ATG3_XENTR
ID ATG3_XENTR Reviewed; 312 AA.
AC Q5I0S6; Q28GX5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=TEgg015l06.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) 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-241. 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; CR761175; CAJ81702.1; -; mRNA.
DR EMBL; BC088024; AAH88024.1; -; mRNA.
DR RefSeq; NP_001011420.1; NM_001011420.1.
DR AlphaFoldDB; Q5I0S6; -.
DR SMR; Q5I0S6; -.
DR STRING; 8364.ENSXETP00000060161; -.
DR Ensembl; ENSXETT00000005166; ENSXETP00000005166; ENSXETG00000002424.
DR GeneID; 496900; -.
DR KEGG; xtr:496900; -.
DR CTD; 64422; -.
DR Xenbase; XB-GENE-953266; atg3.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_0_0_1; -.
DR InParanoid; Q5I0S6; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; Q5I0S6; -.
DR Reactome; R-XTR-1632852; Macroautophagy.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002424; Expressed in liver and 14 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..312
FT /note="Ubiquitin-like-conjugating enzyme ATG3"
FT /id="PRO_0000213574"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 35526 MW; 5C10E4AA9418C0BA CRC64;
MQSVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFL AAGDHLVHHC PTWQWSAGEE
SKIKPYLPND KQFLMTKNVP CYKRCKQMEY SDEQEAIIEE DDGDGGWVDT FHHSLTGVTE
AVKEITLETQ DCGKTTSNIA VDDDDDDDEG EAADMEDYEE SGLLDNDDAT VDTSKIKEAC
KPKADLGGED AILQTRTYDL YITYDKYYQT PRLWLFGYDE QRRPLTVENM YEDISQDHVK
KTVTIENHPH LPPPPMCSVH PCRHAEVMKK IIETVAEGGG ELGVHMYLLI FLKFVQAVIP
TIEYDYTRHF TM