ATG3_MAGO7
ID ATG3_MAGO7 Reviewed; 350 AA.
AC Q51LD2; A4RBA2; G4NLC0; Q2KFF3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Autophagy-related protein 3 {ECO:0000303|PubMed:30776962};
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3 {ECO:0000303|PubMed:30776962};
GN Name=ATG3 {ECO:0000303|PubMed:30776962}; ORFNames=MGCH7_ch7g733, MGG_02959;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, INTERACTION WITH HAT1 AND ATG8, SUBCELLULAR LOCATION, ACETYLATION
RP AT LYS-262 AND LYS-267, AND MUTAGENESIS OF LYS-262 AND LYS-267.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
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 (PubMed:30776962). Plays a role in appressorium formation and
CC pathogenicity (PubMed:30776962). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:30776962}.
CC -!- SUBUNIT: Monomer. Interacts with ATG8 through an intermediate thioester
CC bond through the C-terminal Gly of ATG8 (By similarity)
CC (PubMed:30776962). Also interacts with the 40 amino acid C-terminal
CC region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5
CC conjugate (By similarity). Interacts with HAT1 (PubMed:30776962).
CC {ECO:0000250|UniProtKB:P40344, ECO:0000269|PubMed:30776962}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:30776962}. Cytoplasm
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC binding and is required for ATG8-PE conjugation.
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC {ECO:0000250|UniProtKB:P40344}.
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. {ECO:0000250|UniProtKB:P40344}.
CC -!- PTM: Acetylated by HAT1 at Lys-262 and Lys-267, which affects the
CC interaction with ATG8 and prevents autophagy during both appressorium
CC development and nutrient starvation. {ECO:0000269|PubMed:30776962}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; CM000230; EAQ71326.1; -; Genomic_DNA.
DR EMBL; CM001237; EHA46004.1; -; Genomic_DNA.
DR RefSeq; XP_003720747.1; XM_003720699.1.
DR AlphaFoldDB; Q51LD2; -.
DR SMR; Q51LD2; -.
DR STRING; 318829.MGG_17909T0; -.
DR iPTMnet; Q51LD2; -.
DR EnsemblFungi; MGG_17909T0; MGG_17909T0; MGG_17909.
DR GeneID; 12984780; -.
DR KEGG; mgr:MGG_17909; -.
DR VEuPathDB; FungiDB:MGG_17909; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; Q51LD2; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PHI-base; PHI:2071; -.
DR Proteomes; UP000009058; Chromosome 7.
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:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasm; Germination; Protein transport;
KW Reference proteome; Stress response; Transport; Ubl conjugation pathway;
KW Virulence.
FT CHAIN 1..350
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000213582"
FT REGION 85..166
FT /note="Flexible region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT REGION 97..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..326
FT /note="Handle region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30776962"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30776962"
FT MUTAGEN 262
FT /note="K->R: Weakens acetylation levels of ATG3; when
FT associated with R-267."
FT /evidence="ECO:0000269|PubMed:30776962"
FT MUTAGEN 267
FT /note="K->R: Weakens acetylation levels of ATG3; when
FT associated with R-262."
FT /evidence="ECO:0000269|PubMed:30776962"
SQ SEQUENCE 350 AA; 38938 MW; 2AECA50BB39BB662 CRC64;
MNSLYSVVNT LRDRYAPVSH TSTFRQTGEI TPEEFVAAGD YLVFKFPTWS WGDADSESRR
ASHLPPGKQF LVTRNVPCNR RLNENFAGDA GLEEAVVDDG DEFKGSKGDD DGWLRTGGLS
SSQPLKAREV RTVDDAGNAG ERAQPDDDDD IPDMEDEEDD EAIIRDTDAS GQTSSRRTYT
LYIMYSPYYR TPRLYLSGYG ANGQPLPPHN MMEDIMGDYK DKTVTLEDFP FFANNIKMAS
VHPCKHAPVM KTLLDRADAA LKLRREKLKT GDASGQQAGL EGLADEFNKL GVSGKGDASK
IDKNDEWEDI QHDDVADQEV AIRVDQYLVV FLKFIASVTP GIEHDFTMGV
