UniProt ID: A0A2R8Q487
SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|SAAS:SAAS00534970}.
UniProt ID: A0A2R8Q0F5
SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|SAAS:SAAS00534970}.
UniProt ID: A0A0R4IJ30
SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|SAAS:SAAS00534970}.
UniProt ID: Q5U3A7
FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Binds lipid membranes enriched in negatively charged phospholipids, such as cardiolipin, and promotes membrane tubulation. The intrinsic GTPase activity is low, and is strongly increased by interaction with lipid membranes (By similarity). Plays a role in remodeling cristae and the release of cytochrome c during apoptosis (By similarity). {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
FUNCTION: Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by oma1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:O60313};
SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble forms of OPA1. Binds PARL (By similarity). {ECO:0000250|UniProtKB:P58281}.
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O60313}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane {ECO:0000250|UniProtKB:O60313}. Note=Detected at contact sites between endoplamic reticulum and mitochondrion membranes. {ECO:0000250|UniProtKB:O60313}.
PTM: Proteolytic processing produces an antiapoptotic soluble form Cleaved by oma1 at position S1 following stress conditions. {ECO:0000250}.
PTM: PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion. Cleaved by oma1 at position S1 following stress conditions. {ECO:0000250|UniProtKB:O60313}.
SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE- ProRule:PRU01055}.
UniProt ID: A0A0R4ILJ7
SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|SAAS:SAAS00534970}.
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