OPA1
entrez
4976
canonical
uniprot
O60313
canonical
ensembl
ENSG00000198836
resolver
ensp
ENSP00000354429
resolver
ensp
ENSP00000354681
resolver
ensp
ENSP00000354781
resolver
ensp
ENSP00000355311
resolver
ensp
ENSP00000355324
resolver
ensp
ENSP00000376232
resolver
ensp
ENSP00000493673
resolver
ensp
ENSP00000494512
resolver
ensp
ENSP00000495028
resolver
ensp
ENSP00000560816
resolver
ensp
ENSP00000677187
resolver
ensp
ENSP00000749872
resolver
ensp
ENSP00000783967
resolver
enst
ENST00000361715
resolver
genesymbol
OPA1
resolver
genesymbol_syn
KIAA0567
resolver
hgnc
HGNC:8140
resolver
uniprot
D3DNW4
resolver
uniprot
E5KLJ5
resolver
uniprot
E5KLJ6
resolver
uniprot
E5KLJ7
resolver
uniprot
E5KLJ9
resolver
uniprot
E5KLK0
resolver
uniprot
E5KLK1
resolver
uniprot
E5KLK2
resolver
uniprot_entry
E5KLJ9_HUMAN
resolver
uniprot_entry
E5KLK0_HUMAN
resolver
uniprot_entry
OPA1_HUMAN
resolver
uniprot_sec
D3DNW4
resolver
uniprot_sec
E5KLJ5
resolver
uniprot_sec
E5KLJ6
resolver
uniprot_sec
E5KLJ7
resolver
uniprot_sec
E5KLK1
resolver
uniprot_sec
E5KLK2
resolver
activity_regulation
ACTIVITY REGULATION: Activated by guanine nucleotide exchange factor RCC1L. {ECO:0000269|PubMed:28746876}.
uniprot
proteins
amino_acid_sequence
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
uniprot
proteins
disease_involvement
DISEASE: Optic atrophy 1 (OPA1) [MIM:165500]: A condition that features progressive visual loss 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. OPA1 is characterized by an insidious onset of visual impairment in early childhood with moderate to severe loss of visual acuity, temporal optic disk pallor, color vision deficits, and centrocecal scotoma of variable density. {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11440988, ECO:0000269|PubMed:11440989, ECO:0000269|PubMed:11810270, ECO:0000269|PubMed:12036970, ECO:0000269|PubMed:12566046, ECO:0000269|PubMed:14961560, ECO:0000269|PubMed:15948788, ECO:0000269|PubMed:16513463, ECO:0000269|PubMed:16617242, ECO:0000269|PubMed:18204809, ECO:0000269|PubMed:18360822, ECO:0000269|PubMed:19319978, ECO:0000269|PubMed:19325939, ECO:0000269|PubMed:19969356, ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:22382025, ECO:0000269|PubMed:22857269, ECO:0000269|PubMed:23401657, ECO:0000269|PubMed:32228866}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Optic atrophy plus syndrome (DOA+) [MIM:125250]: An autosomal dominant neurologic disorder characterized most commonly by an insidious onset of visual loss and sensorineural hearing loss in childhood with variable presentation of other clinical manifestations including progressive external ophthalmoplegia, muscle cramps, hyperreflexia, and ataxia. There appears to be a wide range of intermediate phenotypes. {ECO:0000269|PubMed:15531309, ECO:0000269|PubMed:16240368, ECO:0000269|PubMed:18065439, ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:18195150, ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:21112924, ECO:0000269|PubMed:23387428}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Behr syndrome (BEHRS) [MIM:210000]: An autosomal recessive syndrome characterized by optic atrophy beginning in early childhood associated with ataxia, pyramidal signs, spasticity, intellectual disability, and posterior column sensory loss. The ataxia, spasticity, and muscle contractures, mainly of the hip adductors, hamstrings, and soleus, are progressive and become more prominent in the second decade. {ECO:0000269|PubMed:21636302, ECO:0000269|PubMed:25012220, ECO:0000269|PubMed:25146916}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 14B, cardioencephalomyopathic type (MTDPS14B) [MIM:616896]: An autosomal recessive mitochondrial disorder characterized by lethal infantile encephalopathy, hypertrophic cardiomyopathy and optic atrophy. Skeletal muscle biopsies show significant mtDNA depletion and abnormal mitochondria. {ECO:0000269|PubMed:26561570}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 14A, encephalomyopathic type (MTDPS14A) [MIM:621481]: An autosomal dominant mitochondrial disorder characterized by infantile-onset psychomotor delay, hypotonia, spasticity, seizures, encephalopathy, and other neurologic signs resembling those of Leigh syndrome. {ECO:0000269|PubMed:39233737}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.5
uniprot
proteins
function
FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function (PubMed:16778770, PubMed:17709429, PubMed:20185555, PubMed:24616225, PubMed:28628083, PubMed:28746876, PubMed:31922487, PubMed:32228866, PubMed:32567732, PubMed:33130824, PubMed:33237841, PubMed:37612504, PubMed:37612506). Exists in two forms: the transmembrane, long form (Dynamin-like GTPase OPA1, long form; L-OPA1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1), which results from proteolytic cleavage and localizes in the intermembrane space (PubMed:31922487, PubMed:32228866, PubMed:33237841, PubMed:37612504, PubMed:37612506). Both forms (L-OPA1 and S-OPA1) cooperate to catalyze the fusion of the mitochondrial inner membrane (PubMed:31922487, PubMed:37612504, PubMed:37612506). The equilibrium between L-OPA1 and S-OPA1 is essential: excess levels of S-OPA1, produced by cleavage by OMA1 following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, inhibiting mitochondrial fusion (PubMed:20038677, PubMed:31922487). The balance between L-OPA1 and S-OPA1 also influences cristae shape and morphology (By similarity). Involved in remodeling cristae and the release of cytochrome c during apoptosis (By similarity). Proteolytic processing by PARL in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space (By similarity). Acts as a regulator of T-helper Th17 cells, which are characterized by cells with fused mitochondria with tight cristae, by mediating mitochondrial membrane remodeling: OPA1 is required for interleukin-17 (IL-17) production (By similarity). Its role in mitochondrial morphology is required for mitochondrial genome maintenance (PubMed:18158317, PubMed:20974897). {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32567732, ECO:0000269|PubMed:33130824, ECO:0000269|PubMed:33237841, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Dynamin-like GTPase OPA1, long form]: Constitutes the transmembrane long form (L-OPA1) that plays a central role in mitochondrial inner membrane fusion and cristae morphology (PubMed:31922487, PubMed:32228866, PubMed:37612504, PubMed:37612506). L-OPA1 and the soluble short form (S-OPA1) form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (PubMed:31922487, PubMed:37612504, PubMed:37612506). Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (PubMed:37612504, PubMed:37612506). Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature (PubMed:37612504, PubMed:37612506). OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:28628083, PubMed:37612504, PubMed:37612506). Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area (PubMed:32567732, PubMed:33130824). Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions (By similarity). The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape (By similarity). {ECO:0000250|UniProtKB:G0SGC7, ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32567732, ECO:0000269|PubMed:33130824, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Dynamin-like GTPase OPA1, short form]: Constitutes the soluble short form (S-OPA1) generated by cleavage by OMA1, which plays a central role in mitochondrial inner membrane fusion and cristae morphology (PubMed:31922487, PubMed:32228866, PubMed:32245890, PubMed:37612504, PubMed:37612506). The transmembrane long form (L-OPA1) and the S-OPA1 form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (PubMed:31922487, PubMed:32228866, PubMed:37612504, PubMed:37612506). Inner membrane-anchored L-OPA1 molecules initiate membrane remodeling by recruiting soluble S-OPA1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (PubMed:32228866, PubMed:37612504, PubMed:37612506). Once at the membrane surface, the formation of S-OPA1 helices induce bilayer curvature (PubMed:37612504, PubMed:37612506). OPA1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible OPA1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:28628083, PubMed:37612504, PubMed:37612506). Excess levels of S-OPA1 produced by cleavage by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, thereby inhibiting mitochondrial fusion (PubMed:20038677). Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization by mediating flickering: cleavage by OMA1 leads to excess production of S-OPA1, preventing mitochondrial hyperfusion (By similarity). Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area (PubMed:32245890). Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions (By similarity). The equilibrium between L-OPA1 and S-OPA1 influences cristae shape and morphology: increased L-OPA1 levels promote cristae stacking and elongated mitochondria, while increased S-OPA1 levels correlated with irregular cristae packing and round mitochondria shape (By similarity). {ECO:0000250|UniProtKB:G0SGC7, ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:31922487, ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32245890, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.; FUNCTION: [Isoform 1]: Coexpression of isoform 1 with shorter alternative products is required for optimal activity in promoting mitochondrial fusion. {ECO:0000269|PubMed:17709429}.; FUNCTION: [Isoform 4]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.; FUNCTION: [Isoform 5]: Isoforms that contain the alternative exon 4b are required for mitochondrial genome maintenance, possibly by anchoring the mitochondrial nucleoids to the inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.
