ATG3_PENRW
ID ATG3_PENRW Reviewed; 363 AA.
AC A7KAL4; B6HQP6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3;
GN Name=atg3; ORFNames=Pc22g16010;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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). {ECO:0000250,
CC ECO:0000269|PubMed:17204848}.
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; EF107736; ABO31074.1; -; Genomic_DNA.
DR EMBL; AM920437; CAP98889.1; -; Genomic_DNA.
DR RefSeq; XP_002565517.1; XM_002565471.1.
DR AlphaFoldDB; A7KAL4; -.
DR SMR; A7KAL4; -.
DR STRING; 1108849.XP_002565517.1; -.
DR EnsemblFungi; CAP98889; CAP98889; PCH_Pc22g16010.
DR GeneID; 8305155; -.
DR KEGG; pcs:Pc22g16010; -.
DR VEuPathDB; FungiDB:PCH_Pc22g16010; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR BioCyc; PCHR:PC22G16010-MON; -.
DR Proteomes; UP000000724; Contig Pc00c22.
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..363
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317824"
FT REGION 85..176
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 101..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..339
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT COMPBIAS 126..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 40716 MW; 18E43A7D07C7F2F8 CRC64;
MNILHSTLST WRDRLAPVSR TSTFRNTGQI TPEEFVLAGD YLVYKFPTWS WADASSPAKR
VSYLPDGKQF LVTRGVPCHR RLNDNFAGDA GLEDEIVRDF LSGGDGGEGT VADDGEDGWL
RTGGGRDAGA DHDKQEARIR DVRTVDESGN LGEQEEDDDI PDMEDEDDDE EAIIRETDDQ
SGTPSLRTYT LYITYSNFYR TPRLYLSGYL SPSEPLPPHL MMEDIVGDYK DKTVTLEDFP
WFEGSVKMAS VHPCRHASVM KTLLDRADAA LKLRRDKLKQ TQSRDEADRV LRAGGGLEGL
VDETKNMSLG DSHHAQPGGD EWEMLQRDEE EQVAIRVDQY LVVFLKFIAS VTPGIEHDFT
MGV
