ID   ATG12_PENRW             Reviewed;         172 AA.
AC   A7KAM3; B6GXN4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=atg12; ORFNames=Pc12g08030;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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, ECO:0000269|PubMed:17204848}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF107745; ABO31083.1; -; Genomic_DNA.
DR   EMBL; AM920427; CAP80430.1; -; Genomic_DNA.
DR   RefSeq; XP_002557636.1; XM_002557590.1.
DR   AlphaFoldDB; A7KAM3; -.
DR   SMR; A7KAM3; -.
DR   STRING; 1108849.XP_002557636.1; -.
DR   EnsemblFungi; CAP80430; CAP80430; PCH_Pc12g08030.
DR   GeneID; 8309062; -.
DR   KEGG; pcs:Pc12g08030; -.
DR   VEuPathDB; FungiDB:PCH_Pc12g08030; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   HOGENOM; CLU_106795_1_2_1; -.
DR   OMA; ADLPMNM; -.
DR   OrthoDB; 1525971at2759; -.
DR   BioCyc; PCHR:PC12G08030-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c12.
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..172
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317936"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-153 in atg5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  18695 MW;  1D274AC784F192A9 CRC64;
     MNTSSPTRSP QSSPSPNPQS TLSHRPSPRQ PQSSDTPPNS SANAPIPDDE HGADLPMNMT
     ASVMLTNLPR DAHQALADVE SIDSGKVTVR FQPLPSAPIL KNRVFKVSAS QKFETVVKFL
     RKKLDCKDTD SVFCYVNSVF APGLDEGMGG LWRCFKTDDQ LIVAYSMTPA FG