ATG3_ASPOR
ID ATG3_ASPOR Reviewed; 356 AA.
AC Q2U7R4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3;
GN Name=atg3; ORFNames=AO090701000734;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007164; BAE62401.1; -; Genomic_DNA.
DR RefSeq; XP_001823534.1; XM_001823482.2.
DR AlphaFoldDB; Q2U7R4; -.
DR SMR; Q2U7R4; -.
DR STRING; 510516.Q2U7R4; -.
DR EnsemblFungi; BAE62401; BAE62401; AO090701000734.
DR GeneID; 5995591; -.
DR KEGG; aor:AO090701000734; -.
DR VEuPathDB; FungiDB:AO090701000734; -.
DR HOGENOM; CLU_027518_2_0_1; -.
DR OMA; YDKYYQV; -.
DR Proteomes; UP000006564; Chromosome 5.
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:EnsemblFungi.
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 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..356
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317819"
FT REGION 85..174
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 108..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..332
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT COMPBIAS 122..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39939 MW; 85A7E875A2329154 CRC64;
MNILHSTLST WRDRLAPVSR TSTFRNTGQI TPEEFVLAGD YLVYKFPSWS WADASNPAKR
VSYLPPGKQF LVTRGVPCHR RLNDNFAGDA GHDDELVRDM LSGGTGGVDD DGWLRTGGGQ
DSADRQENRI KDVRTVDESG NMGEREEEED EIPDMEDEDD DEEAIIRDPA SGTTQPTRTY
NLYITYSNFY RTPRLYMSGY LSPSEPLPPH LMMEDVVGDY KDKTVTLEDF PWYDGNVKMA
SVHPCRHASV MKTLLDRADA ALKLRREKLK QAQSDPSKAP SVGESGLEGL VDDIKALSLS
DQQQHGSDKS GGDEWEVLQH DEEEQVAIRV DQYLVVFLKF IASVTPGIEH DFTMGV
