ID   ATG12_MAGO7             Reviewed;         181 AA.
AC   Q51P78; A4REQ6; G4NB95;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; ORFNames=MGG_00598;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001235; EHA48856.1; -; Genomic_DNA.
DR   RefSeq; XP_003718440.1; XM_003718392.1.
DR   AlphaFoldDB; Q51P78; -.
DR   SMR; Q51P78; -.
DR   STRING; 318829.MGG_00598T0; -.
DR   EnsemblFungi; MGG_00598T0; MGG_00598T0; MGG_00598.
DR   GeneID; 2674234; -.
DR   KEGG; mgr:MGG_00598; -.
DR   VEuPathDB; FungiDB:MGG_00598; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   HOGENOM; CLU_106795_1_2_1; -.
DR   InParanoid; Q51P78; -.
DR   OMA; ADLPMNM; -.
DR   PHI-base; PHI:2079; -.
DR   Proteomes; UP000009058; Chromosome 5.
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;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..181
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000212481"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        181
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-162 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  19118 MW;  86A3BC56930DE80B CRC64;
     MSSPPTRYTR NPQLRRPSLS TPTPPPPSSS STAPASSSAT PIPDDAPDAD DNDGSPPSPD
     LPLTMSASVM LTQLPRDATA ALATAGEFPA DQKVVVRFKP VGGSAPALRK ELCKISAAQR
     FEAVVAYLRR TLKVGNGESV FLYINSTFAP ALDEIVGNLH RCFKDSNGQL NVSYSMTPAF
     G