ATG3_BOTF1
ID ATG3_BOTF1 Reviewed; 363 AA.
AC M7UQV4;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Autophagy-related protein 3 {ECO:0000303|PubMed:29417220};
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3 {ECO:0000303|PubMed:29417220};
GN Name=atg3 {ECO:0000303|PubMed:29417220}; ORFNames=BcDW1_2003;
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1;
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATG7, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29417220; DOI=10.1007/s00294-018-0810-3;
RA Ren W., Sang C., Shi D., Song X., Zhou M., Chen C.;
RT "Ubiquitin-like activating enzymes BcAtg3 and BcAtg7 participate in
RT development and pathogenesis of Botrytis cinerea.";
RL Curr. Genet. 64:919-930(2018).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy (PubMed:29417220). Required for selective
CC autophagic degradation of the nucleus (nucleophagy) as well as for
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production (By
CC similarity). Responsible for the E2-like covalent binding of
CC phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5
CC conjugate plays a role of an E3 and promotes the transfer of atg8 from
CC atg3 to phosphatidylethanolamine (PE) (By similarity). This step is
CC required for the membrane association of atg8. The formation of the
CC atg8-phosphatidylethanolamine conjugate is essential for autophagy and
CC for the cytoplasm to vacuole transport (Cvt) (By similarity). The atg8-
CC PE conjugate mediates tethering between adjacent membranes and
CC stimulates membrane hemifusion, leading to expansion of the
CC autophagosomal membrane during autophagy (By similarity). Required for
CC normal mycelial growth and conidiogenesis, and regulates sclerotial
CC formation (PubMed:29417220). Plays an essential role in pathogenesis
CC (PubMed:29417220). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:29417220}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with atg8 through an
CC intermediate thioester bond through the C-terminal Gly of atg8 (By
CC similarity). Interacts with the C-terminal region of the E1-like atg7
CC enzyme (PubMed:29417220). Interacts also with the atg12-atg5 conjugate
CC (By similarity). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:29417220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29417220}.
CC -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC binding and is required for atg8-PE conjugation (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The flexible region (FR) is required for atg7-binding (By
CC similarity). {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 (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DISRUPTION PHENOTYPE: Blocks the autophagic process (PubMed:29417220).
CC Leads to fewer aerial hyphae and slower mycelial growth rate and fails
CC to produce any conidia (PubMed:29417220). Reduces also the production
CC of sclerotia in cold environment (PubMed:29417220). Fails to infect
CC wounded cucumber leaves and shows only slight virulence on wounded
CC tomato and grape fruits (PubMed:29417220).
CC {ECO:0000269|PubMed:29417220}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; KB707749; EMR89343.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UQV4; -.
DR SMR; M7UQV4; -.
DR STRING; 1290391.M7UQV4; -.
DR EnsemblFungi; EMR89343; EMR89343; BcDW1_2003.
DR HOGENOM; CLU_027518_2_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..363
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000443869"
FT REGION 84..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..171
FT /note="Flexible region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT REGION 251..339
FT /note="Handle region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT COMPBIAS 84..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40344"
SQ SEQUENCE 363 AA; 40768 MW; 27AE827CCDAD925C CRC64;
MNFLHSTLDR LREFTPVSNT STFRTNGQIT PEEFVAAGDY LVFKFPTWSW ADASPTSKRA
NYLPAGKQFL VTRGVPCHRR LDDDFAGDAG HDETVVRDGE DFRGDGPHSP GDDEDGWLRT
GGLAASQEAR VRDVRTVDES GEMGEREDDE DDIPDMEDDD DDDEAIIRDP KADNASSSRR
TYTIYIAYTP YYRTPRLYLS GYLSSSQPLP PHLMMEDIVG DYKDKTVTLE DFPYFSNNIK
MASIHPCKHA SVMKTLLDRA DAALKLRREK QRQGKAVPGS KDTGMEGLVD DFEKTKIGDK
KAVLEGLKAG GNGNDEWEVL QHDQDFANEE EEVAIRVDQY LVVFLKFMAS VTPGIEHDFT
MGV
