ATG5_BOVIN
ID ATG5_BOVIN Reviewed; 275 AA.
AC Q3MQ24; Q3SZN7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Autophagy protein 5;
GN Name=ATG5;
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 [MRNA].
RA Botti J., Djavaheri-Mergny M., Codogno P., Oriol R.;
RT "Phylogeny and biochemistry of the autophagy protein beclin 1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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: Involved in autophagic vesicle formation. Conjugation with
CC ATG12, through a ubiquitin-like conjugating system involving ATG7 as an
CC E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme,
CC is essential for its function. The ATG12-ATG5 conjugate acts as an E3-
CC like enzyme which is required for lipidation of ATG8 family proteins
CC and their association to the vesicle membranes. Involved in
CC mitochondrial quality control after oxidative damage, and in subsequent
CC cellular longevity. Plays a critical role in multiple aspects of
CC lymphocyte development and is essential for both B and T lymphocyte
CC survival and proliferation. Required for optimal processing and
CC presentation of antigens for MHC II. Involved in the maintenance of
CC axon morphology and membrane structures, as well as in normal adipocyte
CC differentiation. Promotes primary ciliogenesis through removal of OFD1
CC from centriolar satellites and degradation of IFT20 via the autophagic
CC pathway. {ECO:0000250|UniProtKB:Q99J83, ECO:0000250|UniProtKB:Q9H1Y0}.
CC -!- FUNCTION: May play an important role in the apoptotic process, possibly
CC within the modified cytoskeleton. Its expression is a relatively late
CC event in the apoptotic process, occurring downstream of caspase
CC activity. Plays a crucial role in IFN-gamma-induced autophagic cell
CC death by interacting with FADD. {ECO:0000250|UniProtKB:Q9H1Y0}.
CC -!- SUBUNIT: Forms a conjugate with ATG12. The ATG5-ATG12 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 TECPR1; the interaction is direct and does not take place when ATG16L1
CC is associated with the ATG5-ATG12 conjugate. Interacts with DHX58/RIG-
CC 1, IFIH1/MDA5 and MAVS/IPS-1 in monomeric form as well as in ATG12-ATG5
CC conjugate form. The interaction with MAVS is further enhanced upon
CC vesicular stomatitis virus (VSV) infection. Interacts with ATG3 (By
CC similarity). Interacts with ATG7 and ATG10 (By similarity). Interacts
CC with FADD (By similarity). Interacts with ATG16L2 (By similarity).
CC {ECO:0000250|UniProtKB:Q99J83, ECO:0000250|UniProtKB:Q9H1Y0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H1Y0}.
CC Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The conjugate detaches from the membrane
CC immediately before or after autophagosome formation is completed.
CC Localizes also to discrete punctae along the ciliary axoneme and to the
CC base of the ciliary axoneme. {ECO:0000250}.
CC -!- PTM: Conjugated to ATG12; which is essential for autophagy, but is not
CC required for association with isolation membrane. {ECO:0000250}.
CC -!- PTM: Acetylated by EP300. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR EMBL; AM086994; CAJ31263.1; -; mRNA.
DR EMBL; BC102770; AAI02771.1; -; mRNA.
DR RefSeq; NP_001029751.2; NM_001034579.2.
DR AlphaFoldDB; Q3MQ24; -.
DR SMR; Q3MQ24; -.
DR STRING; 9913.ENSBTAP00000007100; -.
DR PaxDb; Q3MQ24; -.
DR PRIDE; Q3MQ24; -.
DR Ensembl; ENSBTAT00000007100; ENSBTAP00000007100; ENSBTAG00000005400.
DR GeneID; 532686; -.
DR KEGG; bta:532686; -.
DR CTD; 9474; -.
DR VEuPathDB; HostDB:ENSBTAG00000005400; -.
DR VGNC; VGNC:56361; ATG5.
DR eggNOG; KOG2976; Eukaryota.
DR GeneTree; ENSGT00390000004766; -.
DR HOGENOM; CLU_051894_3_0_1; -.
DR InParanoid; Q3MQ24; -.
DR OMA; KWHYPLG; -.
DR OrthoDB; 457861at2759; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000005400; Expressed in oocyte and 109 other tissues.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR GO; GO:0005776; C:autophagosome; IEA:Ensembl.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0035973; P:aggrephagy; IEA:Ensembl.
DR GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; 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:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IEA:Ensembl.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IEA:Ensembl.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0048840; P:otolith development; IEA:Ensembl.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:1904973; P:positive regulation of viral translation; IEA:Ensembl.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:1901096; P:regulation of autophagosome maturation; IEA:Ensembl.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0002718; P:regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
DR Gene3D; 1.10.246.190; -; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR InterPro; IPR007239; Atg5.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR042527; Atg5_UblA_dom.
DR PANTHER; PTHR13040; PTHR13040; 1.
DR Pfam; PF04106; APG5; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Autophagy; Cytoplasm; Immunity; Isopeptide bond;
KW Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..275
FT /note="Autophagy protein 5"
FT /id="PRO_0000218993"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1Y0"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
FT CONFLICT 235
FT /note="K -> N (in Ref. 1; CAJ31263)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 32431 MW; DEF2EE50B38BB34B CRC64;
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDV
IEAHFMSCVK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN
GFRYIPFRIY QTTTERPFIQ KLFRPVSTDG QLHTLGDLLK EVCPSAVAPE DGEKKNQVMI
HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD
