ID   ATG12_YEAS7             Reviewed;         186 AA.
AC   A6ZLF7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; Synonyms=APG12; ORFNames=SCY_0427;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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       ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a conjugate with ATG5. Forms a thioester bond with the
CC       'Cys-133' of ATG10. Interacts with the ATG7 C-terminal 40 amino acids
CC       domain. The ATG12-ATG5 conjugate forms a complex with several units of
CC       ATG16. The ATG12-ATG5 conjugate associates also with ATG3. Interacts
CC       with COG2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Localizes to the isolation membrane (IM), a membrane sac which is
CC       generated from the pre-autophagosomal structure (PAS) (By similarity).
CC       Ultimately, the IM expands to become a mature autophagosome. Localizes
CC       also to a dot at the junction between the IM and the vacuolar membrane,
CC       termed the vacuole-IM contact site (VICS) (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Small amount of ATG5-ATG12 conjugate is enough to
CC       perform normal autophagy. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR   EMBL; AAFW02000011; EDN64826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZLF7; -.
DR   SMR; A6ZLF7; -.
DR   EnsemblFungi; EDN64826; EDN64826; SCY_0427.
DR   HOGENOM; CLU_106795_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
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; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..186
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317943"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        186
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-149 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  21106 MW;  74B3C9FD3CEA9265 CRC64;
     MSRILESENE TESDESSIIS TNNGTAMERS RNNQELRSSP HTVQNRLELF SRRLSQLGLA
     SDISVDQQVE DSSSGTYEQE ETIKTNAQTS KQKSHKDEKN IQKIQIKFQP IGSIGQLKPS
     VCKISMSQSF AMVILFLKRR LKMDHVYCYI NNSFAPSPQQ NIGELWMQFK TNDELIVSYC
     ASVAFG