ID   ATG5_DROME              Reviewed;         269 AA.
AC   Q9W3R7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Autophagy protein 5;
DE   AltName: Full=APG5-like;
GN   Name=Atg5; ORFNames=CG1643;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=15296714; DOI=10.1016/j.devcel.2004.07.009;
RA   Scott R.C., Schuldiner O., Neufeld T.P.;
RT   "Role and regulation of starvation-induced autophagy in the Drosophila fat
RT   body.";
RL   Dev. Cell 7:167-178(2004).
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 and its
CC       association to the vesicle membranes (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:15296714}.
CC   -!- INTERACTION:
CC       Q9W3R7; Q86BR6: Atg16; NbExp=3; IntAct=EBI-109649, EBI-105321;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC       structure membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- PTM: Conjugated to Atg12, which is essential for autophagy.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF46252.2; -; Genomic_DNA.
DR   EMBL; AY069596; AAL39741.1; -; mRNA.
DR   RefSeq; NP_572390.1; NM_132162.4.
DR   AlphaFoldDB; Q9W3R7; -.
DR   SMR; Q9W3R7; -.
DR   BioGRID; 58142; 29.
DR   DIP; DIP-20667N; -.
DR   IntAct; Q9W3R7; 1.
DR   STRING; 7227.FBpp0071023; -.
DR   PaxDb; Q9W3R7; -.
DR   PRIDE; Q9W3R7; -.
DR   DNASU; 31666; -.
DR   EnsemblMetazoa; FBtr0071065; FBpp0071023; FBgn0029943.
DR   GeneID; 31666; -.
DR   KEGG; dme:Dmel_CG1643; -.
DR   CTD; 9474; -.
DR   FlyBase; FBgn0029943; Atg5.
DR   VEuPathDB; VectorBase:FBgn0029943; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   GeneTree; ENSGT00390000004766; -.
DR   HOGENOM; CLU_051894_1_0_1; -.
DR   InParanoid; Q9W3R7; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   PhylomeDB; Q9W3R7; -.
DR   Reactome; R-DME-1632852; Macroautophagy.
DR   Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy.
DR   BioGRID-ORCS; 31666; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31666; -.
DR   PRO; PR:Q9W3R7; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0029943; Expressed in saliva-secreting gland and 27 other tissues.
DR   Genevisible; Q9W3R7; DM.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; ISS:FlyBase.
DR   GO; GO:0005776; C:autophagosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0006914; P:autophagy; IMP:FlyBase.
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:0009267; P:cellular response to starvation; IMP:FlyBase.
DR   GO; GO:0061723; P:glycophagy; IMP:FlyBase.
DR   GO; GO:0035096; P:larval midgut cell programmed cell death; IMP:FlyBase.
DR   GO; GO:0016236; P:macroautophagy; IMP:FlyBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   Autophagy; Cytoplasm; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..269
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000218998"
FT   CROSSLNK        132
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   269 AA;  31468 MW;  92A3B132FC0146D8 CRC64;
     MAHDREVLRM IWEGQIGICF QADRDEIVGI KPEPFYLMIS RLSYLPLVTD KVRKYFSRYI
     SAEHQDGAVW FDFNGTPLRL HYPIGVLYDL LHPEEDSTPW CLTIHFSKFP EDMLVKLNSK
     ELLESHYMSC LKEADVLKHR GLVISAMQKK DHNQLWLGLV NEKFDQFWAV NRRLMEPYGD
     LESFKNIPLR IYTDDDFTYT QKLISPISVG GQKKSLADLM AELSTPVRRA VGCRTHGIDL
     HEETQLQWMS EHLSYPDNFL HLSVDYKDV