ID   ATG12_AJECN             Reviewed;         179 AA.
AC   A6RA46;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; ORFNames=HCAG_05834;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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; CH476661; EDN10031.1; -; Genomic_DNA.
DR   RefSeq; XP_001538229.1; XM_001538179.1.
DR   AlphaFoldDB; A6RA46; -.
DR   SMR; A6RA46; -.
DR   STRING; 339724.A6RA46; -.
DR   EnsemblFungi; EDN10031; EDN10031; HCAG_05834.
DR   GeneID; 5444476; -.
DR   KEGG; aje:HCAG_05834; -.
DR   VEuPathDB; FungiDB:HCAG_05834; -.
DR   HOGENOM; CLU_106795_1_2_1; -.
DR   OMA; ADLPMNM; -.
DR   OrthoDB; 1525971at2759; -.
DR   Proteomes; UP000009297; 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..179
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317928"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        179
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-172 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   179 AA;  19112 MW;  A37E6D3691BE062A CRC64;
     MASTPPLSAS PNSSKPTSPR ASNRGLGLTS RQGSRSSRPS NDNGSRGVAT TPIPDEDHSA
     DLPLTMSASI VLTGLPKDAH QALADVEAID SGKVTVRFQP LPSAPILRNR VFKISASQKF
     ETVVKFLRKK LDCKDTDSVF CYVNSVFAPG LDEGVGGLWR CFKTDDQLIV AYSMTPAFG