ATG3_RAT
ID ATG3_RAT Reviewed; 314 AA.
AC Q6AZ50; Q9ESH2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG3;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 3;
DE Short=APG3-like;
DE AltName: Full=Preconditioning-inducible gene 1 protein;
GN Name=Atg3; Synonyms=Apg3l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Laser M., Li Y., Xu L., Darden A., Wu B.X., Hazard E.S. III, Crosson C.,
RA Ma J.X.;
RT "Identification and characterization of a novel gene induced by ischemic
RT preconditioning in the retina.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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). Preferred substrate is
CC MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the
CC conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a
CC role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like
CC enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3
CC (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. Interacts
CC with FNBP1L. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Conjugated to ATG12 at Lys-243. 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 -!- PTM: Cleaved by CASP8 upon death ligand binding such as tumor necrosis
CC factor-alpha. CASP8 cleavage blocks survival-related autophagy and
CC favors apoptosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; AF175224; AAG09182.1; -; mRNA.
DR EMBL; BC078743; AAH78743.1; -; mRNA.
DR RefSeq; NP_599221.1; NM_134394.2.
DR AlphaFoldDB; Q6AZ50; -.
DR SMR; Q6AZ50; -.
DR BioGRID; 251241; 1.
DR STRING; 10116.ENSRNOP00000002906; -.
DR PhosphoSitePlus; Q6AZ50; -.
DR jPOST; Q6AZ50; -.
DR PaxDb; Q6AZ50; -.
DR PRIDE; Q6AZ50; -.
DR Ensembl; ENSRNOT00000002906; ENSRNOP00000002906; ENSRNOG00000002094.
DR GeneID; 171415; -.
DR KEGG; rno:171415; -.
DR UCSC; RGD:708464; rat.
DR CTD; 64422; -.
DR RGD; 708464; Atg3.
DR eggNOG; KOG2981; Eukaryota.
DR GeneTree; ENSGT00390000010308; -.
DR HOGENOM; CLU_027518_0_0_1; -.
DR InParanoid; Q6AZ50; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; Q6AZ50; -.
DR TreeFam; TF105903; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR PRO; PR:Q6AZ50; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002094; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q6AZ50; RN.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0019777; F:Atg12 transferase activity; ISS:UniProtKB.
DR GO; GO:0019776; F:Atg8 ligase activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEP:RGD.
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:0016236; P:macroautophagy; ISO:RGD.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:1902017; P:regulation of cilium assembly; ISO:RGD.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cytoplasm; Isopeptide bond; Protein transport;
KW Reference proteome; Transferase; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..314
FT /note="Ubiquitin-like-conjugating enzyme ATG3"
FT /id="PRO_0000213571"
FT ACT_SITE 264
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NT62"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
FT CONFLICT 257
FT /note="P -> L (in Ref. 1; AAG09182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35822 MW; 4C78AB0F628C9BDF CRC64;
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
EAVKEITLES KDSIKLQDCS VLCDEEEEEE EGEAADMEEY EESGLLETDE ATLDTRRIVE
ACKAKADAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
IPTIEYDYTR HFTM
