ID   ATG5_KLULA              Reviewed;         271 AA.
AC   Q6CKE2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Autophagy protein 5;
GN   Name=ATG5; OrderedLocusNames=KLLA0F11363g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382126; CAG98305.1; -; Genomic_DNA.
DR   RefSeq; XP_455597.1; XM_455597.1.
DR   AlphaFoldDB; Q6CKE2; -.
DR   SMR; Q6CKE2; -.
DR   STRING; 28985.XP_455597.1; -.
DR   EnsemblFungi; CAG98305; CAG98305; KLLA0_F11363g.
DR   GeneID; 2895087; -.
DR   KEGG; kla:KLLA0_F11363g; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   InParanoid; Q6CKE2; -.
DR   OMA; KWHYPLG; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IEA:EnsemblFungi.
DR   GO; GO:0005776; C:autophagosome; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR   GO; GO:0019776; F:Atg8 ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0140355; F:cargo receptor ligand activity; IEA:EnsemblFungi.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0061912; P:selective autophagy; IEA:EnsemblFungi.
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..271
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000219005"
FT   CROSSLNK        145
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  31408 MW;  42B2B777B63690B7 CRC64;
     MEELRERVWH GSLNVEIMLS DSIVVPNTPL SEKCYHIVVL RESFLALYLP AIVRKLGNNV
     IVTYENPYKQ WWFEYDGVPV PWEYPCGVLF DFLCNSSTTS TGKEDDQRLQ MWKLKLCHGN
     KYPPGILPLV DGLRQVKDHW KHQWKQACFI LNGSAKRIMS LSIPDFEAFW QSLISRHQPD
     YIKVREKLLT PNKTKHIPIR VWTADASFLQ PSIPANSDTM TLFDVMTSMD IKLQENNRAI
     IQGIVICSDE DIINLYDLFA SIDGFLYVVI K