ID   ATG3_PICAN              Reviewed;         339 AA.
AC   A7KAI2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN   Name=ATG3;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
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).
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; EF102883; ABO31287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAI2; -.
DR   SMR; A7KAI2; -.
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; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..339
FT                   /note="Autophagy-related protein 3"
FT                   /id="PRO_0000317826"
FT   REGION          86..182
FT                   /note="Flexible region"
FT                   /evidence="ECO:0000250"
FT   REGION          255..314
FT                   /note="Handle region"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        251
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  38371 MW;  7679BF9F15234D7A CRC64;
     MTGLYLRSTF SSLREYLTPI SHKSTFTDTG EITPEEFVAA GDYLVYKFPT WQWSPAPESK
     KRDFLPNDKQ FLVTRHVPSY VRAADYEHTE KEAEMMEEED GWTSTNVDSV APQRCNTEDE
     RRHSIKYIEM TESGASSPEE GLAQHEGSGK HEINDIDELI DETAEESDLA NDAGQGGIIN
     DPKKRNYDLY ITYSTSYRVP KMYLVGFNSN GVPLSPNEMF EDIASDYRQK TVTIEKAPFL
     SNTTSVSIHP CRHANVMRVL MKRAAHAAQA KKIRDKDLVT GVAKLGLADG KNADEEDDWE
     NVEQGEEGII RVDQYLVIFL KFIASVTPGI EYDYTMDAF