uniprot
proteins
mass_dalton
111631
uniprot
proteins
mutagenesis
MUTAGEN 213; /note="E->A: In interface mutant 9; strongly decreased ability to mediate mitochondrial fusion; when associated with A-217, A-557 and A-565."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 217; /note="Q->A: In interface mutant 9; strongly decreased ability to mediate mitochondrial fusion; when associated with A-213, A-557 and A-565."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 235; /note="R->A: In interface mutant 8; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 243; /note="L->A: In mutant control 1; does not affect ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 248; /note="L->A: In mutant control 2; does not affect ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 297; /note="Q->E: Abolished GTPase activity without affecting the ability to bind membranes."; /evidence="ECO:0000269|PubMed:32228866"; MUTAGEN 298; /note="S->A: Abolished GTPase activity without affecting the ability to bind membranes."; /evidence="ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:32379273"; MUTAGEN 301; /note="K->A: Abolished GTPase activity."; /evidence="ECO:0000269|PubMed:32245890"; MUTAGEN 302; /note="T->A: Abolished GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 302; /note="T->N: Abolished GTPase activity without affecting the ability to bind membranes."; /evidence="ECO:0000269|PubMed:32228866"; MUTAGEN 316; /note="R->A: Strongly decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 320; /note="E->A: Decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 321; /note="M->A: Strongly decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 322; /note="M->A: Decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 323; /note="T->A: Abolished GTPase activity."; /evidence="ECO:0000269|PubMed:28628083, ECO:0000269|PubMed:32379273"; MUTAGEN 324; /note="R->A: Strongly decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 359; /note="L->A: In mutant control 3; does not affect ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 398; /note="D->A: Strongly decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 444; /note="E->A: In interface mutant 5; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 503; /note="T->A: Decreased GTPase activity."; /evidence="ECO:0000269|PubMed:32379273"; MUTAGEN 557; /note="R->A: In interface mutant 9; strongly decreased ability to mediate mitochondrial fusion; when associated with A-213, A-217 and A-565."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 565; /note="D->A: In interface mutant 9; strongly decreased ability to mediate mitochondrial fusion; when associated with A-213, A-217 and A-557."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 614..615; /note="KH->AA: In interface mutant 2; strongly decreased ability to mediate mitochondrial fusion; when associated with A-835."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 626; /note="E->A: In interface mutant 1b; strongly decreased ability to mediate mitochondrial fusion; when associated with A-630, A-668 and A-671."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 627; /note="R->A: In interface mutant 1a; strongly decreased ability to mediate mitochondrial fusion; when associated with A-663 and A-683."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 630; /note="T->A: In interface mutant 1b; strongly decreased ability to mediate mitochondrial fusion; when associated with A-626, A-668 and A-671."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 631; /note="H->A: In interface mutant 1e; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 651; /note="T->A: In mutant control 4; does not affect ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 659; /note="Q->A: In interface mutant 1c; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 663; /note="K->A: In interface mutant 1a; strongly decreased ability to mediate mitochondrial fusion; when associated with A-627 and A-683."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 668; /note="K->A: In interface mutant 1b; strongly decreased ability to mediate mitochondrial fusion; when associated with A-626, A-630 and A-671."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 671; /note="E->A: In interface mutant 1b; strongly decreased ability to mediate mitochondrial fusion; when associated with A-626, A-630 and A-668."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 683; /note="R->A: In interface mutant 1a; strongly decreased ability to mediate mitochondrial fusion; when associated with A-627 and A-663."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 716; /note="D->A: In interface mutant 6; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 735; /note="I->A: In interface mutant 4b; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 738; /note="K->E: Abolished ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 760; /note="E->A: In interface mutant 1d; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 771..781; /note="WKKRWLYWKNR->AAAAAAAAAAA: In P-alpha-2 membrane insertion mutant; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 771; /note="W->A: Abolished ability to bind and bend membranes."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 772; /note="K->E: Abolished ability to bind and bend membranes."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 774; /note="R->E: Abolished ability to bind and bend membranes."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 775; /note="W->A: Does not affect ability to bind and bend membranes."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 779; /note="K->E: Decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 781; /note="R->E: Abolished ability to bind and bend membranes."