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Q811U4 (MFN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitofusin-1

EC=3.6.5.-
Alternative name(s):
Transmembrane GTPase MFN1
Gene names
Name:Mfn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

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. Ref.1 Ref.6

Subcellular location

Mitochondrion outer membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Widely expressed. Ref.4

Developmental stage

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

Post-translational modification

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 By similarity.

Disruption phenotype

In cardiomyocytes, no effect on mitochondrial morphometry or respiratory function. Ref.5

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.

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Sequence caution

The sequence AAH47050.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC25260.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0073EBI-9029118,EBI-5323863From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Mitofusin-1
PRO_0000127673

Regions

Topological domain1 – 584584Cytoplasmic Potential
Transmembrane585 – 60521Helical; Name=1; Potential
Topological domain606 – 6083Mitochondrial intermembrane Potential
Transmembrane609 – 62921Helical; Name=2; Potential
Topological domain630 – 741112Cytoplasmic Potential
Domain72 – 321250Dynamin-type G
Nucleotide binding82 – 898GTP Probable
Nucleotide binding178 – 1825GTP Probable
Nucleotide binding237 – 2404GTP Probable
Coiled coil371 – 40838 Ref.6
Coiled coil677 – 73559 Ref.6

Experimental info

Sequence conflict2091E → G in BAB31111. Ref.2
Sequence conflict328 – 3292IS → VL in BAB31111. Ref.2
Sequence conflict3351T → A in BAB31111. Ref.2
Sequence conflict5211V → A in BAB31111. Ref.2
Sequence conflict5881L → W in BAB31111. Ref.2
Sequence conflict6191L → S in BAB31111. Ref.2
Sequence conflict7181K → R in BAB31111. Ref.2
Sequence conflict7201V → I in AAH02133. Ref.3
Sequence conflict7201V → I in AAH56641. Ref.3

Secondary structure

... 741
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q811U4 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 36E5E90DB0C0D5A1

FASTA74183,726
        10         20         30         40         50         60 
MAETVSPLKH FVLAKKAITA IFGQLLEFVT EGSHFVEATY RNPELDRIAS EDDLVEIQGY 

        70         80         90        100        110        120 
RNKLAVIGEV LSRRHMKVAF FGRTSSGKSS VINAMLWDKV LPSGIGHTTN CFLSVEGTDG 

       130        140        150        160        170        180 
DKAYLMTEGS DEKKSVKTVN QLAHALHMDK DLKAGCLVHV FWPKAKCALL RDDLVLVDSP 

       190        200        210        220        230        240 
GTDVTTELDI WIDKFCLDAD VFVLVANSES TLMNTEKHFF HKVNERLSKP NIFILNNRWD 

       250        260        270        280        290        300 
ASASEPEYME DVRRQHMERC LHFLVEELKV VSPSEARNRI FFVSAKEVLN SRKHKAQGMP 

       310        320        330        340        350        360 
EGGGALAEGF QARLQEFQNF EQTFEECISQ SAVKTKFEQH TIRAKQILDT VKNILDSVNV 

       370        380        390        400        410        420 
AAAEKRVYSM EEREDQIDRL DFIRNQMNLL TLDVKKKIKE VTEEVANKVS CAMTDEICRL 

       430        440        450        460        470        480 
SVLVDEFCSE FHPTPSVLKV YKSELNKHIE DGMGRNLADR CTNEVNASIL QSQQEIIENL 

       490        500        510        520        530        540 
KPLLPAGIQN KLHTLIPCKK FDLSYDLNCH KLCSDFQEDI VFRFSLGWSS LVHRFLGSTN 

       550        560        570        580        590        600 
AQRVLLGLSE PIFQVPRSLA STPTAPSNPA APDNAAQEEL MITLITGLAS LTSRTSMGII 

       610        620        630        640        650        660 
VVGGVIWKTV GWKLISVTLS MYGALYLYER LTWTTRAKER AFKQQFVNYA TEKLQMIVSF 

       670        680        690        700        710        720 
TSANCSHQVQ QEMATTFARL CQQVDVTQKH LEEEIARLSK EIDQLEKIQN NSKLLRNKAV 

       730        740 
QLESELENFS KQFLHPSSGE S 

« Hide

References

« Hide 'large scale' references
[1]"Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development."
Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., Chan D.C.
J. Cell Biol. 160:189-200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, MULTIMERIZATION.
Strain: FVB.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Hippocampus, Medulla oblongata and Tongue.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver and Mammary tumor.
[4]"Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo."
Rojo M., Legros F., Chateau D., Lombes A.
J. Cell Sci. 115:1663-1674(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."
Chen Y., Dorn G.W. II
Science 340:471-475(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[6]"Structural basis of mitochondrial tethering by mitofusin complexes."
Koshiba T., Detmer S.A., Kaiser J.T., Chen H., McCaffery J.M., Chan D.C.
Science 305:858-862(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 660-735, FUNCTION, SUBUNIT, COILED-COIL DOMAINS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17296.1.
RefSeqNP_077162.2. NM_024200.4.
UniGeneMm.290414.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3JX-ray2.50A660-735[»]
ProteinModelPortalQ811U4.
SMRQ811U4. Positions 674-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212170. 2 interactions.
IntActQ811U4. 1 interaction.

PTM databases

PhosphoSiteQ811U4.

Proteomic databases

MaxQBQ811U4.
PaxDbQ811U4.
PRIDEQ811U4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091257; ENSMUSP00000088801; ENSMUSG00000027668.
ENSMUST00000118286; ENSMUSP00000113251; ENSMUSG00000027668.
GeneID67414.
KEGGmmu:67414.
UCSCuc008owi.2. mouse.

Organism-specific databases

CTD55669.
MGIMGI:1914664. Mfn1.

Phylogenomic databases

eggNOGCOG0699.
GeneTreeENSGT00390000013727.
HOVERGENHBG052465.
InParanoidQ3URC4.
KOK06030.
OMAAMTDEIC.
OrthoDBEOG7HB58M.
TreeFamTF314289.

Gene expression databases

ArrayExpressQ811U4.
BgeeQ811U4.
CleanExMM_MFN1.
GenevestigatorQ811U4.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR001401. Dynamin_GTPase.
IPR006884. Fzo/mitofusin_HR2.
IPR027088. Mitofusin-1.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF2. PTHR10465:SF2. 1 hit.
PfamPF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMFN1. mouse.
EvolutionaryTraceQ811U4.
NextBio324498.
PROQ811U4.
SOURCESearch...

Entry information

Entry nameMFN1_MOUSE
AccessionPrimary (citable) accession number: Q811U4
Secondary accession number(s): Q3URC4 expand/collapse secondary AC list , Q811D5, Q8CEY6, Q99M10, Q9D395
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot