ATG12_RAT
ID ATG12_RAT Reviewed; 141 AA.
AC Q2TBJ5; Q5M9F9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ubiquitin-like protein ATG12;
DE AltName: Full=Autophagy-related protein 12;
DE Short=APG12-like;
GN Name=Atg12; Synonyms=Apg12l;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Placenta;
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).
RN [2]
RP INDUCTION.
RX PubMed=18521932; DOI=10.1002/jnr.21738;
RA Kim S.H., Munemasa Y., Kwong J.M., Ahn J.H., Mareninov S., Gordon L.K.,
RA Caprioli J., Piri N.;
RT "Activation of autophagy in retinal ganglion cells.";
RL J. Neurosci. Res. 86:2943-2951(2008).
RN [3]
RP INDUCTION.
RX PubMed=19696026; DOI=10.1074/jbc.m109.024406;
RA Sengupta A., Molkentin J.D., Yutzey K.E.;
RT "FoxO transcription factors promote autophagy in cardiomyocytes.";
RL J. Biol. Chem. 284:28319-28331(2009).
CC -!- FUNCTION: Ubiquitin-like protein involved in autophagy vesicles
CC formation. Conjugation with ATG5 through a ubiquitin-like conjugating
CC system involving also ATG7 as an E1-like activating enzyme and ATG10 as
CC an E2-like conjugating enzyme, is essential for its function. The
CC ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for
CC lipidation of ATG8 family proteins and their association to the vesicle
CC membranes. The ATG12-ATG5 conjugate also regulates negatively the
CC innate antiviral immune response by blocking the type I IFN production
CC pathway through direct association with RARRES3 and MAVS. Also plays a
CC role in translation or delivery of incoming viral RNA to the
CC translation apparatus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a conjugate with ATG5. The ATG12-ATG5 conjugate forms a
CC complex with several units of ATG16L1. Forms an 800-kDa complex
CC composed of ATG12-ATG5 and ATG16L2 (By similarity). Interacts with
CC ATG3, ATG7 and ATG10. ATG12-ATG5 also interacts with MAVS, MGA, RARRES3
CC and TECPR1 (By similarity). {ECO:0000250|UniProtKB:O94817,
CC ECO:0000250|UniProtKB:Q9CQY1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the
CC autolysosomal membrane. {ECO:0000250}.
CC -!- INDUCTION: Activated in retinal ganglion cells (RGCs) following optic
CC nerve transection. Also induced under starvation conditions, through
CC the action of the foxo1 and foxo3 transcription factors.
CC {ECO:0000269|PubMed:18521932, ECO:0000269|PubMed:19696026}.
CC -!- DOMAIN: Shares weak sequence similarity with ubiquitin family, but
CC contains an 'ubiquitin superfold' and the C-terminal Gly is required
CC for isopeptide linkage. {ECO:0000250}.
CC -!- PTM: Acetylated by EP300. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR EMBL; BC087139; AAH87139.1; -; mRNA.
DR EMBL; BC110056; AAI10057.1; -; mRNA.
DR RefSeq; NP_001033584.1; NM_001038495.1.
DR AlphaFoldDB; Q2TBJ5; -.
DR SMR; Q2TBJ5; -.
DR BioGRID; 262598; 1.
DR STRING; 10116.ENSRNOP00000000170; -.
DR jPOST; Q2TBJ5; -.
DR PaxDb; Q2TBJ5; -.
DR PRIDE; Q2TBJ5; -.
DR Ensembl; ENSRNOT00000000170; ENSRNOP00000000170; ENSRNOG00000000157.
DR GeneID; 361321; -.
DR KEGG; rno:361321; -.
DR UCSC; RGD:1306306; rat.
DR CTD; 9140; -.
DR RGD; 1306306; Atg12.
DR eggNOG; KOG3439; Eukaryota.
DR GeneTree; ENSGT00390000016654; -.
DR HOGENOM; CLU_106795_3_0_1; -.
DR InParanoid; Q2TBJ5; -.
DR OMA; LFIYVHQ; -.
DR OrthoDB; 1525971at2759; -.
DR PhylomeDB; Q2TBJ5; -.
DR TreeFam; TF325131; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q2TBJ5; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000000157; Expressed in thymus and 20 other tissues.
DR Genevisible; Q2TBJ5; RN.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; ISO:RGD.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IMP: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:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISO:RGD.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISO:RGD.
DR GO; GO:1904973; P:positive regulation of viral translation; ISO:RGD.
DR GO; GO:0006497; P:protein lipidation; ISO:RGD.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISO:RGD.
DR InterPro; IPR007242; Atg12.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13385; PTHR13385; 1.
DR Pfam; PF04110; APG12; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cytoplasm; Immunity; Innate immunity;
KW Isopeptide bond; Membrane; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..141
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000233273"
FT REGION 24..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor protein)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 141 AA; 15284 MW; 938B3F50F6454CB6 CRC64;
MAEDPEAVLQ LPAAPAAAAG ESLLELSPET AIPEPPSSVA VSPGTEEPPG DTKKKIDILL
KAVGDTPIMK TKKWAVERTR TVQALIDFIR KFLRLLASEQ LFIYVNQSFA PSPDQEVGTL
YECFGSDGKL VLHYCKSQAW G
