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Protein

Mitofusin FZO1

Gene

FZO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Essential transmembrane GTPase, which mediates mitochondrial fusion (PubMed:9685359, PubMed:9786948, PubMed:10562274, PubMed:11266460, PubMed:15297626, PubMed:15760898, PubMed:16624808, PubMed:19812251, PubMed:21385840, PubMed:21502136, PubMed:23317502, PubMed:27253069). Fusion proceeds through several steps; first mitochondria are tethered together, then brought into close contact, followed by the formation of a docking ring around contact areas, and finally membrane fusion (PubMed:27253069). Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission, mediated by FZO1 and DNM1, respectively (PubMed:10562274). Functions antagonistically with DNM1 (PubMed:10562274). Probably acts by forming membrane contact sites that mediate mitochondrial membrane fusion (PubMed:27253069). Mitochondrial docking and fusion requires GTP hydrolysis (PubMed:15297626, PubMed:19812251, PubMed:27253069). Mitochondrial fusion promotes also increased lifespan.12 Publications

Miscellaneous

Present with 1000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei408GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi197 – 202GTPBy similarity6
Nucleotide bindingi370 – 373GTPBy similarity4

GO - Molecular functioni

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

GO - Biological processi

  • mitochondrial fusion Source: SGD

Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29123-MONOMER

Protein family/group databases

TCDBi9.B.25.1.1 the mitochondrial inner/outer membrane fusion (mmf) family

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin FZO1 (EC:3.6.5.-1 Publication)
Alternative name(s):
Transmembrane GTPase FZO1
Gene namesi
Name:FZO1
Ordered Locus Names:YBR179C
ORF Names:YBR1241
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR179C
SGDiS000000383 FZO1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole 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 – 705Cytoplasmic1 PublicationAdd BLAST705
Transmembranei706 – 726Helical; Name=11 PublicationAdd BLAST21
Topological domaini727 – 736Mitochondrial intermembrane1 Publication10
Transmembranei737 – 757Helical; Name=21 PublicationAdd BLAST21
Topological domaini758 – 855Cytoplasmic1 PublicationAdd BLAST98

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172V → P: Abolishes fusion function. 1 Publication1
Mutagenesisi195D → A: Abolishes fusion function. 1 Publication1
Mutagenesisi196V → M: Leads to an unusual intermediate mitochondrial morphology described as disorganized tubules in which mitochondria are tubular, distorted, less branched, and poorly distributed throughout the cell. 1 Publication1
Mutagenesisi197N → A: Abolishes fusion function. 1 Publication1
Mutagenesisi200K → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination. No effect on localization or interaction with UGO1. 5 Publications1
Mutagenesisi200K → D: Abolishes respiratory growth. 1 Publication1
Mutagenesisi200K → R: No effect. 1 Publication1
Mutagenesisi201S → N: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications1
Mutagenesisi221T → A: Abolishes fusion function, MDM30-binding and MDM30-dependent ubiquitination, but not localization to mitochondrial outer membrane. 4 Publications1
Mutagenesisi313D → K: Abolishes respiratory growth. 1 Publication1
Mutagenesisi320D → A: Loss of mitochondrial fusion. 1 Publication1
Mutagenesisi327V → T: Impairs GTP Hydrolysis and abolishes fusion function. 1 Publication1
Mutagenesisi335D → K: Abolishes respiratory growth. Restores respiratory growth; when associated with D-464. 1 Publication1
Mutagenesisi371K → A: No effect. 1 Publication1
Mutagenesisi398K → R: Leads to accelerated proteolysis. 1 Publication1
Mutagenesisi464K → D: Abolishes respiratory growth. Restores respiratory growth; when associated with K-335. 1 Publication1
Mutagenesisi464K → R: Abolishes fusion function. 1 Publication1
Mutagenesisi490Y → A or K: No effect. 1 Publication1
Mutagenesisi490Y → P: Abolishes fusion function. 1 Publication1
Mutagenesisi501L → A: Abolishes fusion function; when associated with Ala-504. 1 Publication1
Mutagenesisi504L → A: Abolishes fusion function; when associated with Ala-501. 1 Publication1
Mutagenesisi518L → P: Abolishes fusion function. 1 Publication1
Mutagenesisi523D → H: Abolishes respiratory growth. Restores respiratory growth; when associated with D-780. 1 Publication1
Mutagenesisi538K → P: Abolishes fusion function. 1 Publication1
Mutagenesisi769Y → P: Abolishes fusion function. 1 Publication1
Mutagenesisi773L → P: Abolishes fusion function. 1 Publication1
Mutagenesisi780H → D: No effect. Restores respiratory growth; when associated with H-523. 1 Publication1
Mutagenesisi818E → A or R: No effect. 1 Publication1
Mutagenesisi818E → P: Abolishes respiratory growth. 1 Publication1
Mutagenesisi819L → A: No effect. 1 Publication1
Mutagenesisi819L → P or E: Abolishes fusion function. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276821 – 855Mitofusin FZO1Add BLAST855

