ATG5_DEBHA
ID ATG5_DEBHA Reviewed; 292 AA.
AC Q6BVI8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Autophagy protein 5;
GN Name=ATG5; OrderedLocusNames=DEHA2C02332g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC autophagic vesicle formation. Autophagy is essential for maintenance of
CC amino acid levels and protein synthesis under nitrogen starvation.
CC Required for selective autophagic degradation of the nucleus
CC (nucleophagy). Also required for mitophagy, which eliminates defective
CC or superfluous mitochondria in order to fulfill cellular energy
CC requirements and prevent excess ROS production. Conjugation with ATG12,
CC through a ubiquitin-like conjugating system involving ATG7 as an E1-
CC like activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC essential for its function. The ATG12-ATG5 conjugate acts as an E3-like
CC enzyme which is required for lipidation of ATG8 and ATG8 association to
CC the vesicle membranes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Conjugated with ATG12. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {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; CR382135; CAG85819.2; -; Genomic_DNA.
DR RefSeq; XP_457781.2; XM_457781.1.
DR AlphaFoldDB; Q6BVI8; -.
DR SMR; Q6BVI8; -.
DR STRING; 4959.XP_457781.2; -.
DR EnsemblFungi; CAG85819; CAG85819; DEHA2C02332g.
DR GeneID; 2900722; -.
DR KEGG; dha:DEHA2C02332g; -.
DR VEuPathDB; FungiDB:DEHA2C02332g; -.
DR eggNOG; KOG2976; Eukaryota.
DR HOGENOM; CLU_051894_2_0_1; -.
DR InParanoid; Q6BVI8; -.
DR OMA; KWHYPLG; -.
DR OrthoDB; 457861at2759; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Autophagy; Isopeptide bond; Membrane; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..292
FT /note="Autophagy protein 5"
FT /id="PRO_0000219003"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 34128 MW; FEE1EFCF26A38AF7 CRC64;
MQSSNELIEI KDKLWNGSIN VRILMGDDNI KDPKEFLITV YRNSYFPIYF PSVITYFQKY
NEKIKYMPVW LEYETVPIKW NLPIGVLYDL LHLSSIVQNR EDSSWTLTLR FSDDYPTDQV
IPFTYTDVDN SVNYNKSLKE VVVNQLKQSC FVINGNSKPI MNLSEKDSDE LWNSIRIHNL
KSFNQINKKI IPIQKKFQKL PVKIYIPGSA TIIHAPIYPY SDSGEAVLLR DILEEYLPDL
MSSNNETLGS IYIHGINVET IINKDIIDVW ELFKHLDNFL YIIVLFSTYS TI