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ATG5_RAT
ID   ATG5_RAT                Reviewed;         275 AA.
AC   Q3MQ06;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Autophagy protein 5;
GN   Name=Atg5;
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].
RC   STRAIN=Wistar;
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.
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 Bassoon/BSN; this interaction
CC       is important for the regulation of presynaptic autophagy (By
CC       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; AM087012; CAJ31281.1; -; mRNA.
DR   AlphaFoldDB; Q3MQ06; -.
DR   SMR; Q3MQ06; -.
DR   IntAct; Q3MQ06; 1.
DR   STRING; 10116.ENSRNOP00000053910; -.
DR   PhosphoSitePlus; Q3MQ06; -.
DR   jPOST; Q3MQ06; -.
DR   PaxDb; Q3MQ06; -.
DR   Ensembl; ENSRNOT00000080283; ENSRNOP00000075339; ENSRNOG00000000322.
DR   UCSC; RGD:1359580; rat.
DR   RGD; 1359580; Atg5.
DR   eggNOG; KOG2976; Eukaryota.
DR   GeneTree; ENSGT00390000004766; -.
DR   InParanoid; Q3MQ06; -.
DR   PhylomeDB; Q3MQ06; -.
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:Q3MQ06; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; ISO:RGD.
DR   GO; GO:0005776; C:autophagosome; ISO:RGD.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
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:0035973; P:aggrephagy; ISO:RGD.
DR   GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; ISO:RGD.
DR   GO; GO:0000045; P:autophagosome assembly; IMP:RGD.
DR   GO; GO:0006914; P:autophagy; IMP:RGD.
DR   GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR   GO; GO:0061684; P:chaperone-mediated autophagy; IMP:ARUK-UCL.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; ISO:RGD.
DR   GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR   GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; ISO:RGD.
DR   GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; ISO:RGD.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; ISO:RGD.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; ISO:RGD.
DR   GO; GO:0039689; P:negative stranded viral RNA replication; ISO:RGD.
DR   GO; GO:0045060; P:negative thymic T cell selection; ISO:RGD.
DR   GO; GO:0048840; P:otolith development; ISO:RGD.
DR   GO; GO:0070257; P:positive regulation of mucus secretion; ISO:RGD.
DR   GO; GO:1904973; P:positive regulation of viral translation; ISO:RGD.
DR   GO; GO:0043687; P:post-translational protein modification; ISO:RGD.
DR   GO; GO:0006497; P:protein lipidation; ISO:RGD.
DR   GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   GO; GO:1901096; P:regulation of autophagosome maturation; ISO:RGD.
DR   GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR   GO; GO:0002718; P:regulation of cytokine production involved in immune response; ISO:RGD.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR   GO; GO:1902617; P:response to fluoride; IEP:RGD.
DR   GO; GO:0009620; P:response to fungus; ISO:RGD.
DR   GO; GO:0010040; P:response to iron(II) ion; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR   GO; GO:0042311; P:vasodilation; ISO:RGD.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; ISO:RGD.
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_0000250584"
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"
SQ   SEQUENCE   275 AA;  32398 MW;  1F6EDC95C7870105 CRC64;
     MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
     RQEDVSEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPCKDA
     VEAHFMSCVK EADALKHKSQ VINEMQRKDH KQLWMGLQND RFDQFWTINR KLMEYPPEEN
     GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLR EVCPSAVAPE DGEKKSQVMI
     HGIEPLLETP LQWLSEHLSY PDNFLHISIV PQPTD
 
 
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