ATG3_SORMK
ID ATG3_SORMK Reviewed; 346 AA.
AC F7VSU2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Autophagy-related protein 3 {ECO:0000303|PubMed:27309377};
DE AltName: Full=Autophagy-related E2-like conjugation enzyme atg3 {ECO:0000303|PubMed:27309377};
GN Name=ATG3 {ECO:0000303|PubMed:27309377}; ORFNames=SMAC_05399;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
RN [2]
RP INTERACTION WITH ATG12.
RX PubMed=27309377; DOI=10.1371/journal.pone.0157960;
RA Werner A., Herzog B., Frey S., Poeggeler S.;
RT "Autophagy-Associated Protein SmATG12 Is Required for Fruiting-Body
RT Formation in the Filamentous Ascomycete Sordaria macrospora.";
RL PLoS ONE 11:E0157960-E0157960(2016).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy (By similarity). 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 -!- SUBUNIT: Monomer (By similarity). Interacts with ATG8 through an
CC intermediate thioester bond between Cys-238 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 (PubMed:27309377). {ECO:0000250|UniProtKB:P40344,
CC ECO:0000269|PubMed:27309377}.
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 -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; CABT02000006; CCC08759.1; -; Genomic_DNA.
DR RefSeq; XP_003347100.1; XM_003347052.1.
DR AlphaFoldDB; F7VSU2; -.
DR SMR; F7VSU2; -.
DR STRING; 771870.F7VSU2; -.
DR EnsemblFungi; CCC08759; CCC08759; SMAC_05399.
DR GeneID; 10804596; -.
DR KEGG; smp:SMAC_05399; -.
DR VEuPathDB; FungiDB:SMAC_05399; -.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; F7VSU2; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR Proteomes; UP000001881; 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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..346
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000443872"
FT REGION 84..158
FT /note="Flexible region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT REGION 242..322
FT /note="Handle region"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT ACT_SITE 238
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P40344"
SQ SEQUENCE 346 AA; 38373 MW; 98985C1140EBFE7F CRC64;
MNFLRSTAAT LLDKYTPVSH TSTFRNTGQI TPEEFVAAGD YLTFKFPSWS WADADSPSKR
LTFLPAGKQF LVTRHVPCHR RLNNDFAGDA GHEEALVEGN KGGDDDDGWL RTGSMTSSQP
LRVREVRNID DAGNVGDREV VDEDDIPDME DDDDDEAIIR AEGDNSNSGK RTYTLYITYA
NAYKCPRMYM SGYLANGQPL PPHLMMEDIV GDYKDKTVTL EDFPFFSHSV KMASVHPCRH
ASVMKTLLDR ADAALKLRRE KMKAGQGSGS EQGMEGLVDE INKLDVSGAH ANAVEAAPGE
DAEWEEVPHD VTDQEVAIRV DQYLVVFLKF IASVTPGIEH DFTMGV
