Q8R500
uniprot
Q8R500
canonical
amino_acid_sequence
MSLLFSRCNSIVTVKKDKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESAGFLEDTHRNTELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVGGTDGHEAFLLTEGSEEKKSVKTVNQLAHALHQDEQLHAGSLVSVMWPNSKCPLLKDGLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKQFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRAQAGDRIFFVSAKEVLSARVQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHIAAQEQRVYCLEMREERQDRLRFIDKQLELLAQDYKLRIKQMTEEVERQVSTAMAEEIRRLSVLVDEYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAIASSLQTMQQDMIDGLKPLLPVSVRNQIDMLVPRQCFSLSYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALLGYNDQVQRPLPLTPANPSMPPLPQGSLTQEELMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTRAKERAFKRQFVEYASEKLQLIISYTGSNCSHQVQQELSGTFAHLCQQVDITRDNLEQEIAAMNKKVEALDSLQSKAKLLRNKAGWLDSELNMFIHQYLQPSR
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12589796, PubMed:12598526, PubMed:14561718, PubMed:15322553). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events. Overexpression induces the formation of mitochondrial networks. Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (By similarity). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (PubMed:12598526). Plays an important role in the regulation of vascular smooth muscle cell proliferation (PubMed:15322553). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PRKN recruitment to dysfunctional mitochondria (By similarity). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity). {ECO:0000250|UniProtKB:O95140, ECO:0000250|UniProtKB:Q80U63, ECO:0000269|PubMed:12589796, ECO:0000269|PubMed:12598526, ECO:0000269|PubMed:14561718, ECO:0000269|PubMed:15322553}.
uniprot
proteins
mass_dalton
86123
uniprot
proteins
mutagenesis
MUTAGEN 109; /note="K->T: Induces mitochondria fragmentation when overexpressed."; /evidence="ECO:0000269|PubMed:14561718
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PINK1. {ECO:0000250|UniProtKB:O95140}.; PTM: Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (By similarity). Ubiquitinated by HUWE1 when dietary stearate (C18:0) levels are low; ubiquitination inhibits mitochondrial fusion (By similarity). {ECO:0000250|UniProtKB:O95140}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
Mitofusin subfamily
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
12589796
uniprot
proteins
pubmed
12598526
uniprot
proteins
pubmed
14561718
uniprot
proteins
pubmed
14592431
uniprot
proteins
pubmed
15322553
uniprot
proteins
pubmed
17105775
uniprot
proteins
sequence_length
757
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:14561718, ECO:0000269|PubMed:15322553}; Multi-pass membrane protein {ECO:0000269|PubMed:14561718}. Note=Colocalizes with BAX during apoptosis. {ECO:0000250|UniProtKB:O95140}.
uniprot
proteins
transmembrane_region
TRANSMEM 605..625; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 627..647; /note="Helical; Name=2"; /evidence="ECO:0000255
uniprot
proteins