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 794..796; /note="ELE->ALA: Decreased ability to bind membranes."; /evidence="ECO:0000269|PubMed:32228866"; MUTAGEN 795..799; /note="LEKML->AKALA,EKELE: Decreased ability to bind membranes."; /evidence="ECO:0000269|PubMed:32228866"; MUTAGEN 797..800; /note="KMLK->AMLA: Abolished GTPase activity and ability to bend membranes."; /evidence="ECO:0000269|PubMed:32228866"; MUTAGEN 819..820; /note="KN->AA: In interface mutant 7; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 819; /note="K->E: Abolished ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 835; /note="D->A: In interface mutant 2; strongly decreased ability to mediate mitochondrial fusion; when associated with 614-A-A-615."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN 858; /note="R->E: Abolished ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612504"; MUTAGEN 860..867; /note="FYYYQRHF->AAAAAAAA: In interface mutant 4a; strongly decreased ability to mediate mitochondrial fusion."; /evidence="ECO:0000269|PubMed:37612506"; MUTAGEN O60313-10:195..204; /note="Missing: Abolished cleavage at position S3."; /evidence="ECO:0000269|PubMed:33237841"; MUTAGEN O60313-10:200..204; /note="Missing: Abolished cleavage at position S3."; /evidence="ECO:0000269|PubMed:33237841"; MUTAGEN O60313-11:195..204; /note="Missing: Abolished cleavage at position S3."; /evidence="ECO:0000269|PubMed:21081504"; MUTAGEN O60313-11:200..204; /note="Missing: Abolished cleavage at position S3."; /evidence="ECO:0000269|PubMed:21081504
uniprot
proteins
post_translational_modification
PTM: Cleaved by OMA1 or YME1L1 downstream of the transmembrane region in response to different signals to generate soluble forms (PubMed:16778770, PubMed:17709429, PubMed:20038677, PubMed:24616225, PubMed:27495975, PubMed:33237841). Cleaved by OMA1 at position S1 following stress conditions, generating the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1) (PubMed:20038677). AFG3L2 is involved in the regulation of OMA1-dependent processing of OPA1 (PubMed:17615298). PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion (By similarity). {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17615298, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:20038677, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:33237841}.; PTM: [Isoform 2]: Cleavage at position S2 by YME1L1 is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975}.; PTM: [Isoform 3]: Cleavage at position S2 by YME1L1 is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975}.; PTM: [Isoform 4]: Cleavage at position S2 by YME1L1 is required to mediate oxidative phosphorylation (OXPHOS)-induced mitochondrial fusion (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage occurs in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (PubMed:16778770). Cleavage at position S3 by YME1L1 is required for membrane tubulation (PubMed:33237841). {ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975, ECO:0000269|PubMed:33237841}.; PTM: [Isoform 5]: Cleavage at position S3 by YME1L1 is required for membrane tubulation. {ECO:0000269|PubMed:33237841}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
11017079
uniprot
proteins
pubmed
11017080
uniprot
proteins
pubmed
11440988
uniprot
proteins
pubmed
11440989
uniprot
proteins
pubmed
11810270
uniprot
proteins
pubmed
12036970
uniprot
proteins
pubmed
12566046
uniprot
proteins
pubmed
14961560
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15531309
uniprot
proteins
pubmed
15948788
uniprot
proteins
pubmed
16240368
uniprot
proteins
pubmed
16513463
uniprot
proteins
pubmed
16617242
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16778770
uniprot
proteins
pubmed
17615298
uniprot
proteins
pubmed
17709429
uniprot
proteins
pubmed
18065439
uniprot
proteins
pubmed
18158317
uniprot
proteins
pubmed
18195150
uniprot
proteins
pubmed
18204809
uniprot
proteins
pubmed
18360822
uniprot
proteins
pubmed
19319978
uniprot
proteins
pubmed
19325939
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19969356
uniprot
proteins
pubmed
20038677
uniprot
proteins
pubmed
20185555
uniprot
proteins
pubmed
20843780
uniprot
proteins
pubmed
20974897
uniprot
proteins
pubmed
21081504
uniprot
proteins
pubmed
21112924
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21364629
uniprot
proteins
pubmed
21636302
uniprot
proteins
pubmed
22382025
uniprot
proteins
pubmed
22857269
uniprot
proteins
pubmed
23387428
uniprot
proteins
pubmed
23401657
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24616225
uniprot
proteins
pubmed
25012220
uniprot
proteins
pubmed
25146916
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26561570
uniprot
proteins
pubmed
27495975
uniprot
proteins
pubmed
28628083
uniprot
proteins
pubmed
28746876
uniprot
proteins
pubmed
31922487
uniprot
proteins
pubmed
32228866
uniprot
proteins
pubmed
32245890
uniprot
proteins
pubmed
32379273
uniprot
proteins
pubmed
32567732
uniprot
proteins
pubmed
33130824
uniprot
proteins
pubmed
33237841
uniprot
proteins
pubmed
37612504
uniprot
proteins
pubmed
37612506
uniprot
proteins
pubmed
39233737
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
960
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, long form]: Mitochondrion inner membrane {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:28746876, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}; Single-pass membrane protein {ECO:0000255}. Note=Detected at contact sites between endoplasmic reticulum and mitochondrion membranes. {ECO:0000269|PubMed:24616225}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase OPA1, short form]: Mitochondrion intermembrane space {ECO:0000269|PubMed:32228866, ECO:0000269|PubMed:37612504, ECO:0000269|PubMed:37612506}.
uniprot
proteins
transmembrane_region
TRANSMEM 97..113; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins