ATG3_SCLS1
ID ATG3_SCLS1 Reviewed; 362 AA.
AC A7F172;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3;
GN Name=atg3; ORFNames=SS1G_11342;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476638; EDN95464.1; -; Genomic_DNA.
DR RefSeq; XP_001587350.1; XM_001587300.1.
DR AlphaFoldDB; A7F172; -.
DR SMR; A7F172; -.
DR STRING; 665079.A7F172; -.
DR GeneID; 5483489; -.
DR KEGG; ssl:SS1G_11342; -.
DR VEuPathDB; FungiDB:sscle_07g059210; -.
DR InParanoid; A7F172; -.
DR OMA; YDKYYQV; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019776; F:Atg8 ligase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
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..362
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317829"
FT REGION 84..168
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 85..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..338
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT COMPBIAS 85..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40579 MW; 3266501941175EB1 CRC64;
MNFLHSTLDR LREFTPVSNT STFRTNGQIT PEEFVAAGDY LVFKFPTWSW ADASPTSKRA
SYLPAGKQFL VTRGVPCHRR LDDDFAGEAG HDETVVGDGE DFRGTGHSPG DDEDGWLRTG
GLAASQEARA RDVRTVDESG EMGEREDDED DIPDMEDEDD DDEAIIRDPK ADNANSSRRT
YTIYIAYTPY YRTPRLYLSG YLSSSQPLPP HLMMEDIVGD YKDKTVTLED FPYFSNNIKM
ASIHPCKHAS VMKTLLDRAD AALKLRREKQ KQGKTVPGAK DTGMEGLVDD FEKTKISDKK
AMLEGLKAGG NGNDEWEVLQ HDQDFASEEE EVAIRVDQYL VVFLKFMASV TPGIEHDFTM
GV
