Q925S8
uniprot
Q925S8
canonical
amino_acid_sequence
MFSLSSTVQPQVTVPLSHLINAFHSPKNISVSVNTSASPKQHRDTVAEHEAPSSEPVLNLRDLGLSELKIGQIDKLVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLQSICSDLQNFPVFIQSRGFKTLKSRTRRLQSTSERLAEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIEFPMHPYSRQTIIQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDKSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNEIRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRESYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
ec_number
3.6.-.-
uniprot
proteins
function
FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region. Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism (By similarity). Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (By similarity). Involved in the mitochondrial adaptation in response to various signals, such as stress or developmental cues, by mediating degradation of mitochondrial proteins to rewire the mitochondrial proteome (By similarity). Catalyzes degradation of mitochondrial proteins, such as translocases, lipid transfer proteins and metabolic enzymes in response to nutrient starvation in order to limit mitochondrial biogenesis: mechanistically, YME1L1 is activated by decreased phosphatidylethanolamine levels caused by LPIN1 activity in response to mTORC1 inhibition (By similarity). Acts as a regulator of adult neural stem cell self-renewal by promoting mitochondrial proteome rewiring, preserving neural stem and progenitor cells self-renewal. Required for normal, constitutive degradation of PRELID1 (By similarity). Catalyzes the degradation of OMA1 in response to membrane depolarization. Mediates degradation of TIMM17A downstream of the integrated stress response (ISR) (By similarity). Catalyzes degradation of MICU1 when MICU1 is not assembled via an interchain disulfide (By similarity). Cleaves STARD7 mitochondrial targeting sequence (By similarity). {ECO:0000250|UniProtKB:O88967, ECO:0000250|UniProtKB:Q96TA2}.
uniprot
proteins
mass_dalton
79867
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. Degraded in an OMA1-dependent manner in response to oxidative stress. {ECO:0000250|UniProtKB:Q96TA2}.
uniprot
proteins
protein_family
AAA ATPase family; Peptidase M41 family
uniprot
proteins
sequence_length
715
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion {ECO:0000250|UniProtKB:Q96TA2}.
uniprot
proteins
transmembrane_region
TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins