ID ATG7_CHICK Reviewed; 709 AA.
AC Q5ZKY2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE AltName: Full=ATG12-activating enzyme E1 ATG7;
DE AltName: Full=Autophagy-related protein 7;
DE Short=APG7-like;
GN Name=ATG7; Synonyms=APG7L; ORFNames=RCJMB04_8l10;
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: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and
CC autophagy. Activates ATG12 for its conjugation with ATG5 as well as the
CC ATG8 family proteins for their conjugation with
CC phosphatidylethanolamine. Both systems are needed for the ATG8
CC association to Cvt vesicles and autophagosomes membranes. Required for
CC autophagic death induced by caspase-8 inhibition. Facilitates LC3-I
CC lipidation with phosphatidylethanolamine to form LC3-II which is found
CC on autophagosomal membranes (By similarity). Required for mitophagy
CC which contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. Modulates
CC p53/TP53 activity to regulate cell cycle and survival during metabolic
CC stress (By similarity). Plays a role in regulating the liver clock and
CC glucose metabolism by mediating the autophagic degradation of CRY1
CC (clock repressor) in a time-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:O95352, ECO:0000250|UniProtKB:Q9D906}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG3 and ATG12. The complex,
CC composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to
CC ATG5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {ECO:0000250}.
CC -!- DOMAIN: The C-terminal part of the protein is essential for the
CC dimerization and interaction with ATG3 and ATG12. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; AJ719952; CAG31611.1; -; mRNA.
DR RefSeq; NP_001025763.1; NM_001030592.1.
DR RefSeq; XP_015148538.1; XM_015293052.1.
DR RefSeq; XP_015148539.1; XM_015293053.1.
DR RefSeq; XP_015148540.1; XM_015293054.1.
DR AlphaFoldDB; Q5ZKY2; -.
DR SMR; Q5ZKY2; -.
DR STRING; 9031.ENSGALP00000051055; -.
DR PaxDb; 9031-ENSGALP00000035497; -.
DR Ensembl; ENSGALT00000147952; ENSGALP00000081162; ENSGALG00000004932.
DR Ensembl; ENSGALT00015064101; ENSGALP00015039075; ENSGALG00015026323.
DR GeneID; 415961; -.
DR KEGG; gga:415961; -.
DR CTD; 10533; -.
DR VEuPathDB; HostDB:geneid_415961; -.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_1_0_1; -.
DR InParanoid; Q5ZKY2; -.
DR PhylomeDB; Q5ZKY2; -.
DR Reactome; R-GGA-1632852; Macroautophagy.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q5ZKY2; -.
DR Proteomes; UP000000539; Chromosome 12.
DR Bgee; ENSGALG00000004932; Expressed in spermatid and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd01486; Apg7; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 1.
DR InterPro; IPR006285; Atg7.
DR InterPro; IPR032197; Atg7_N.
DR InterPro; IPR042522; Atg7_N_1.
DR InterPro; IPR042523; Atg7_N_2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR NCBIfam; TIGR01381; E1_like_apg7; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Biological rhythms; Cytoplasm; Protein transport;
KW Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..709
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212809"
FT ACT_SITE 578
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 709 AA; 78800 MW; 3B0060E12C49E15C CRC64;
MAAVSNESQN PVDPGSSKLQ FAPFSSALNV GFWHELTQKK LNEYRLDETP KVIKGYYYNG
DPSGFPARLT LEYSAFDINA SIPARCCPAF GTLYNTNTFE TFKSCDKKSL LEKEANEIWE
SIKSGAALEN PMLLNRFLLL TFADLKKYHF YYWFCYPALC FPDGIHVIQK PVCLGDRFSL
NQIQALQKAY DELCQTEGVT AFPYFLIKYH DNSVVVSPLK KWDGFFQDQG GKVTVGVYDP
CNLSHYPGWP LRNFLILASH KWGNILQSIE VLCFRDRTMQ GVRDITHSII FEIKLPQGAF
GPDCPKAVGW EKNQKGGMGP RVVNLSECMD PKRLAESSVD LNLKLMCWRL VPTLDLEKIV
SAKCLLLGAG TLGCSVARTL MGWGVRKITF VDNARISYSN PVRQPLYEFE DCLSGGKPKA
LAAAERLQKI FPGVNSEGYN MSIPMPGHPV NFSEVTMAQA RKDVATLEEL IDAHDVVFLL
MDTRESRWLP AVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQETGNAC FSTAPGPSDL
LGSSLFSNIP GYKLGCYFCN DVVAPGDSTR DRTLDQQCTV SRPGLAMIAG ALAVELMVSV
LQHPEGGYAV ASSSDDRMNE PPTSLGLVPH QIRGFLSRFD NVLPVSLAFD KCTACSPKVL
DQYEREGFNF LAKVFNSSHS FLEDLTGLTL LHQETQAAEI WDMSDDETV
//
