ATG3_BOTFB
ID ATG3_BOTFB Reviewed; 347 AA.
AC A6S8P6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3;
GN Name=atg3; ORFNames=BC1G_08793;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476898; EDN29569.1; -; Genomic_DNA.
DR RefSeq; XP_001552315.1; XM_001552265.1.
DR AlphaFoldDB; A6S8P6; -.
DR SMR; A6S8P6; -.
DR OMA; YDKYYQV; -.
DR PHI-base; PHI:7877; -.
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; 2.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..347
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317820"
FT REGION 84..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..171
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 235..323
FT /note="Handle region"
FT /evidence="ECO:0000250"
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 231
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 38699 MW; 2C9FE24C47CC6450 CRC64;
MNFLHSTLDR LREFTPVSNT STFRTNGQIT PEEFVAAGDY LVFKFPTWSW ADASPTSKRA
NYLPAGKQFL VTRGVPCHRR LDDDFAGDAG HDETVVRDGE DFRGDGPHSP GDDEDGWLRT
GGLAASQEAR VRDVRTVDES GEMGEREDDE DDIPDMEDDD DDDEAIIRDP KADNASSTPR
LYLSGYLSSS QPLPPHLMME DIVGDYKDKT VTLEDFPYFS NNIKMASIHP CKHASVMKTL
LDRADAALKL RREKQRQGKA VPGSKDTGME GLVDDFEKTK IGDKKAVLEG LKAGGNGNDE
WEVLQHDQDF ANEEEEVAIR VDQYLVVFLK FMASVTPGIE HDFTMGV
