ID   ATG3_XENLA              Reviewed;         313 AA.
AC   Q6GQE7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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-242. 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; BC072798; AAH72798.1; -; mRNA.
DR   RefSeq; NP_001085459.1; NM_001091990.2.
DR   AlphaFoldDB; Q6GQE7; -.
DR   SMR; Q6GQE7; -.
DR   PRIDE; Q6GQE7; -.
DR   DNASU; 443885; -.
DR   GeneID; 443885; -.
DR   KEGG; xla:443885; -.
DR   CTD; 443885; -.
DR   Xenbase; XB-GENE-953272; atg3.S.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 443885; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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..313
FT                   /note="Ubiquitin-like-conjugating enzyme ATG3"
FT                   /id="PRO_0000213573"
FT   ACT_SITE        263
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  35644 MW;  71922B319A9667CA CRC64;
     MQNVFNTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFL AAGDHLVHHC PTWQWSAGEE
     SKIKPYLPND KQFLMTKNVP CYKRCKQMEY SDEQEAIIEE DDGDGGWVDT FHHTGLSGVT
     EAVKEITLET QDCGKTTDNI AVCDDDDDDE GEAADMEDYE ESGLLENDDA TVDTSKIKEA
     CKPKADLGGE DAILQTRTYD LYITYDKYYQ TPRLWLFGYD EQRRPLAVEN MYEDISQDHV
     KKTVTIENHP HLPPPPMCSV HPCRHAEVMK KIIETVAEGG GELGVHMYLL IFLKFVQAVI
     PTIEYDYTRH FTM