Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 3) (Autophagin-3) (Autophagy-related protein 4 homolog C) (HsAPG4C)
1_MEATG 6_ TDEVD 11_ KLKTK 16_ FISAW 21_ NNMKY 26_ SWVLK 31_ TKTYF 36_ SRNSP 41_ VLLLG 46_ KCYHF 51_ KYEDE 56_ DKTLP 61_ AESGC 66_ TIEDH 71_ VIAGN 76_ VEEFR 81_ KDFIS 86_ RIWLT 91_ YREEF 96_ PQIEG 101_ SALTT 106_ DCGWG 111_ CTLRT 116_ GQMLL 121_ AQGLI 126_ LHFLG 131_ RAWTW 136_ PDALN 141_ IENSD 146_ SESWT 151_ SHTVK 156_ KFTAS 161_ FEASL 166_ SGERE 171_ FKTPT 176_ ISLKE 181_ TIGKY 186_ SDDHE 191_ MRNEV 196_ YHRKI 201_ ISWFG 206_ DSPLA 211_ LFGLH 216_ QLIEY 221_ GKKSG 226_ KKAGD 231_ WYGPA 236_ VVAHI 241_ LRKAV 246_ EEARH 251_ PDLQG 256_ ITIYV 261_ AQDCT 266_ VYNSD 271_ VIDKQ 276_ SASMT 281_ SDNAD 286_ DKAVI 291_ ILVPV 296_ RLGGE 301_ RTNTD 306_ YLEFV 311_ KGILS 316_ LEYCV 321_ GIIGG 326_ KPKQS 331_ YYFAG 336_ FQDDS 341_ LIYMD 346_ PHYCQ 351_ SFVDV 356_ SIKDF 361_ PLETF 366_ HCPSP 371_ KKMSF 376_ RKMDP 381_ SCTIG 386_ FYCRN 391_ VQDFK 396_ RASEE 401_ ITKML 406_ KFSSK 411_ EKYPL 416_ FTFVN 421_ GHSRD 426_ YDFTS 431_ TTTNE 436_ EDLFS 441_ EDEKK 446_ QLKRF 451_STEEF
1: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:21177865, PubMed:29458288, PubMed:30661429). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (PubMed:21177865). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:29458288, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:29458288, PubMed:33909989). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed:29458288). In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (PubMed:33773106)