ATG3_DANRE
ID ATG3_DANRE Reviewed; 317 AA.
AC Q6PFS7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG3;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 3;
DE Short=APG3-like;
GN Name=atg3; Synonyms=apg3l; ORFNames=zgc:64156;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible
CC for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC terminal Gly of atg8-like proteins (gabarap, gabarapl1, gabarapl2 or
CC map1lc3a). The atg12-atg5 conjugate plays a role of an E3 and promotes
CC the transfer of atg8-like proteins from atg3 to
CC phosphatidylethanolamine (PE). This step is required for the membrane
CC association of atg8-like proteins. The formation of the atg8-
CC phosphatidylethanolamine conjugates is essential for autophagy and for
CC the cytoplasm to vacuole transport (Cvt). Also acts as an autocatalytic
CC E2-like enzyme, catalyzing the conjugation of atg12 to itself, atg12
CC conjugation to atg3 playing a role in mitochondrial homeostasis but not
CC in autophagy. atg7 (E1-like enzyme) facilitates this reaction by
CC forming an E1-E2 complex with atg3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with atg7 and atg12. The complex composed of atg3
CC and atg7 plays a role in the conjugation of atg12 to atg5.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Conjugated to atg12 at Lys-246. ATG12-conjugation plays a role in
CC regulation of mitochondrial homeostasis and cell death, while it is not
CC involved in PE-conjugation to ATG8-like proteins and autophagy (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; BC057434; AAH57434.1; -; mRNA.
DR RefSeq; NP_956316.1; NM_200022.1.
DR AlphaFoldDB; Q6PFS7; -.
DR SMR; Q6PFS7; -.
DR STRING; 7955.ENSDARP00000041303; -.
DR PaxDb; Q6PFS7; -.
DR DNASU; 336632; -.
DR Ensembl; ENSDART00000041304; ENSDARP00000041303; ENSDARG00000009350.
DR GeneID; 336632; -.
DR KEGG; dre:336632; -.
DR CTD; 64422; -.
DR ZFIN; ZDB-GENE-030131-8576; atg3.
DR eggNOG; KOG2981; Eukaryota.
DR GeneTree; ENSGT00390000010308; -.
DR HOGENOM; CLU_027518_0_0_1; -.
DR InParanoid; Q6PFS7; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; Q6PFS7; -.
DR TreeFam; TF105903; -.
DR Reactome; R-DRE-1632852; Macroautophagy.
DR PRO; PR:Q6PFS7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000009350; Expressed in spleen and 30 other tissues.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019777; F:Atg12 transferase activity; ISS:UniProtKB.
DR GO; GO:0019776; F:Atg8 ligase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Isopeptide bond; Protein transport;
KW Reference proteome; Transferase; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..317
FT /note="Ubiquitin-like-conjugating enzyme ATG3"
FT /id="PRO_0000213572"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 35699 MW; 2FC8CD5FCC5639BC CRC64;
MQNVINSVKG TALGVAEFLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWKWASGEE
AKVKPYLPND KQFLLTRNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT FHNSGVTGVT
EAVREISLDN KDNMNMNVKT GACGNSGDDD DDEEGEAADM EEYEESGLLE TDDATLDTSK
MADLSKTKAE AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEDRQPL TVDQMYEDIS
QDHVKKTVTI ENHPNLPPPA MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV
QAVIPTIEYD YTRHFTM