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Protein

Mitofusin-1

Gene

Mfn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:14561718, PubMed:12589796). Membrane clustering requires GTPase activity. It may involve a major rearrangement of the coiled coil domains (By similarity). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:14561718). Overexpression induces the formation of mitochondrial networks (in vitro) (PubMed:14561718). Has low GTPase activity (By similarity).By similarity2 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei284GTPBy similarity1
Binding sitei286GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 90GTPBy similarity6
Nucleotide bindingi237 – 240GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to oxygen-glucose deprivation Source: RGD
  • GTP metabolic process Source: UniProtKB
  • intracellular distribution of mitochondria Source: RGD
  • male gonad development Source: RGD
  • mitochondrial fusion Source: UniProtKB
  • mitochondrial membrane fusion Source: UniProtKB
  • mitochondrion localization Source: UniProtKB
  • mitochondrion morphogenesis Source: RGD
  • negative regulation of mitochondrial fission Source: RGD
  • positive regulation of dendritic spine morphogenesis Source: RGD
  • positive regulation of mitochondrial fusion Source: RGD
  • response to calcium ion Source: RGD
  • response to corticosterone Source: RGD
  • response to electrical stimulus Source: RGD
  • response to ethanol Source: RGD
  • response to flavonoid Source: RGD
  • response to fluoride Source: RGD
  • response to hypobaric hypoxia Source: RGD
  • response to manganese ion Source: RGD
  • response to muscle activity Source: RGD
  • response to nutrient levels Source: RGD

Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin-1 (EC:3.6.5.-By similarity)
Alternative name(s):
Mitochondrial transmembrane GTPase FZO1B
Transmembrane GTPase MFN1
Gene namesi
Name:Mfn1
Synonyms:Fzo1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi621460 Mfn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88K → T: Induces partial mitochondria fragmentation; when overexpressed. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276741 – 741Mitofusin-1Add BLAST741

Post-translational modificationi

Ubiquitinated by non-degradative ubiquitin by PRKN (By similarity). Deubiquitination by USP30 inhibits mitochondrial fusion (By similarity). 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 PRKN (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ8R4Z9
PRIDEiQ8R4Z9

PTM databases

iPTMnetiQ8R4Z9
PhosphoSitePlusiQ8R4Z9

Expressioni

Tissue specificityi

Ubiquitous. In brain, it is expressed at weaker level than MFN2, while it is expressed at a higher level than MFN2 in heart and testis. Expressed at high level in elongating spermatids of seminiferous tubules.2 Publications

Interactioni

Subunit structurei

Homodimer, also in the absence of bound GTP. Forms higher oligomers in the presence of a transition state GTP analog (By similarity). Forms homomultimers and heteromultimers with MFN2 (PubMed:14561718). Oligomerization is essential for mitochondrion fusion. Component of a high molecular weight multiprotein complex (By similarity). Interacts with VAT1 (PubMed:17105775).By similarity2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060265

Structurei

3D structure databases

ProteinModelPortaliQ8R4Z9
SMRiQ8R4Z9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 321Dynamin-type GPROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 73Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST65
Regioni82 – 89G1 motifPROSITE-ProRule annotation8
Regioni108 – 109G2 motifPROSITE-ProRule annotation2
Regioni178 – 181G3 motifPROSITE-ProRule annotation4
Regioni237 – 240G4 motifPROSITE-ProRule annotation4
Regioni266G5 motifPROSITE-ProRule annotation1
Regioni338 – 364Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST27
Regioni703 – 734Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili371 – 408Sequence analysisAdd BLAST38
Coiled coili677 – 735Sequence analysisAdd BLAST59

Domaini

A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0448 Eukaryota
COG0699 LUCA
HOVERGENiHBG052465
InParanoidiQ8R4Z9
KOiK21356
PhylomeDBiQ8R4Z9

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR006884 Fzo/mitofusin_HR2
IPR030381 G_DYNAMIN_dom
IPR027088 Mitofusin-1
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PTHR10465:SF2 PTHR10465:SF2, 1 hit
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
PF04799 Fzo_mitofusin, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q8R4Z9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETVSPLKH FVLAKKAITA IFGQLLEFVT EGSHFVEATY RNPELDRIAT
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 VSPLEARNRI FFVSAKEVLN SRMNKAQGMP
310 320 330 340 350
EGGGALAEGF QARLQEFQNF EQTFEECISQ SAVKTKFEQH TIRAKQILDT
360 370 380 390 400
VKNILDSVNV AAAEKRVYSM EEREDQIDRL DFIRNQMNLL TMDVKKKIKE
410 420 430 440 450
VTEEVANKVS CAMTDEICRL SVLVDEFCSE FHPTPSVLKV YKSELNKHIE
460 470 480 490 500
DGMGRNLADR CTSEVNASIL 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
TEKLQMIVKF TSANCSHQVQ QEMATTFARL CQQVDVTQKH LEEEIARLSK
710 720 730 740
EIDQLEKIQN NSKLLRNKAV QLERELENFS KQFLHPSSGE S
Length:741
Mass (Da):83,847
Last modified:June 1, 2002 - v1
Checksum:i39ED084CDD5D27A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB084166 mRNA Translation: BAB90983.1
RefSeqiNP_620432.1, NM_138976.1
UniGeneiRn.160939

Genome annotation databases

GeneIDi192647
KEGGirno:192647
UCSCiRGD:621460 rat

Similar proteinsi

Entry informationi

Entry nameiMFN1_RAT
AccessioniPrimary (citable) accession number: Q8R4Z9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2002
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See 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

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