ATG7_YARLI
ID ATG7_YARLI Reviewed; 598 AA.
AC Q6CBC3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE AltName: Full=ATG12-activating enzyme E1 ATG7;
DE AltName: Full=Autophagy-related protein 7;
GN Name=ATG7; OrderedLocusNames=YALI0C20119g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {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; CR382129; CAG82359.1; -; Genomic_DNA.
DR RefSeq; XP_502039.1; XM_502039.1.
DR AlphaFoldDB; Q6CBC3; -.
DR SMR; Q6CBC3; -.
DR STRING; 4952.CAG82359; -.
DR EnsemblFungi; CAG82359; CAG82359; YALI0_C20119g.
DR GeneID; 2909898; -.
DR KEGG; yli:YALI0C20119g; -.
DR VEuPathDB; FungiDB:YALI0_C20119g; -.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; Q6CBC3; -.
DR OMA; GKMGPNI; -.
DR Proteomes; UP000001300; Chromosome C.
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; IBA:GO_Central.
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: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 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; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..598
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212821"
FT MOTIF 308..313
FT /note="GXGXXG motif"
FT ACT_SITE 486
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 66794 MW; E6681938785482E0 CRC64;
MSFTPFSSFL EASFFQTLAA KKLNEYKLDD SPKRVSAEYT WQQGRLVFDS DSFSDRDSHC
KGVVECPGTL LNYNTIEEFK GADKKALLAE WGDKMLSGAI MNGSIFRNPE ILNSFLLITF
CDLKKYIFVY WMGVPCLNTK WDLQEVADEG NYTNLSTRIP ALGESFVVID PDDNVTPFSE
LEYVERSEDP TIAFLSPTSP ENTPWTVRNI CLMLHILGFK SATMILVGRE KNRFLEWKRG
DGELGAWTGW EKNSAGKLLP KQTNLGPLLN PLQLASQAVD LNLKLMKWRI APELDLDTIK
HTRCLLLGAG TLGSYVSRSL LAWGVEQVTF VDNGTVSFSN PVRQPLYKYV DCLDGGKPKA
ETAAEALKEI YPAVKTSGIT LEVPMIGHST TSSSEKRVHQ QYDELVSLIK SHDAVFLLMD
SRESRWLPTV ICAALKKKCI TAAIGFDSFV VMRHGVEGVN DLGCYFCNDV VAPTDSMNDR
TLDQQCTVTR PGIAPIVSGY GVEILQAMCQ DEPSAPHQLR GFLHNFSTVK ITGQRFKCCS
ACSPVIVQEW KDKTWGFVKK ALNERGFVEE LCGLAELQRG VDELDFGEGE GSEEEWEM
