ID   ATG3_CHAGB              Reviewed;         338 AA.
AC   Q2H427;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN   Name=ATG3; ORFNames=CHGG_06588;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ89969.1; -; Genomic_DNA.
DR   RefSeq; XP_001222683.1; XM_001222682.1.
DR   AlphaFoldDB; Q2H427; -.
DR   SMR; Q2H427; -.
DR   STRING; 38033.XP_001222683.1; -.
DR   EnsemblFungi; EAQ89969; EAQ89969; CHGG_06588.
DR   GeneID; 4390343; -.
DR   eggNOG; KOG2981; Eukaryota.
DR   HOGENOM; CLU_027518_2_0_1; -.
DR   InParanoid; Q2H427; -.
DR   OMA; YDKYYQV; -.
DR   OrthoDB; 1432328at2759; -.
DR   Proteomes; UP000001056; 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   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..338
FT                   /note="Autophagy-related protein 3"
FT                   /id="PRO_0000317821"
FT   REGION          85..167
FT                   /note="Flexible region"
FT                   /evidence="ECO:0000250"
FT   REGION          135..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..319
FT                   /note="Handle region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        141..158
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        238
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  37395 MW;  D13FBF464AC887CB CRC64;
     MNIIYSTVNS LRDRYTPASH TSTFRNTGEI TPEEFVAAGD YLVFKFPSWT WSDAETPAKR
     VAHLPPEKQY LVTRNVPCHR RLNDDFAGDA GHEEAVVEGG KNSGDDGWLR TGGLASSQPL
     KARDVRTVDD AGNVADRGAI DDEDDIPDME EEEDDEAIIQ DGSHGKHSGS RTYSLYITYS
     PWYKTPRMYM LGYQPNGQAL IPHLMMEDIV GDYKDKTVTL EDFPFFATSV KTASIHPCKH
     APVMKTLLDR ADAALKLRKE RQKAGLEVGS NQGLEGLEAQ VVKLAVSGTG TDVANDANDE
     WEEVQHDAAD QDVAIRVDQY LFIASVTPGI EHDFTMGV