Fundc1
entrez
72018
canonical
uniprot
Q9DB70
canonical
ensembl
ENSMUSG00000025040
resolver
ensp
ENSMUSP00000026016
resolver
ensp
ENSMUSP00000134878
resolver
ensp
ENSMUSP00000135026
resolver
ensp
ENSMUSP00000135183
resolver
ensp
ENSMUSP00000292836
resolver
enst
ENSMUST00000026016
resolver
enst
ENSMUST00000142638
resolver
enst
ENSMUST00000176638
resolver
enst
ENSMUST00000177213
resolver
genesymbol
Fundc1
resolver
uniprot
A2BEA3
resolver
uniprot
H3BJ77
resolver
uniprot
H3BJZ1
resolver
uniprot_entry
FUND1_MOUSE
resolver
uniprot_entry
H3BJ77_MOUSE
resolver
uniprot_entry
H3BJZ1_MOUSE
resolver
uniprot_sec
A2BEA3
resolver
amino_acid_sequence
MASRNPPPQDYESDDESYEVLDLTEYARRHHWWNRVFGHSSGPMVEKYSVATQIVMGGVTGWCAGFLFQKVGKLAATAVGGGFLLLQVASHSGYVQIDWKRVEKDVNKAKRQIKKRANKAAPEINNIIEEATDFIKQNIVISSGFVGGFLLGLAS
uniprot
proteins
function
FUNCTION: Integral mitochondrial outer-membrane protein that mediates the formation of mitochondria-associated endoplasmic reticulum membranes (MAMs). In turn, mediates angiogenesis and neoangiogenesis through interference with intracellular Ca(2+) communication and regulation of the vascular endothelial growth factor receptor KDR/VEGFR2 expression at both mRNA and protein levels. Also acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality and homeostasis, by interacting with and recruiting LC3 protein family to mitochondria. Mechanistically, recruits DRP1 at ER-mitochondria contact sites leading to DRP1 oligomerization and GTPase activity to facilitate mitochondrial fission during hypoxia (By similarity). Additionally, plays a role in hepatic ferroptosis by interacting directly with glutathione peroxidase/GPX4 to facilitate its recruitment into mitochondria through TOM/TIM complex where it is degraded by mitophagy (PubMed:36828120). {ECO:0000250|UniProtKB:Q8IVP5, ECO:0000269|PubMed:36828120}.
uniprot
proteins
mass_dalton
17159
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-13 by CK2 and at Tyr-18 by SRC inhibits activation of mitophagy. Following hypoxia, dephosphorylated at Tyr-18, leading to interaction with MAP1 LC3 family proteins and triggering mitophagy. Dephosphorylation is mediated by PGAM5. Phosphorylated by ULK1 at Ser-17 which enhances FUNDC1 binding to LC3. {ECO:0000250|UniProtKB:Q8IVP5}.; PTM: Ubiquitinated on Lys-119. Deubiquitinated by USP19; leading to hypoxia-induced DRP1 oligomerization and GTPase activity. {ECO:0000250|UniProtKB:Q8IVP5}.
uniprot
proteins
protein_family
FUN14 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
36828120
uniprot
proteins
sequence_length
155
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8IVP5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IVP5}.
uniprot
proteins
transmembrane_region
TRANSMEM 48..68; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 75..95; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 134..154; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins