ATG3_VANPO
ID ATG3_VANPO Reviewed; 318 AA.
AC A7TK16;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN Name=ATG3; ORFNames=Kpol_1060p18;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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).
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; DS480405; EDO17362.1; -; Genomic_DNA.
DR RefSeq; XP_001645220.1; XM_001645170.1.
DR AlphaFoldDB; A7TK16; -.
DR SMR; A7TK16; -.
DR STRING; 436907.A7TK16; -.
DR EnsemblFungi; EDO17362; EDO17362; Kpol_1060p18.
DR GeneID; 5545579; -.
DR KEGG; vpo:Kpol_1060p18; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; A7TK16; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; A7TK16; -.
DR Proteomes; UP000000267; 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..318
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317830"
FT REGION 83..164
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 122..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..293
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 318 AA; 36469 MW; 6EE71061192AE5C2 CRC64;
MLRSTLSSWR EYLTPVSHKS TFLSSGQITP DEFVQAGDYL CHMFPTWEWN KAGNDVLFRN
FLPEDKQFLV MRKVPCNVRA KQFVNIDDSA SEAFVQGIND EDGSIENGWM IGGGETDHLS
KHSLSSGDVT PSGNNTKTMD ETTPDIDDLM ESMGIEDTDD IIDTPQNTDR RYYDLYITYS
TSYKVPKMYI VGFNGSGSPL TPEEMFEDIA PDYRSKTATI EKLPFYKNTI SSVSIHPCKH
ANVMRILLDK VLVVKRRRRE EMSENHNEHK PNPESDEWED LQNDVDDTIR ADQYLIIFLK
FITSVTPGIE HDYTMEGW