ATG4A_CHICK
ID ATG4A_CHICK Reviewed; 380 AA.
AC Q5ZIW7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cysteine protease ATG4A {ECO:0000305};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q8WYN0};
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 ORFNames=RCJMB04_23b20 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. Protease activity is also required to
CC counteract formation of high-molecular weight conjugates of ATG8
CC proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that
CC removes ATG8 conjugated to other proteins, such as ATG3. In addition to
CC the protease activity, also mediates delipidation of ATG8 family
CC proteins. Catalyzes delipidation of PE-conjugated forms of ATG8
CC proteins during macroautophagy. {ECO:0000250|UniProtKB:Q8WYN0}.
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 -!- 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; AJ720667; CAG32326.1; -; mRNA.
DR RefSeq; NP_001258915.1; NM_001271986.1.
DR RefSeq; NP_001258916.1; NM_001271987.1.
DR AlphaFoldDB; Q5ZIW7; -.
DR SMR; Q5ZIW7; -.
DR STRING; 9031.ENSGALP00000013462; -.
DR MEROPS; C54.002; -.
DR GeneID; 772074; -.
DR KEGG; gga:772074; -.
DR CTD; 115201; -.
DR VEuPathDB; HostDB:geneid_772074; -.
DR eggNOG; KOG2674; Eukaryota.
DR HOGENOM; CLU_021259_0_1_1; -.
DR InParanoid; Q5ZIW7; -.
DR OrthoDB; 431748at2759; -.
DR PhylomeDB; Q5ZIW7; -.
DR PRO; PR:Q5ZIW7; -.
DR Proteomes; UP000000539; 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..380
FT /note="Cysteine protease ATG4A"
FT /id="PRO_0000215841"
FT MOTIF 375..378
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q8WYN0"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 262
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 264
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
SQ SEQUENCE 380 AA; 43383 MW; BE3EA6B9C8119417 CRC64;
MESEFPDTDE PVWILGRQHH LNEDKSKLLL DVSARLWFTY RRKFSPIGGT GPSSDAGWGC
MLRCGQMMLA QALICRHLGR DWQWEKHKKQ PEEYHRILHC FLDRKDCCYS IHQMAQMGVG
EGKSIGEWFG PNTVAQVLKK LALFDEWNSL AVYVSMDNTV VIEDIKKMCR SPPQSSSTAH
SSAHLHRSAL GRNRNAAGLC TGWKPLLLII PLRLGINHIN PVYIDAFKEC FKMPQSLGAL
GGKPNNAYYF IGFLGNELIY LDPHTTQSFV DSEENGTVDD QSFHCQQAPH RMKIMNLDPS
VALGFFCKEE CDFDNWCSLV QKEILKQQSL RMFELVQKHP PHWPPFIPPT KPEVTTTGAE
LIESTDKLFE LEEEFEILSV
