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ATG4A_BOVIN
ID   ATG4A_BOVIN             Reviewed;         398 AA.
AC   Q6PZ05;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cysteine protease ATG4A {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q8WYN0};
DE   AltName: Full=Autophagy-related cysteine endopeptidase 2A {ECO:0000250|UniProtKB:Q8WYN0};
DE            Short=Autophagin-2A {ECO:0000250|UniProtKB:Q8WYN0};
DE            Short=bAut2A {ECO:0000303|PubMed:15140988};
DE   AltName: Full=Autophagy-related protein 4 homolog A {ECO:0000250|UniProtKB:Q8WYN0};
GN   Name=ATG4A {ECO:0000250|UniProtKB:Q8WYN0};
GN   Synonyms=APG4A {ECO:0000250|UniProtKB:Q8WYN0},
GN   AUT2A {ECO:0000303|PubMed:15140988};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION (MICROBIAL INFECTION).
RX   PubMed=15140988; DOI=10.1128/jvi.78.11.5900-5912.2004;
RA   Fricke J., Voss C., Thumm M., Meyers G.;
RT   "Processing of a pestivirus protein by a cellular protease specific for
RT   light chain 3 of microtubule-associated proteins.";
RL   J. Virol. 78:5900-5912(2004).
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. Exposure of the glycine at the
CC       C-terminus is essential for ATG8 proteins conjugation to
CC       phosphatidylethanolamine (PE) and insertion to membranes, which is
CC       necessary for autophagy. Preferred substrate is GABARAPL2 followed by
CC       MAP1LC3A and GABARAP. Protease activity is also required to counteract
CC       formation of high-molecular weight conjugates of ATG8 proteins
CC       (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8
CC       conjugated to other proteins, such as ATG3. In addition to the protease
CC       activity, also mediates delipidation of ATG8 family proteins. Catalyzes
CC       delipidation of PE-conjugated forms of ATG8 proteins during
CC       macroautophagy. Compared to ATG4B, the major protein for proteolytic
CC       activation of ATG8 proteins, shows weaker ability to cleave the C-
CC       terminal amino acid of ATG8 proteins, while it displays stronger
CC       delipidation activity. Involved in phagophore growth during mitophagy
CC       independently of its protease activity and of ATG8 proteins: acts by
CC       regulating ATG9A trafficking to mitochondria and promoting phagophore-
CC       endoplasmic reticulum contacts during the lipid transfer phase of
CC       mitophagy. {ECO:0000250|UniProtKB:Q8WYN0}.
CC   -!- FUNCTION: (Microbial infection) Mediates cleavage of an ATG8 protein
CC       homolog coded in the genome of cytopathogenic bovine viral diarrhea
CC       virus (BVDV). {ECO:0000269|PubMed:15140988}.
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:Q8WYN0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000250|UniProtKB:Q8WYN0};
CC   -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. Redox-regulated
CC       during autophagy since reducing conditions activate ATG4A whereas an
CC       oxidizing environment such as the presence of H(2)O(2) inhibits its
CC       activity. {ECO:0000250|UniProtKB:Q8WYN0}.
CC   -!- SUBUNIT: Interacts with ATG9A; the interaction is direct.
CC       {ECO:0000250|UniProtKB:Q8WYN0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC   -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC       interaction with the ATG8 family proteins. Required for proteolytic
CC       activation and delipidation of ATG8 proteins.
CC       {ECO:0000250|UniProtKB:Q8WYN0}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR   EMBL; AY570549; AAS78581.1; -; mRNA.
DR   RefSeq; NP_001001171.1; NM_001001171.1.
DR   AlphaFoldDB; Q6PZ05; -.
DR   SMR; Q6PZ05; -.
DR   STRING; 9913.ENSBTAP00000018239; -.
DR   MEROPS; C54.002; -.
DR   PaxDb; Q6PZ05; -.
DR   GeneID; 408003; -.
DR   KEGG; bta:408003; -.
DR   CTD; 115201; -.
DR   eggNOG; KOG2674; Eukaryota.
DR   InParanoid; Q6PZ05; -.
DR   OrthoDB; 431748at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019786; F:Atg8-specific peptidase activity; ISS:UniProtKB.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; IPR033474; ATG4A.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; PTHR22624; 1.
DR   PANTHER; PTHR22624:SF35; PTHR22624:SF35; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Hydrolase; Lipid metabolism; Protease;
KW   Protein transport; Reference proteome; Thiol protease; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..398
FT                   /note="Cysteine protease ATG4A"
FT                   /id="PRO_0000215837"
FT   MOTIF           393..396
FT                   /note="LIR"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYN0"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
SQ   SEQUENCE   398 AA;  45354 MW;  C0E9F9D2A29B8E0C CRC64;
     MESVLSKYEN QITIFADYLE EFPDTDELVW ILGKQHLLKT EKSKLLSDIS ARLWFTYRRK
     FSPIGGTGPS SDAGWGCMLR CGQMMLAQAL ICRHLGRDWN WEKQKEQPKE YQRILQCFLD
     RKDCCYSIHQ MAQMGVGEGK SIGEWFGPNT VAQVLKKLAL FDEWNSLAVY VSMDNTVVIE
     DIKKMCRTLS LSADTPAERP LESLTASNQS KGPSACCTAW KPLLLIVPLR LGINQINPVY
     VDAFKECFKM PQSLGALGGK PNNAYYFIGF LGDELIFLDP HTTQTFVDTE ENGTADDQTF
     HCLQPPQRMN ILNLDPSVAL GFFCKEEKDF DSWCSLVQKE ILKENLRMFE LVQKHPSHWP
     PFVPPAKPEV TTTGAEFIDS TEQLEEFDLE EDFEILSI
 
 
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