ID   ATG12_YARLI             Reviewed;         205 AA.
AC   Q6BZZ1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; OrderedLocusNames=YALI0F29689g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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: Ubiquitin-like protein involved in cytoplasm to vacuole
CC       transport (Cvt), autophagy vesicles formation, mitophagy, and
CC       nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating
CC       system involving also ATG7 as an E1-like activating enzyme and ATG10 as
CC       an E2-like conjugating enzyme, is essential for its function. The
CC       ATG12-ATG5 conjugate functions as an E3-like enzyme which is required
CC       for lipidation of ATG8 and ATG8 association to the vesicle membranes
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a conjugate with ATG5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR   EMBL; CR382132; CAG78834.1; -; Genomic_DNA.
DR   RefSeq; XP_506021.1; XM_506021.1.
DR   AlphaFoldDB; Q6BZZ1; -.
DR   SMR; Q6BZZ1; -.
DR   STRING; 4952.CAG78834; -.
DR   EnsemblFungi; CAG78834; CAG78834; YALI0_F29689g.
DR   GeneID; 2908558; -.
DR   KEGG; yli:YALI0F29689g; -.
DR   VEuPathDB; FungiDB:YALI0_F29689g; -.
DR   HOGENOM; CLU_106795_1_2_1; -.
DR   InParanoid; Q6BZZ1; -.
DR   OMA; ELATAHM; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
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: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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007242; Atg12.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13385; PTHR13385; 1.
DR   Pfam; PF04110; APG12; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..205
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000212484"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        205
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-112 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   205 AA;  22073 MW;  7D0D2A1370286B02 CRC64;
     MIESDSDTSD DAPQEYVSAS ANIPAQFELA TAHMKATPEP QPTQQPDAEA LHDDDPLTTT
     QDHPTGPSAT ASDTIDSTPQ PMAPATLSAS AVLPSLPSDT AALLETFSQQ LQQSNVKCQL
     KFRPIGGATP SLKQSVYKIA ETQQFGVVVK FLRKQLKIKN SQSSQIFCYI SSFAPGLDET
     VGSLYNRYAI RGELTISYCL NQAFG