MARCHF5
entrez
54708
canonical
uniprot
Q9NX47
canonical
ensembl
ENSG00000198060
resolver
ensp
ENSP00000351813
resolver
enst
ENST00000358935
resolver
genesymbol
MARCHF5
resolver
genesymbol_syn
MARCH5
resolver
genesymbol_syn
RNF153
resolver
hgnc
HGNC:26025
resolver
uniprot_entry
MARH5_HUMAN
resolver
amino_acid_sequence
MPDQALQQMLDRSCWVCFATDEDDRTAEWVRPCRCRGSTKWVHQACLQRWVDEKQRGNSTARVACPQCNAEYLIVFPKLGPVVYVLDLADRLISKACPFAAAGIMVGSIYWTAVTYGAVTVMQVVGHKEGLDVMERADPLFLLIGLPTIPVMLILGKMIRWEDYVLRLWRKYSNKLQILNSIFPGIGCPVPRIPAEANPLADHVSATRILCGALVFPTIATIVGKLMFSSVNSNLQRTILGGIAFVAIKGAFKVYFKQQQYLRQAHRKILNYPEQEEA
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission and as an important regulator of immune response (PubMed:16874301, PubMed:17606867, PubMed:26246171, PubMed:31881323). Plays a crucial role in maintaining mitochondrial homeostasis by regulating the dynamics of mitochondria through the ubiquitination of key proteins involved in fission and fusion such as FIS1, DNM1L and MFN1 (PubMed:16874301, PubMed:17606867). Acts as a critical determinant of mitotic apoptosis through both MCL1-dependent and -independent pathways (By similarity). Turns off persistent immune signaling by degrading oligomeric complexes of retinoic acid-inducible gene I/DDX58 and mitochondrial antiviral-signaling protein/MAVS formed upon RNA virus infection (PubMed:26246171, PubMed:31881323, PubMed:40071916). Promotes STING-mediated type-I interferon production via 'Lys-63'-linked ubiquitination of STING1 thereby preserving its activity and preventing the formation of inactive STING1 polymers (PubMed:37916870). Plays also an essential role in the formation of PEX3-containing vesicles in the de novo biogenesis of peroxisomes from mitochondria (PubMed:39423820, PubMed:39423819). Acts as a regulator of NLRP3 inflammasome activation on the mitochondria by mediating the 'Lys-27'-linked polyubiquitination of NLRP3, positively regulating the NLRP3-NEK7 complex formation and NLRP3 oligomerization (PubMed:37575012). {ECO:0000250|UniProtKB:Q3KNM2, ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:20103533, ECO:0000269|PubMed:37575012, ECO:0000269|PubMed:37916870, ECO:0000269|PubMed:39423819, ECO:0000269|PubMed:39423820, ECO:0000269|PubMed:40071916}.; FUNCTION: (Microbial infection) Plays a positive role in Japanese encephalitis virus infection by catalyzing the 'Lys-27'-linked polyubiquitination of viral E protein to facilitate efficient viral attachment. {ECO:0000269|PubMed:40071916}.
uniprot
proteins
mass_dalton
31232
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="H->W: Loss of ubiquitin ligase activity, formation of highly interconnected mitochondria, change in mitochondria morphology that in turns triggers senescence, and perinuclear accumulation."; /evidence="ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:20103533, ECO:0000269|PubMed:26246171"; MUTAGEN 65; /note="C->S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-68."; /evidence="ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867"; MUTAGEN 68; /note="C->S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-65."; /evidence="ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated leading to degradation (short half-life). {ECO:0000269|PubMed:16874301}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14722266
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16874301
uniprot
proteins
pubmed
16936636
uniprot
proteins
pubmed
17606867
uniprot
proteins
pubmed
19741096
uniprot
proteins
pubmed
20103533
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26246171
uniprot
proteins
pubmed
31881323
uniprot
proteins
pubmed
37575012
uniprot
proteins
pubmed
37916870
uniprot
proteins
pubmed
39423819
uniprot
proteins
pubmed
39423820
uniprot
proteins
pubmed
40071916
uniprot
proteins
sequence_length
278
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:16874301}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:37916870}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:39423819}. Note=Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301). {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:16874301}.
uniprot
proteins
transmembrane_region
TRANSMEM 99..119; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 139..159; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins