ATG12_BOVIN
ID ATG12_BOVIN Reviewed; 140 AA.
AC Q3T0W7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ubiquitin-like protein ATG12;
DE AltName: Full=Autophagy-related protein 12;
DE Short=APG12-like;
GN Name=ATG12;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC102225; AAI02226.1; -; mRNA.
DR RefSeq; NP_001070450.1; NM_001076982.1.
DR AlphaFoldDB; Q3T0W7; -.
DR SMR; Q3T0W7; -.
DR STRING; 9913.ENSBTAP00000023301; -.
DR PaxDb; Q3T0W7; -.
DR PRIDE; Q3T0W7; -.
DR GeneID; 767903; -.
DR KEGG; bta:767903; -.
DR CTD; 9140; -.
DR eggNOG; KOG3439; Eukaryota.
DR InParanoid; Q3T0W7; -.
DR OrthoDB; 1525971at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
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 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..140
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000233272"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor protein)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15285 MW; 15C72EBA52F3DC46 CRC64;
MAEEQESALQ LPPSTAPEAE VPTEVSPETA TPEPPSSAAV SPGTEEPVGD TKKKIDILLK
AVGDTPIMKT KKWAVERTRT IQGLFDFIKK FLKLVASEQL FIYVNQSFAP SPDQEVGTLY
ECFGSDGKLV LHYCKSQAWG