MIEF1
entrez
54471
canonical
uniprot
Q9NQG6
canonical
ensembl
ENSG00000100335
resolver
ensp
ENSP00000327124
resolver
ensp
ENSP00000385110
resolver
enst
ENST00000402881
resolver
genesymbol
MIEF1
resolver
genesymbol_syn
MID51
resolver
genesymbol_syn
SMCR7L
resolver
hgnc
HGNC:25979
resolver
uniprot
B0QY95
resolver
uniprot
Q52MA5
resolver
uniprot
Q7L890
resolver
uniprot
Q9BUI3
resolver
uniprot_entry
B0QY95_HUMAN
resolver
uniprot_entry
MID51_HUMAN
resolver
uniprot_sec
Q52MA5
resolver
uniprot_sec
Q7L890
resolver
uniprot_sec
Q9BUI3
resolver
amino_acid_sequence
MAGAGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSPTRLSHSGKRSWEEPNWMGSPRLLNRDMKTGLSRSLQTLPTDSSTFDTDTFCPPRPKPVARKGQVDLKKSRLRMSLQEKLLTYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMPLRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCIPGEDTIMNVPGFFLVRRENPEYFPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPPPEALTLEVQYERDKHLFIDFLPSVTLGDTVLVAKPHRLAQYDNLWRLSLRPAETARLRALDQADSGCRSLCLKILKAICKSTPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLEAGVLPSALNPKVNLFAELTPEEIDELGYTLYCSLSEPEVLLQT
uniprot
proteins
disease_involvement
DISEASE: Optic atrophy 14 (OPA14) [MIM:620550]: A disease characterized by visual impairment in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA14 is an autosomal dominant form characterized by adult-onset progressive reduction in visual acuity, and pale and excavated optic disk. Optical coherence tomography discloses a severe loss of the retinal nerve fiber layer. {ECO:0000269|PubMed:33632269}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission/fusion dynamics (PubMed:21701560, PubMed:23921378, PubMed:33632269). Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L. {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:24515348, ECO:0000269|PubMed:29083303, ECO:0000269|PubMed:33632269}.
uniprot
proteins
mass_dalton
51293
uniprot
proteins
mutagenesis
MUTAGEN 201; /note="H->D: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with E-342; E-368 and E-372."; /evidence="ECO:0000269|PubMed:24515348"; MUTAGEN 235; /note="R->A: No effect on mitochondrial localization. Impairs DNM1L recruitment."; /evidence="ECO:0000269|PubMed:24515348"; MUTAGEN 238..242; /note="Missing: No effect on mitochondrial localization. Impairs DNM1L recruitment."; /evidence="ECO:0000269|PubMed:24515348"; MUTAGEN 342; /note="R->E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-368 and E-372."; /evidence="ECO:0000269|PubMed:24515348"; MUTAGEN 368; /note="K->E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-372."; /evidence="ECO:0000269|PubMed:24515348"; MUTAGEN 372; /note="K->E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-368."; /evidence="ECO:0000269|PubMed:24515348
uniprot
proteins
protein_family
SMCR7 family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
12529303
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
21508961
uniprot
proteins
pubmed
21701560
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23283981
uniprot
proteins
pubmed
23530241
uniprot
proteins
pubmed
23921378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24515348
uniprot
proteins
pubmed
25621764
uniprot
proteins
pubmed
29083303
uniprot
proteins
pubmed
31666358
uniprot
proteins
pubmed
33632269
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}; Single-pass membrane protein {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..46; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins