEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 356356GTPase domainBy similarityAdd
BLAST
Regioni1 – 356356N-terminal dimerization domainBy similarityAdd
BLAST
Regioni357 – 502146Middle domainBy similarityAdd
BLAST
Regioni461 – 704244Interaction with GSK3BBy similarityAdd
BLAST
Regioni461 – 667207Interaction with GSK3BBy similarityAdd
BLAST
Regioni515 – 58268B domainBy similarityAdd
BLAST
Regioni555 – 755201C-terminal dimerization domainBy similarityAdd
BLAST
Regioni673 – 68715Important for homodimerizationBy similarityAdd
BLAST

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.
GeneTreeiENSGT00840000129895.
HOVERGENiHBG107833.
InParanoidiO35303.
KOiK17065.
OMAiGQEPTTG.
OrthoDBiEOG091G02TQ.
PhylomeDBiO35303.
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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35303-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL
60 70 80 90 100
LPRGTGVVTR RPLILQLVHV SPEDKRKTTG EENDPATWKN SRHLSKGVEA
110 120 130 140 150
EEWGKFLHTK NKLYTDFDEI RQEIENETER ISGNNKGVSP EPIHLKVFSP
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 KLIQDNRRET KNVASAGGGI GDGGRIGDGG
610 620 630 640 650
QEPTTGNWRG MLKTSKAEEL LAEEKSKPIP IMPASPQKGH AVNLLDVPVP
660 670 680 690 700
VARKLSAREQ RDCEVIERLI KSYFLIVRKN IQDSVPKAVM HFLVNHVKDT
710 720 730 740 750
LQSELVGQLY KSSLLDDLLT ESEDMAQRRK EAADMLKALQ GASQIIAEIR

ETHLW
Length:755
Mass (Da):83,908
Last modified:January 1, 1998 - v1
Checksum:i0568353907794C43
GO
Isoform 2 (identifier: O35303-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-96: Missing.
     546-571: Missing.

Show »
Length:716
Mass (Da):79,951
Checksum:iE7A629A401FA7004
GO
Isoform 3 (identifier: O35303-3) [UniParc]FASTAAdd to basket
Also known as: DLP1-37

The sequence of this isoform differs from the canonical sequence as follows:
     84-84: D → GKFQSWN
     546-596: SSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRI → VASGGGGV

Show »
Length:718
Mass (Da):80,253
Checksum:iBC6D99B05A12B398
GO
Isoform 4 (identifier: O35303-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-97: DPATWKNSRHLSKG → GKFQSWR

Note: No experimental confirmation available.
Show »
Length:748
Mass (Da):83,220
Checksum:iFFF210166CD3398E
GO
Isoform 5 (identifier: O35303-5) [UniParc]FASTAAdd to basket
Also known as: DLP1-11

The sequence of this isoform differs from the canonical sequence as follows:
     572-582: Missing.

Show »
Length:744
Mass (Da):82,540
Checksum:i5C1E562180C58035
GO
Isoform 6 (identifier: O35303-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     546-582: Missing.

