ATG4D_XENLA
ID ATG4D_XENLA Reviewed; 469 AA.
AC Q68FJ9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cysteine protease ATG4D {ECO:0000305};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q86TL0};
DE AltName: Full=Autophagy-related protein 4 homolog D {ECO:0000250|UniProtKB:Q86TL0};
DE Short=Autophagin-4 {ECO:0000250|UniProtKB:Q86TL0};
GN Name=atg4d {ECO:0000250|UniProtKB:Q86TL0};
GN Synonyms=apg4d {ECO:0000250|UniProtKB:Q86TL0};
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=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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 (By similarity). The protease activity is required for
CC proteolytic activation of ATG8 family proteins to reveal a C-terminal
CC glycine (By similarity). Exposure of the glycine at the C-terminus is
CC essential for ATG8 proteins conjugation to phosphatidylethanolamine
CC (PE) and insertion to membranes, which is necessary for autophagy (By
CC similarity). In addition to the protease activity, also mediates
CC delipidation of ATG8 family proteins. Catalyzes delipidation of PE-
CC conjugated forms of ATG8 proteins during macroautophagy (By
CC similarity). Also involved in non-canonical autophagy, a parallel
CC pathway involving conjugation of ATG8 proteins to single membranes at
CC endolysosomal compartments, by catalyzing delipidation of ATG8 proteins
CC conjugated to phosphatidylserine (PS) (By similarity).
CC {ECO:0000250|UniProtKB:Q86TL0, 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:Q86TL0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC Evidence={ECO:0000250|UniProtKB:Q86TL0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine +
CC H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine; Xref=Rhea:RHEA:67576, Rhea:RHEA-
CC COMP:17324, Rhea:RHEA-COMP:17326, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:172940, ChEBI:CHEBI:172942;
CC Evidence={ECO:0000250|UniProtKB:Q86TL0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67577;
CC Evidence={ECO:0000250|UniProtKB:Q86TL0};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}.
CC -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR EMBL; BC079754; AAH79754.1; -; mRNA.
DR RefSeq; NP_001087417.1; NM_001093948.1.
DR AlphaFoldDB; Q68FJ9; -.
DR SMR; Q68FJ9; -.
DR MEROPS; C54.005; -.
DR DNASU; 447241; -.
DR GeneID; 447241; -.
DR CTD; 447241; -.
DR Xenbase; XB-GENE-1016723; atg4d.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 447241; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0051697; P:protein delipidation; ISS:UniProtKB.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Hydrolase; Protease; Protein transport;
KW Reference proteome; Thiol protease; Transport; Ubl conjugation pathway.
FT CHAIN 1..469
FT /note="Cysteine protease ATG4D"
FT /id="PRO_0000215856"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 356
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 358
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
SQ SEQUENCE 469 AA; 52812 MW; 73413D2256A3F304 CRC64;
MNSVSPLATQ YGSPKGSQQM ENRSTQSGGH EQRKMGHQDA TLDGEADEVD KLKSKLLSAW
NNVKYGWSVK MKTTFSRSAP VYLLGERYFF RLDDEIERFQ KDFVSRVWLT YRRDFPALEG
TALTTDCGWG CMIRSGQMLL AQGLLLHLLS REWTWSEALY RHFVEMEPIR SSSPPSMPLS
SLATGHSAGD YQPHTQCSGA PHGDQVHRNI MRWFSDHPGS PFGLHQLVTL GSIFGKKAGD
WYGPSIVAHI IKKAIETSSE VPELSVYVSQ DCTVYKADIE QLFAGDVPHA ETSRGAGKAV
IILVPVRLGG ETFNPVYKHC LKEFLRMPSC LGIIGGKPKH SLYFIGYQDN YLLYLDPHYC
QPYIDTSKND FPLESFHCNS PRKISITRMD PSCTFAFYAK NSEDFGKLCD HLMKVLHSPR
AEEKYPIFSI SEGQAQEYAE GPQSSSHPPV CRKKGPLVKR PSSDEFEFL
