ATP-dependent zinc metalloprotease YME1L1 (EC 3.4.24.-) (ATP-dependent metalloprotease FtsH1) (Meg-4) (Presenilin-associated metalloprotease) (PAMP) (YME1-like protein 1)
1_MFSLS 6_ STVQP 11_ QVTVP 16_ LSHLI 21_ NAFHT 26_ PKNTS 31_ VSLSG 36_ VSVSQ 41_ NQHRD 46_ VVPEH 51_ EAPSS 56_ ECMFS 61_ DFLTK 66_ LNIVS 71_ IGKGK 76_ IFEGY 81_ RSMFM 86_ EPAKR 91_ MKKSL 96_ DTTDN 101_ WHIRP 106_ EPFSL 111_ SIPPS 116_ LNLRD 121_ LGLSE 126_ LKIGQ 131_ IDQLV 136_ ENLLP 141_ GFCKG 146_ KNISS 151_ HWHTS 156_ HVSAQ 161_ SFFEN 166_ KYGNL 171_ DIFST 176_ LRSSC 181_ LYRHH 186_ SRALQ 191_ SICSD 196_ LQYWP 201_ VFIQS 206_ RGFKT 211_ LKSRT 216_ RRLQS 221_ TSERL 226_ AETQN 231_ IAPSF 236_ VKGFL 241_ LRDRG 246_ SDVES 251_ LDKLM 256_ KTKNI 261_ PEAHQ 266_ DAFKT 271_ GFAEG 276_ FLKAQ 281_ ALTQK 286_ TNDSL 291_ RRTRL 296_ ILFVL 301_ LLFGI 306_ YGLLK 311_ NPFLS 316_ VRFRT 321_ TTGLD 326_ SAVDP 331_ VQMKN 336_ VTFEH 341_ VKGVE 346_ EAKQE 351_ LQEVV 356_ EFLKN 361_ PQKFT 366_ ILGGK 371_ LPKGI 376_ LLVGP 381_ PGTGK 386_ TLLAR 391_ AVAGE 396_ ADVPF 401_ YYASG 406_ SEFDE 411_ MFVGV 416_ GASRI 421_ RNLFR 426_ EAKAN 431_ APCVI 436_ FIDEL 441_ DSVGG 446_ KRIES 451_ PMHPY 456_ SRQTI 461_ NQLLA 466_ EMDGF 471_ KPNEG 476_ VIIIG 481_ ATNFP 486_ EALDN 491_ ALIRP 496_ GRFDM 501_ QVTVP 506_ RPDVK 511_ GRTEI 516_ LKWYL 521_ NKIKF 526_ DQSVD 531_ PEIIA 536_ RGTVG 541_ FSGAE 546_ LENLV 551_ NQAAL 556_ KAAVD 561_ GKEMV 566_ TMKEL 571_ EFSKD 576_ KILMG 581_ PERRS 586_ VEIDN 591_ KNKTI 596_ TAYHE 601_ SGHAI 606_ IAYYT 611_ KDAMP 616_ INKAT 621_ IMPRG 626_ PTLGH 631_ VSLLP 636_ ENDRW 641_ NETRA 646_ QLLAQ 651_ MDVSM 656_ GGRVA 661_ EELIF 666_ GTDHI 671_ TTGAS 676_ SDFDN 681_ ATKIA 686_ KRMVT 691_ KFGMS 696_ EKLGV 701_ MTYSD 706_ TGKLS 711_ PETQS 716_ AIEQE 721_ IRILL 726_ RDSYE 731_ RAKHI 736_ LKTHA 741_ KEHKN 746_ LAEAL 751_ LTYET 756_ LDAKE 761_ IQIVL 766_EGKKL
1: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:24315374, PubMed:26923599, PubMed:27786171, PubMed:31695197, PubMed:33237841, PubMed:36206740). 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 (PubMed:18076378, PubMed:26923599, PubMed:27495975, PubMed:33237841). 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 (PubMed:22262461). Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) (PubMed:22262461). 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 (PubMed:31695197). 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, YME1L is activated by decreased phosphatidylethanolamine levels caused by LPIN1 activity in response to mTORC1 inhibition (PubMed:31695197). Acts as a regulator of adult neural stem cell self-renewal by promoting mitochondrial proteome rewiring, preserving neural stem and progenitor cells self-renewal (By similarity). Required for normal, constitutive degradation of PRELID1 (PubMed:27495975). Catalyzes the degradation of OMA1 in response to membrane depolarization (PubMed:26923599). Mediates degradation of TIMM17A downstream of the integrated stress response (ISR) (PubMed:24315374). Catalyzes degradation of MICU1 when MICU1 is not assembled via an interchain disulfide (PubMed:36206740)