ID   ATG4C_XENLA             Reviewed;         450 AA.
AC   Q5XH30;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Cysteine protease ATG4C {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q96DT6};
DE   AltName: Full=Autophagy-related protein 4 homolog C {ECO:0000250|UniProtKB:Q96DT6};
GN   Name=atg4c {ECO:0000250|UniProtKB:Q96DT6};
GN   Synonyms=apg4c {ECO:0000250|UniProtKB:Q96DT6};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC       mediating both proteolytic activation and delipidation of ATG8 family
CC       proteins. The protease activity is required for proteolytic activation
CC       of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8
CC       proteins to reveal a C-terminal glycine (By similarity). Exposure of
CC       the glycine at the C-terminus is essential for ATG8 proteins
CC       conjugation to phosphatidylethanolamine (PE) and insertion to
CC       membranes, which is necessary for autophagy (By similarity). In
CC       addition to the protease activity, also mediates delipidation of ATG8
CC       family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8
CC       proteins during macroautophagy (By similarity).
CC       {ECO:0000250|UniProtKB:Q96DT6, ECO:0000250|UniProtKB:Q9Y4P1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-C-terminal L-amino acid-glycyl-
CC         phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-
CC         glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940,
CC         ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q96DT6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000250|UniProtKB:Q96DT6};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR   EMBL; BC084245; AAH84245.1; -; mRNA.
DR   RefSeq; NP_001088249.1; NM_001094780.1.
DR   AlphaFoldDB; Q5XH30; -.
DR   SMR; Q5XH30; -.
DR   MEROPS; C54.004; -.
DR   DNASU; 495080; -.
DR   GeneID; 495080; -.
DR   KEGG; xla:495080; -.
DR   CTD; 495080; -.
DR   Xenbase; XB-GENE-941092; atg4c.S.
DR   OMA; EAVFIMK; -.
DR   OrthoDB; 431748at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 495080; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR   GO; GO:0051697; P:protein delipidation; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR032915; ATG4C.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; PTHR22624; 1.
DR   PANTHER; PTHR22624:SF38; PTHR22624:SF38; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Reference proteome; Thiol protease; Transport; Ubl conjugation pathway.
FT   CHAIN           1..450
FT                   /note="Cysteine protease ATG4C"
FT                   /id="PRO_0000215851"
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
SQ   SEQUENCE   450 AA;  51768 MW;  336763FCA05549F8 CRC64;
     MEASGTDDVE KLKSKFLSAW HNMKYSWVLK TKTYFKRNSP VFLLGKCYHF KYEDSGVTAD
     DCSNSGSDSK EDLSGNVDEF RKDFISRIWL TYRKEFPQIE SSSWTTDCGW GCTLRTGQML
     LAQGLLVHFL GRDWTWTEAL DIFCSESDFW TANTARKLDP SLEKSSPENE EYVSLGKQPL
     QNSEKKRYSE DLHRKIISWF ADYPLAYFGL HQLVKLGKNS GKVAGDWYGP AVVSHLLRKA
     IEESSDPELQ GITIYVAQDC TIYNADVYDL QCNKGNEKAV VILVPVRLGG ERTNMEYFEY
     VKGILSLEFC IGIIGGKPKQ SYYFVGFQDD SLIYMDPHYC QSFVDVSIKN FPLESFHCPS
     PKKMSFKKMD PSCTVGFYCR NAREFEKAAE ELTKVLKSST KQNYPLFTFV NGHAQDFDFV
     CTPVYDQNDL FTEDEKKRLK RFSTEEFVLL