ATG5_CAEEL
ID ATG5_CAEEL Reviewed; 275 AA.
AC Q3V5I7; Q3V5I8; W6RR39;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Autophagy-related protein 5 {ECO:0000312|WormBase:Y71G12B.12a};
GN Name=atg-5 {ECO:0000312|WormBase:Y71G12B.12a};
GN Synonyms=atgr-5 {ECO:0000312|WormBase:Y71G12B.12a};
GN ORFNames=Y71G12B.12 {ECO:0000312|WormBase:Y71G12B.12a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH ATG-16.1 AND ATG-16.2, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-130.
RX PubMed=24185444; DOI=10.4161/auto.26095;
RA Zhang H., Wu F., Wang X., Du H., Wang X., Zhang H.;
RT "The two C. elegans ATG-16 homologs have partially redundant functions in
RT the basal autophagy pathway.";
RL Autophagy 9:1965-1974(2013).
CC -!- FUNCTION: Involved in autophagic vesicle formation (By similarity).
CC Conjugation with lgg-3/ATG12, through a ubiquitin-like conjugating
CC system involving atg-7 as an E1-like activating enzyme and atg-10 as an
CC E2-like conjugating enzyme, is essential for its function (By
CC similarity). Most likely a component of an atg-5-lgg-3-atg-16 complex
CC that promotes autophagosome formation by associating with lgg-2, but
CC not lgg-1, at the preautophagosomal membrane (PubMed:24185444).
CC Probably, as part of an atg-5-lgg-3-atg-16 complex, required for lgg-1
CC lipidation; the complex acts as an E3-like enzyme promoting atg-3-
CC mediated lgg-1 lipidation (Probable). Furthermore, association with
CC atg-16.2 is required for the nucleation of lgg-1 positive autophagic
CC vesicles (PubMed:24185444). {ECO:0000250|UniProtKB:Q9H1Y0,
CC ECO:0000269|PubMed:24185444, ECO:0000305|PubMed:24185444}.
CC -!- SUBUNIT: Most likely a component of a complex at least containing atg-
CC 5, lgg-3/ATG12, atg-16.1 and/or atg-16.2 (Probable). Interacts with
CC lgg-3/ATG12 (By similarity). Interacts with atg-16.1 (via N-terminus)
CC and atg-16.2 (via N-terminus) (PubMed:24185444).
CC {ECO:0000255|RuleBase:RU361202, ECO:0000269|PubMed:24185444,
CC ECO:0000305|PubMed:24185444}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000255|RuleBase:RU361202, ECO:0000269|PubMed:24185444};
CC Peripheral membrane protein {ECO:0000255|RuleBase:RU361202}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:Y71G12B.12a};
CC IsoId=Q3V5I7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y71G12B.12b};
CC IsoId=Q3V5I7-2; Sequence=VSP_060205, VSP_060207;
CC Name=c {ECO:0000312|WormBase:Y71G12B.12c};
CC IsoId=Q3V5I7-3; Sequence=VSP_060206;
CC -!- PTM: Conjugated to lgg-3/ATG12; which is essential for autophagy.
CC {ECO:0000250|UniProtKB:W0T4V8}.
CC -!- SIMILARITY: Belongs to the ATG5 family.
CC {ECO:0000255|RuleBase:RU361202}.
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DR EMBL; BX284601; CCD67969.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD67987.1; -; Genomic_DNA.
DR EMBL; BX284601; CDM63580.1; -; Genomic_DNA.
DR RefSeq; NP_001293440.1; NM_001306511.1. [Q3V5I7-3]
DR RefSeq; NP_490885.3; NM_058484.5. [Q3V5I7-1]
DR RefSeq; NP_871858.2; NM_182058.4. [Q3V5I7-2]
DR AlphaFoldDB; Q3V5I7; -.
DR SMR; Q3V5I7; -.
DR ComplexPortal; CPX-3863; atg-5-atg-12-atg-16.1-atg-16.2 complex.
DR ComplexPortal; CPX-3864; ATG12-ATG5 complex.
DR ComplexPortal; CPX-3865; atg-5-atg-12-atg-16.1 complex.
DR ComplexPortal; CPX-3866; atg-5-atg-12-atg-16.2 complex.
DR STRING; 6239.Y71G12B.12a.2; -.
DR EPD; Q3V5I7; -.
DR PaxDb; Q3V5I7; -.
DR PeptideAtlas; Q3V5I7; -.
DR EnsemblMetazoa; Y71G12B.12a.1; Y71G12B.12a.1; WBGene00022152. [Q3V5I7-1]
DR EnsemblMetazoa; Y71G12B.12b.1; Y71G12B.12b.1; WBGene00022152. [Q3V5I7-2]
DR EnsemblMetazoa; Y71G12B.12c.1; Y71G12B.12c.1; WBGene00022152. [Q3V5I7-3]
DR GeneID; 171735; -.
DR KEGG; cel:CELE_Y71G12B.12; -.
DR CTD; 171735; -.
DR WormBase; Y71G12B.12a; CE43967; WBGene00022152; atg-5. [Q3V5I7-1]
DR WormBase; Y71G12B.12b; CE39066; WBGene00022152; atg-5. [Q3V5I7-2]
DR WormBase; Y71G12B.12c; CE39065; WBGene00022152; atg-5. [Q3V5I7-3]
DR eggNOG; KOG2976; Eukaryota.
DR GeneTree; ENSGT00390000004766; -.
DR HOGENOM; CLU_051894_3_0_1; -.
DR InParanoid; Q3V5I7; -.
DR OMA; KWHYPLG; -.
DR OrthoDB; 457861at2759; -.
DR PhylomeDB; Q3V5I7; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-CEL-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q3V5I7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022152; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:1990234; C:transferase complex; IC:ComplexPortal.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:WormBase.
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:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IC:ComplexPortal.
DR GO; GO:0006497; P:protein lipidation; IC:ComplexPortal.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Isopeptide bond; Membrane;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..275
FT /note="Autophagy-related protein 5"
FT /id="PRO_0000447607"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in lgg-3/ATG12)"
FT /evidence="ECO:0000250|UniProtKB:W0T4V8"
FT VAR_SEQ 159..163
FT /note="IPDNF -> SMGVF (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060205"
FT VAR_SEQ 159..161
FT /note="IPD -> N (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060206"
FT VAR_SEQ 164..275
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060207"
FT MUTAGEN 130
FT /note="E->K: In bp546; results in defective degradation of
FT protein aggregates by autophagy."
FT /evidence="ECO:0000269|PubMed:24185444"
SQ SEQUENCE 275 AA; 31339 MW; 5D6691CB9FF94D42 CRC64;
MDYEVCRKVW ESHVPCQFTL QSSGGTHGEP LPFYTMLPRF SYLALAIQKV LSSFNRRDDG
EKVHSDKMWL EHNGIPLKMY IPIGVIYDQA NLSENDSILE IIVRTSQPPP QFQMVDRDMM
EAMFMQNIKE ADYLKTKAEI TKNMMKDESA QLWRSVCNIP DNFDEFWTIV QKLMETSEGN
EFAHIPLRVY VKNQAFKQAL ITAKHPDGSL RTIGEAVSDV LSSSSSSSTD SQSEHPPRLI
SHGIDIPHHT PLIFAAKNLS YPDNFIHVVL LLVVP
