ATG3_KLUMD
ID ATG3_KLUMD Reviewed; 308 AA.
AC W0TEF9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Autophagy-related protein 3 {ECO:0000303|PubMed:26442587};
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3 {ECO:0000303|PubMed:26442587};
GN Name=ATG3 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_60454;
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA Limtong S., Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT structural and biochemical studies of autophagy.";
RL J. Biol. Chem. 290:29506-29518(2015).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy (PubMed:26442587). Required for selective
CC autophagic degradation of the nucleus (nucleophagy) as well as for
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production (By
CC similarity). Responsible for the E2-like covalent binding of
CC phosphatidylethanolamine to the C-terminal Gly of ATG8 (By similarity).
CC The ATG12-ATG5 conjugate plays a role of an E3 and promotes the
CC transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE) (By
CC similarity). This step is required for the membrane association of ATG8
CC (By similarity). The formation of the ATG8-phosphatidylethanolamine
CC conjugate is essential for autophagy and for the cytoplasm to vacuole
CC transport (Cvt) (By similarity). The ATG8-PE conjugate mediates
CC tethering between adjacent membranes and stimulates membrane
CC hemifusion, leading to expansion of the autophagosomal membrane during
CC autophagy (By similarity). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:26442587}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ATG8 through an
CC intermediate thioester bond between Cys-235 and the C-terminal Gly of
CC ATG8 (By similarity). Interacts with the C-terminal region of the E1-
CC like ATG7 enzyme (By similarity). Interacts also with the ATG12-ATG5
CC conjugate (By similarity). {ECO:0000250|UniProtKB:P40344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC binding and is required for ATG8-PE conjugation (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding (By
CC similarity). {ECO:0000250|UniProtKB:P40344}.
CC -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC (AIM) and mediates binding to ATG8 (By similarity). It is crucial for
CC the cytoplasm-to-vacuole targeting pathway (By similarity).
CC {ECO:0000250|UniProtKB:P40344}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of preautophagosomal
CC structures (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC and have a more ordered secondary structure than their S.cerevisiae
CC counterparts, which might contribute to the superior thermotolerance
CC and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC as a new model organism for further elucidation of the molecular
CC details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; AP012218; BAO41745.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TEF9; -.
DR SMR; W0TEF9; -.
DR EnsemblFungi; BAO41745; BAO41745; KLMA_60454.
DR OrthoDB; 1432328at2759; -.
DR Proteomes; UP000065495; Chromosome 6.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; 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; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..308
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000443871"
FT REGION 83..159
FT /note="Flexible region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT REGION 89..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..283
FT /note="Handle region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT COMPBIAS 93..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40344"
SQ SEQUENCE 308 AA; 35479 MW; 42882CD2F3F8B39B CRC64;
MLRSTLSNWR EYLTPITHTS TFETTGQLTP EEFVKAGDYL VHMFPTWRWN GTDYNNVSYK
DFLPKEKQFL ITRKVPCKLR ASNFVETQTT ETRDVGDGWE LEGQSEGERE SGREDTKSNE
EALASNIEDL QIVDDDESEG GGDEEQLLQN ELADDDDDIV DIKPSTLRYY DLYITYSTSY
RVPKMYLCGF ANEGTPLSPD QMFEDIAPDY RSKTATIEPL PFFKGNQISV SIHPCKHANV
MKVLMEKVRA SRHRARDTEA QKNAEEDWED LQSDIDDGLR VDQYLVVFLK FITSVTPGIE
HDYTMEGW
