ID   ATG3_CANGA              Reviewed;         309 AA.
AC   Q6FQJ2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN   Name=ATG3; OrderedLocusNames=CAGL0I05808g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: E2 conjugating enzyme required for the cytoplasm to vacuole
CC       transport (Cvt) and autophagy. 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. Responsible
CC       for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC       terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3
CC       and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine
CC       (PE). This step is required for the membrane association of ATG8. The
CC       formation of the ATG8-phosphatidylethanolamine conjugate is essential
CC       for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC       ATG8-PE conjugate mediates tethering between adjacent membranes and
CC       stimulates membrane hemifusion, leading to expansion of the
CC       autophagosomal membrane during autophagy (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts with ATG8 through an intermediate thioester
CC       bond through the C-terminal Gly of ATG8. Also interacts with the 40
CC       amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also
CC       with the ATG12-ATG5 conjugate. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC       binding and is required for ATG8-PE conjugation. {ECO:0000250}.
CC   -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC       (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-
CC       vacuole targeting pathway (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR   EMBL; CR380955; CAG60439.1; -; Genomic_DNA.
DR   RefSeq; XP_447502.1; XM_447502.1.
DR   AlphaFoldDB; Q6FQJ2; -.
DR   SMR; Q6FQJ2; -.
DR   STRING; 5478.XP_447502.1; -.
DR   EnsemblFungi; CAG60439; CAG60439; CAGL0I05808g.
DR   GeneID; 2889347; -.
DR   KEGG; cgr:CAGL0I05808g; -.
DR   CGD; CAL0132232; CAGL0I05808g.
DR   VEuPathDB; FungiDB:CAGL0I05808g; -.
DR   eggNOG; KOG2981; Eukaryota.
DR   HOGENOM; CLU_027518_2_0_1; -.
DR   InParanoid; Q6FQJ2; -.
DR   OMA; YDKYYQV; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0019776; F:Atg8 ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR   InterPro; IPR007135; Atg3/Atg10.
DR   PANTHER; PTHR12866; PTHR12866; 1.
DR   Pfam; PF03987; Autophagy_act_C; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..309
FT                   /note="Autophagy-related protein 3"
FT                   /id="PRO_0000213577"
FT   REGION          83..151
FT                   /note="Flexible region"
FT                   /evidence="ECO:0000250"
FT   REGION          226..284
FT                   /note="Handle region"
FT                   /evidence="ECO:0000250"
FT   REGION          243..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  35528 MW;  8424C2251E73DF49 CRC64;
     MIRSALSNWR EYLTPVSHKS TFLTTGQITP EEFVQAGDYL CHMFPTWKWN DMADDNKYRD
     FLPKDKQFLV IRKVPCSERA QAVVTMDEIE NGTSTDAFSA ADDEDNDDDS IEIIPVSKSS
     SGADNDVNDI DELMEEMELE EDDDIVANKT NEMLRYYDLF ITYSTSYRVP KMYIVGFNGN
     GTPLTPKEMF EDITPDYRKK TATIEKLPFY KRNVPSVSIH PCKHANVMKV LLDKISVVKE
     RQREEEMQKN AEVGAPKSAG SDDGDNENWE DLQQDIDDSL RVDLYLVVFL KFITSVTPTI
     QHDYTMEGW