ID   ATG4_MEDTR              Reviewed;         487 AA.
AC   A2Q1V6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Cysteine protease ATG4 {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q9Y4P1};
DE   AltName: Full=Autophagy-related protein 4;
GN   Name=ATG4; Synonyms=APG4; ORFNames=MtrDRAFT_AC149129g15v2;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The international Medicago genome annotation group;
RL   Submitted (FEB-2007) 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. In addition to the
CC       protease activity, also mediates delipidation of PE-conjugated ATG8
CC       proteins (By similarity). {ECO:0000250|UniProtKB:Q2XPP4,
CC       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:Q9Y4P1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC   -!- SUBUNIT: Interacts with ATG8. {ECO:0000250|UniProtKB:Q9Y4P1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR   EMBL; AC149129; ABN05923.1; -; Genomic_DNA.
DR   RefSeq; XP_003624282.1; XM_003624234.2.
DR   AlphaFoldDB; A2Q1V6; -.
DR   SMR; A2Q1V6; -.
DR   STRING; 3880.AES80500; -.
DR   EnsemblPlants; AES80500; AES80500; MTR_7g081230.
DR   GeneID; 11436743; -.
DR   Gramene; AES80500; AES80500; MTR_7g081230.
DR   eggNOG; KOG2674; Eukaryota.
DR   OMA; CHTRRIR; -.
DR   OrthoDB; 431748at2759; -.
DR   ExpressionAtlas; A2Q1V6; differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; PTHR22624; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Thiol protease; Transport; Ubl conjugation pathway.
FT   CHAIN           1..487
FT                   /note="Cysteine protease ATG4"
FT                   /id="PRO_0000286900"
FT   ACT_SITE        174
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        369
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
SQ   SEQUENCE   487 AA;  53809 MW;  CFF32A0570DE3D0E CRC64;
     MVLKDLCDRI VAAKCSSKSS TEIVDNTQVP ASSKAGSSDS KFPKASLWST FFTSGFSVDE
     TYSESSSSEK KTVHSRNSGW AAAVRKVVSG GSMRRFQERV LGSCRTDVSS SDGDIWLLGV
     CHKISQHEST GDVDIRNVFA AFEQDFFSRI LITYRKGFDA IEDSKYTSDV NWGCMLRSSQ
     MLVAQALLFH KLGRSWRKTV DKPVDKEYID ILQLFGDSEA AAFSIHNLLQ AGKGYGLAVG
     SWVGPYAMCR TWEVLARNQR EKNEQGEQLL PMAIYVVSGD EDGERGGAPV VCIEDACKRC
     LEFSRGLVPW TPLLLLVPLV LGLDKVNLRY IPLLQSTFKF PQSLGILGGK PGASTYIIGV
     QNDKAFYLDP HEVKPVVNIT GDTQEPNTSS YHCNISRHMP LDSIDPSLAI GFYCRDKDDF
     DDFCSRATKL AEESNGAPLF TVAQSRSLPM QVTSNSVSGD DTRFEEDDSL SMNLVNDAGN
     EDDWQFL