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   03-AUG-2022, entry version 116.
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.ENSGALP00000035497; -.
DR   PaxDb; Q5ZKY2; -.
DR   PRIDE; Q5ZKY2; -.
DR   Ensembl; ENSGALT00000047265; ENSGALP00000051055; ENSGALG00000004932.
DR   GeneID; 415961; -.
DR   KEGG; gga:415961; -.
DR   CTD; 10533; -.
DR   VEuPathDB; HostDB:geneid_415961; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   GeneTree; ENSGT00390000017509; -.
DR   HOGENOM; CLU_012998_1_0_1; -.
DR   InParanoid; Q5ZKY2; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
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 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:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0044805; P:late 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   Gene3D; 3.40.140.100; -; 1.
DR   Gene3D; 3.40.140.70; -; 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   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF16420; ATG7_N; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 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