ATG7_YEAS7
ID ATG7_YEAS7 Reviewed; 630 AA.
AC A6ZT79;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
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 AltName: Full=Cytoplasm to vacuole targeting protein 2;
GN Name=ATG7; Synonyms=APG7, CVT2; ORFNames=SCY_2563;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 and ATG8 for
CC its conjugation with phosphatidylethanolamine. Both systems are needed
CC for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC Autophagy is essential for maintenance of amino acid levels and protein
CC synthesis under nitrogen starvation. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC 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. Plays a role
CC in the regulation of filamentous growth and chronological longevity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG8 through a thioester bond
CC between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12
CC through a thioester bond between Cys-507 and the C-terminal 'Gly-186'
CC of ATG12. Interacts also with ATG3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {ECO:0000250}.
CC -!- DOMAIN: The C-terminal 40 residues are required for homodimerization,
CC as well as the interactions with ATG3, ATG8 and ATG12; and the C-
CC terminal 17 residues are required for the ATG8 lipidation.
CC {ECO:0000250}.
CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC through binding with ATP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; AAFW02000082; EDN62410.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZT79; -.
DR SMR; A6ZT79; -.
DR EnsemblFungi; EDN62410; EDN62410; SCY_2563.
DR HOGENOM; CLU_012998_2_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; 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 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..630
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000317873"
FT MOTIF 331..336
FT /note="GXGXXG motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 507
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 630 AA; 71410 MW; 4318544C3C2F64CC CRC64;
MSSERVLNYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN IPKSADQVPL
FLTNRSFEKQ NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL FLHQRALECW EDGIKDINKC
VSFVIISFAD LKKYRFYYWL GVPCFQRPSS TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV
CILDADDEIV NYDKCIIRKT KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI
IRQNEGSFAL NATFASSDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK ITFVDNGTVS
YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK LSIPMIGHKL VNEEAQHKDF
DRLRALIKEH DIIFLLVDSR ESRWLPSLLS NIENKTVINA ALGFDSYLVM RHGNRDEQSS
KQLGCYFCHD VVAPTDSLTD RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT
VLGDIPHQIR GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
ISGLSVMKQE VEQLGNDVFE WEDDESDEIA