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Protein

Mitofusin-1

Gene

Mfn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN1 acts independently of the cytoskeleton. Overexpression induces the formation of mitochondrial networks.2 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi82 – 89GTPCurated8
Nucleotide bindingi178 – 182GTPCurated5
Nucleotide bindingi237 – 240GTPCurated4

GO - Molecular functioni

GO - Biological processi

  • mitochondrial fusion Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5205685. Pink/Parkin Mediated Mitophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin-1 (EC:3.6.5.-)
Alternative name(s):
Transmembrane GTPase MFN1
Gene namesi
Name:Mfn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914664. Mfn1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 584CytoplasmicSequence analysisAdd BLAST584
Transmembranei585 – 605Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini606 – 608Mitochondrial intermembraneSequence analysis3
Transmembranei609 – 629Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini630 – 741CytoplasmicSequence analysisAdd BLAST112

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

In cardiomyocytes, no effect on mitochondrial morphometry or respiratory function.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276731 – 741Mitofusin-1Add BLAST741

Post-translational modificationi

Ubiquitinated by MARCH5. When mitochondria are depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7 and PARK2. Ubiquitinated by non-degradative ubiquitin by PARK2, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:24513856).1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ811U4.
MaxQBiQ811U4.
PaxDbiQ811U4.
PeptideAtlasiQ811U4.
PRIDEiQ811U4.

PTM databases

iPTMnetiQ811U4.
PhosphoSitePlusiQ811U4.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Expressed in E8.5, E9.5, E10.5 and E11.5 embryos.1 Publication

Gene expression databases

BgeeiENSMUSG00000027668.
CleanExiMM_MFN1.
ExpressionAtlasiQ811U4. baseline and differential.
GenevisibleiQ811U4. MM.

Interactioni

Subunit structurei

Forms homomultimers and heteromultimers with MFN2. Multimerization, which is mediated by the second coiled coil region, may play an essential role in mitochondrion fusion. Participates in a high molecular weight multiprotein complex. Interacts with VAT1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-9029118,EBI-5323863From a different organism.

Protein-protein interaction databases

BioGridi212170. 2 interactors.
DIPiDIP-60969N.
IntActiQ811U4. 1 interactor.
STRINGi10090.ENSMUSP00000088801.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi676 – 733Combined sources58

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T3JX-ray2.50A660-735[»]
ProteinModelPortaliQ811U4.
SMRiQ811U4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ811U4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 321Dynamin-type GAdd BLAST250

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili371 – 4081 PublicationAdd BLAST38
Coiled coili677 – 7351 PublicationAdd BLAST59

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0448. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00390000013727.
HOVERGENiHBG052465.
InParanoidiQ811U4.
KOiK06030.
OMAiAMTDEIC.
OrthoDBiEOG091G02ES.
TreeFamiTF314289.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR006884. Fzo/mitofusin_HR2.
IPR030381. G_DYNAMIN_dom.
IPR027088. Mitofusin-1.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF2. PTHR10465:SF2. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q811U4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETVSPLKH FVLAKKAITA IFGQLLEFVT EGSHFVEATY RNPELDRIAS
60 70 80 90 100
EDDLVEIQGY RNKLAVIGEV LSRRHMKVAF FGRTSSGKSS VINAMLWDKV
110 120 130 140 150
LPSGIGHTTN CFLSVEGTDG DKAYLMTEGS DEKKSVKTVN QLAHALHMDK
160 170 180 190 200
DLKAGCLVHV FWPKAKCALL RDDLVLVDSP GTDVTTELDI WIDKFCLDAD
210 220 230 240 250
VFVLVANSES TLMNTEKHFF HKVNERLSKP NIFILNNRWD ASASEPEYME
260 270 280 290 300
DVRRQHMERC LHFLVEELKV VSPSEARNRI FFVSAKEVLN SRKHKAQGMP
310 320 330 340 350
EGGGALAEGF QARLQEFQNF EQTFEECISQ SAVKTKFEQH TIRAKQILDT
360 370 380 390 400
VKNILDSVNV AAAEKRVYSM EEREDQIDRL DFIRNQMNLL TLDVKKKIKE
410 420 430 440 450
VTEEVANKVS CAMTDEICRL SVLVDEFCSE FHPTPSVLKV YKSELNKHIE
460 470 480 490 500
DGMGRNLADR CTNEVNASIL QSQQEIIENL KPLLPAGIQN KLHTLIPCKK
510 520 530 540 550
FDLSYDLNCH KLCSDFQEDI VFRFSLGWSS LVHRFLGSTN AQRVLLGLSE
560 570 580 590 600
PIFQVPRSLA STPTAPSNPA APDNAAQEEL MITLITGLAS LTSRTSMGII
610 620 630 640 650
VVGGVIWKTV GWKLISVTLS MYGALYLYER LTWTTRAKER AFKQQFVNYA
660 670 680 690 700
TEKLQMIVSF TSANCSHQVQ QEMATTFARL CQQVDVTQKH LEEEIARLSK
710 720 730 740
EIDQLEKIQN NSKLLRNKAV QLESELENFS KQFLHPSSGE S
Length:741
Mass (Da):83,726
Last modified:July 27, 2011 - v3
Checksum:i36E5E90DB0C0D5A1
GO

