ATG3_DEBHA
ID ATG3_DEBHA Reviewed; 324 AA.
AC Q6BSC4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN Name=ATG3; OrderedLocusNames=DEHA2D09900g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87049.2; -; Genomic_DNA.
DR RefSeq; XP_458896.2; XM_458896.1.
DR AlphaFoldDB; Q6BSC4; -.
DR SMR; Q6BSC4; -.
DR STRING; 4959.XP_458896.2; -.
DR EnsemblFungi; CAG87049; CAG87049; DEHA2D09900g.
DR GeneID; 2901758; -.
DR KEGG; dha:DEHA2D09900g; -.
DR VEuPathDB; FungiDB:DEHA2D09900g; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; Q6BSC4; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..324
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000213579"
FT REGION 82..166
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 100..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..299
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT COMPBIAS 112..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 36763 MW; 6423F05961E2BFD1 CRC64;
MLRSKLSSLR EYLTPIRHTS DFTTTGEISP EEFVEAGDYL VYKFPTWQWS SAPDKLKKDF
LPPDKQYLIT KHVSSYQRAV TYLGIKSDLD EDEEELEDGW VKSHKINNDP SRLKTDASGE
NSGGNTNDND DTNEINDIDE LIDENAEEQS SEDENDFEEL VETNANSNLR KYDLYITYST
SYRVPKMYLV GFNSNGIPLL PKQMFEDISG DYRDKTATIE TLPVSYNTMS VSIHPCKHSS
VMKVLMAHAA ASKKRENPAD LTDLAEQTGS LNLKDKVPGR DFGEDVDIEE NVPGIRVDQY
LIIFLKFIAS VTPGIEYDYT MDAL