Note: No experimental confirmation available.
Show »
Length:718
Mass (Da):80,104
Checksum:i459857BD43835FE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti517 – 5171A → V in AAB71237 (PubMed:9472031).Curated
Sequence conflicti600 – 6001G → V in AAD31278 (PubMed:10679301).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei84 – 9714DPATW…HLSKG → GKFQSWR in isoform 4. 1 PublicationVSP_013696Add
BLAST
Alternative sequencei84 – 9613Missing in isoform 2. 2 PublicationsVSP_013697Add
BLAST
Alternative sequencei84 – 841D → GKFQSWN in isoform 3. 2 PublicationsVSP_013698
Alternative sequencei546 – 59651SSKVP…DGGRI → VASGGGGV in isoform 3. 2 PublicationsVSP_013699Add
BLAST
Alternative sequencei546 – 58237Missing in isoform 6. 1 PublicationVSP_013700Add
BLAST
Alternative sequencei546 – 57126Missing in isoform 2. 2 PublicationsVSP_013701Add
BLAST
Alternative sequencei572 – 58211Missing in isoform 5. 2 PublicationsVSP_013702Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019043 mRNA. Translation: AAB72197.1.
AF020207 mRNA. Translation: AAB71232.1.
AF020208 mRNA. Translation: AAB71233.1.
AF020209 mRNA. Translation: AAB71234.1.
AF020210 mRNA. Translation: AAB71235.1.
AF020211 mRNA. Translation: AAB71236.1.
AF020212 mRNA. Translation: AAB71237.1.
AF020213 mRNA. Translation: AAB71238.1.
AF107048 mRNA. Translation: AAD22412.1.
AF132727 mRNA. Translation: AAD31278.1.
BC085843 mRNA. Translation: AAH85843.1.
RefSeqiNP_446107.2. NM_053655.3. [O35303-2]
XP_006248778.1. XM_006248716.2. [O35303-1]
XP_006248780.1. XM_006248718.2. [O35303-4]
XP_006248785.1. XM_006248723.2. [O35303-6]
XP_008767063.1. XM_008768841.1. [O35303-1]
XP_008767064.1. XM_008768842.1. [O35303-4]
XP_008767065.1. XM_008768843.1. [O35303-5]
UniGeneiRn.216851.

Genome annotation databases

EnsembliENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813. [O35303-2]
ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813. [O35303-1]
ENSRNOT00000002482; ENSRNOP00000002482; ENSRNOG00000001813. [O35303-6]
GeneIDi114114.
KEGGirno:114114.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019043 mRNA. Translation: AAB72197.1.
AF020207 mRNA. Translation: AAB71232.1.
AF020208 mRNA. Translation: AAB71233.1.
AF020209 mRNA. Translation: AAB71234.1.
AF020210 mRNA. Translation: AAB71235.1.
AF020211 mRNA. Translation: AAB71236.1.
AF020212 mRNA. Translation: AAB71237.1.
AF020213 mRNA. Translation: AAB71238.1.
AF107048 mRNA. Translation: AAD22412.1.
AF132727 mRNA. Translation: AAD31278.1.
BC085843 mRNA. Translation: AAH85843.1.
RefSeqiNP_446107.2. NM_053655.3. [O35303-2]
XP_006248778.1. XM_006248716.2. [O35303-1]
XP_006248780.1. XM_006248718.2. [O35303-4]
XP_006248785.1. XM_006248723.2. [O35303-6]
XP_008767063.1. XM_008768841.1. [O35303-1]
XP_008767064.1. XM_008768842.1. [O35303-4]
XP_008767065.1. XM_008768843.1. [O35303-5]
UniGeneiRn.216851.

3D structure databases

ProteinModelPortaliO35303.
SMRiO35303. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250292. 2 interactions.
DIPiDIP-29699N.
IntActiO35303. 3 interactions.
MINTiMINT-4582542.
STRINGi10116.ENSRNOP00000002478.

PTM databases

iPTMnetiO35303.
PhosphoSiteiO35303.

Proteomic databases

PaxDbiO35303.
PeptideAtlasiO35303.
PRIDEiO35303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813. [O35303-2]
ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813. [O35303-1]
ENSRNOT00000002482; ENSRNOP00000002482; ENSRNOG00000001813. [O35303-6]
GeneIDi114114.
KEGGirno:114114.

Organism-specific databases

CTDi10059.
RGDi620416. Dnm1l.

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00840000129895.
HOVERGENiHBG107833.
InParanoidiO35303.
KOiK17065.
OMAiGQEPTTG.
OrthoDBiEOG091G02TQ.
PhylomeDBiO35303.
TreeFamiTF352031.

Enzyme and pathway databases

ReactomeiR-RNO-75153. Apoptotic execution phase.

Miscellaneous databases

PROiO35303.

Gene expression databases

BgeeiENSRNOG00000001813.
GenevisibleiO35303. RN.

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_RAT
AccessioniPrimary (citable) accession number: O35303
Secondary accession number(s): O35318
, O35319, O35320, O35321, O35322, O35323, Q5U2W1, Q792T7, Q9R234, Q9R277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 129 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, Direct protein sequencing, 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.