Sequence cautioni

The sequence AAH47050 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC25260 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209E → G in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti328 – 329IS → VL in BAB31111 (PubMed:16141072).Curated2
Sequence conflicti335T → A in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti521V → A in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti588L → W in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti619L → S in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti718K → R in BAB31111 (PubMed:16141072).Curated1
Sequence conflicti720V → I in AAH02133 (PubMed:15489334).Curated1
Sequence conflicti720V → I in AAH56641 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY174062 mRNA. Translation: AAO34660.1.
AK009490 mRNA. Translation: BAC25260.1. Different initiation.
AK018181 mRNA. Translation: BAB31111.1.
AK141611 mRNA. Translation: BAE24764.1.
BC002133 mRNA. Translation: AAH02133.1.
BC047050 mRNA. Translation: AAH47050.1. Different initiation.
BC056641 mRNA. Translation: AAH56641.1.
CCDSiCCDS17296.1.
RefSeqiNP_077162.2. NM_024200.4.
UniGeneiMm.290414.

Genome annotation databases

EnsembliENSMUST00000091257; ENSMUSP00000088801; ENSMUSG00000027668.
ENSMUST00000118286; ENSMUSP00000113251; ENSMUSG00000027668.
GeneIDi67414.
KEGGimmu:67414.
UCSCiuc008owi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY174062 mRNA. Translation: AAO34660.1.
AK009490 mRNA. Translation: BAC25260.1. Different initiation.
AK018181 mRNA. Translation: BAB31111.1.
AK141611 mRNA. Translation: BAE24764.1.
BC002133 mRNA. Translation: AAH02133.1.
BC047050 mRNA. Translation: AAH47050.1. Different initiation.
BC056641 mRNA. Translation: AAH56641.1.
CCDSiCCDS17296.1.
RefSeqiNP_077162.2. NM_024200.4.
UniGeneiMm.290414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T3JX-ray2.50A660-735[»]
ProteinModelPortaliQ811U4.
SMRiQ811U4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212170. 2 interactors.
DIPiDIP-60969N.
IntActiQ811U4. 1 interactor.
STRINGi10090.ENSMUSP00000088801.

PTM databases

iPTMnetiQ811U4.
PhosphoSitePlusiQ811U4.

Proteomic databases

EPDiQ811U4.
MaxQBiQ811U4.
PaxDbiQ811U4.
PeptideAtlasiQ811U4.
PRIDEiQ811U4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091257; ENSMUSP00000088801; ENSMUSG00000027668.
ENSMUST00000118286; ENSMUSP00000113251; ENSMUSG00000027668.
GeneIDi67414.
KEGGimmu:67414.
UCSCiuc008owi.2. mouse.

Organism-specific databases

CTDi55669.
MGIiMGI:1914664. Mfn1.

Phylogenomic databases

eggNOGiKOG0448. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00390000013727.
HOVERGENiHBG052465.
InParanoidiQ811U4.
KOiK06030.
OMAiAMTDEIC.
OrthoDBiEOG091G02ES.
TreeFamiTF314289.

Enzyme and pathway databases

ReactomeiR-MMU-5205685. Pink/Parkin Mediated Mitophagy.

Miscellaneous databases

ChiTaRSiMfn1. mouse.
EvolutionaryTraceiQ811U4.
PROiQ811U4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027668.
CleanExiMM_MFN1.
ExpressionAtlasiQ811U4. baseline and differential.
GenevisibleiQ811U4. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR006884. Fzo/mitofusin_HR2.
IPR030381. G_DYNAMIN_dom.
IPR027088. Mitofusin-1.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF2. PTHR10465:SF2. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMFN1_MOUSE
AccessioniPrimary (citable) accession number: Q811U4
Secondary accession number(s): Q3URC4
, Q811D5, Q8CEY6, Q99M10, Q9D395
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

MFN1 deficient mice die early during embryonic development, due to altered mitochondria morphology, which are fragmented, showing that mitochondrial fusion is essential for embryonic development.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.