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki398Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated at Lys-398 and Lys-464. MDM30 and UGO1 are involved in ubiquitination. Deubiquitinated by UBP2 and UBP12. UBP2 and UBP12 recognize distinct ubiquitin chains on FZO1 that have opposing effects on mitochondrial fusion. UBP2 removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit fusion. UBP12 recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization.5 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP38297
PaxDbiP38297
PRIDEiP38297
TopDownProteomicsiP38297

PTM databases

iPTMnetiP38297

Interactioni

Subunit structurei

Homodimer. Dimerization depends on GTP binding. Binds the cytoplasmic domain of UGO1 which binds MGM1 through its intermembrane space domain. Interacts with MDM30, UBP2 and UBP12. Component of a large multiprotein complex of 800 kDa.9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein homodimerization activity Source: SGD

Protein-protein interaction databases

BioGridi32877, 139 interactors
ComplexPortaliCPX-161 FZO1:MGM1:UGO1 complex
DIPiDIP-5581N
IntActiP38297, 4 interactors
MINTiP38297
STRINGi4932.YBR179C

Structurei

3D structure databases

ProteinModelPortaliP38297
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini184 – 467Dynamin-type GSequence analysisAdd BLAST284

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni91 – 190HRN1 PublicationAdd BLAST100
Regioni484 – 547HR11 PublicationAdd BLAST64
Regioni630 – 843Required for interaction with UGO1Add BLAST214
Regioni769 – 831HR21 PublicationAdd BLAST63

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili798 – 825Sequence analysisAdd BLAST28

Domaini

The GTPase domain may regulate the interaction with UGO1 since FZO1 lacking the GTPase domain binds 5-fold higher amount of UGO1 than full-length FZO1. The coiled-coil heptad repeat domains HRN, HR1 and HR2 are required for the oligomerization and function in mitochondrial fusion.1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000177197
InParanoidiP38297
KOiK06030
OMAiIVVNGFD
OrthoDBiEOG092C0RVE

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

P38297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGKQQFKD SNKPHKDSTD QDDDAATIVP QTLTYSRNEG HFLGSNFHGV
60 70 80 90 100
TDDRTTLFDG EEGRREDDLL PSLRSSNSKA HLISSQLSQW NYNNNRVLLK
110 120 130 140 150
RSILKTQAFM DQLQEENNIR PIFIAANDER EKLHVLQLNI KLDGQYNTKE
160 170 180 190 200
KNGFNIEKKA LSKLFHSQIV SVTNHLNALK KRVDDVSSKV FITGDVNTGK
210 220 230 240 250
SALCNSLLKQ RLLPEDQLPC TNVFSEILEA RENDGIEEVH AIPLNIAPTL
260 270 280 290 300
KEAIDMYSIQ NPKTYEIHTL KELPDLVPQN GKYALLKIYI KDDKRPASTS
310 320 330 340 350
LLRNGTVDIS LIDSPGLNMD SLQTAEVMSR QEEIDLVIFV VNAENQLTLS
360 370 380 390 400
AKEFISLASR EKKLMFFVVK KFDKIRDKQR CKELILKQIR DLSPETYKRA
410 420 430 440 450
ADFVHFVSKN GDELPHYHNE NDNEDHGDRK PDDDPYSSSD PDPDFDSLED
460 470 480 490 500
SLRNFVLKKR SLSKLLPAKT YLSKLLSDII MISKSNMKMY SEEEIKINEQ
510 520 530 540 550
LETLRPEILS ARAKCNDLTT SVDQMAEQTI TMTYNNTKEA LLNALDVPLH
560 570 580 590 600
EYPKYQGLGQ IYDFIFSTEA FIANQIDESI GSSELFAKQK TDLLVKKIYE
610 620 630 640 650
IGKNELGDDF MCERVFRSEL MFRKRKHLIG KRLKVSLSIT DLFAPTWKGF
660 670 680 690 700
LSYLSWQKPV TAPLPDIEGQ TNEGQIGLMK YLGLKNYPLT QYWSRPSLLF
710 720 730 740 750
TSKIPTLTLY FLGSTKVVGN IILNGIKLSS WSSLKKLSVP VIVVGSLLGL
760 770 780 790 800
TYLIHDLPRA LPMNLSIKYK RKLQELDYIH LNAQRTSNEV RDVLRVPTRE
810 820 830 840 850
ILRSCEIIMD KKQITKKELE NKKESNLLSI KFFQSLYEGT VAQKLMVEEI

NLDID
Length:855
Mass (Da):97,808
Last modified:October 1, 1994 - v1
Checksum:iD796DA455E2AE28B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36048 Genomic DNA Translation: CAA85140.1
BK006936 Genomic DNA Translation: DAA07293.1
PIRiS46050
RefSeqiNP_009738.1, NM_001178527.1

Genome annotation databases

EnsemblFungiiYBR179C; YBR179C; YBR179C
GeneIDi852477
KEGGisce:YBR179C

Similar proteinsi

Entry informationi

Entry nameiFZO1_YEAST
AccessioniPrimary (citable) accession number: P38297
Secondary accession number(s): D6VQH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 20, 2018
This is version 145 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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