ID   ATG12_LODEL             Reviewed;         210 AA.
AC   A5E1F1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; ORFNames=LELG_03438;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981527; EDK45259.1; -; Genomic_DNA.
DR   RefSeq; XP_001525510.1; XM_001525460.1.
DR   AlphaFoldDB; A5E1F1; -.
DR   SMR; A5E1F1; -.
DR   STRING; 379508.A5E1F1; -.
DR   PRIDE; A5E1F1; -.
DR   EnsemblFungi; EDK45259; EDK45259; LELG_03438.
DR   GeneID; 5232424; -.
DR   KEGG; lel:LELG_03438; -.
DR   VEuPathDB; FungiDB:LELG_03438; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   HOGENOM; CLU_106795_0_1_1; -.
DR   InParanoid; A5E1F1; -.
DR   OrthoDB; 1525971at2759; -.
DR   Proteomes; UP000001996; 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;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..210
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317934"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        210
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-160 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23631 MW;  51FDFF0E4F674E82 CRC64;
     MSQLQDSSIR QSDPDSDLDS DSNSNSDLGS LVDQGNAQFE DEYIATEEQT NLEPKVPLST
     SIVLDKLPQD QQSQLNHNPY LKSEQKSQSR EGTKFRMETV LPKKTTEKNE NQHSSASTTK
     SPEKVTIRFQ PIGSTTAIHP KVFKISSVQS ILTVNRFLSQ KLKNNERQPL HLYIQNSFLP
     SPDERVGDLY ALFATNHELI ISYCNTIAFG