ID   ATG12_PICST             Reviewed;         247 AA.
AC   A3GI31;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 3.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=ATG12; ORFNames=PICST_29200;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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 association to the vesicle membranes (By
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAZ63162.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAZ63162.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AAVQ01000002; EAZ63162.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001387185.2; XM_001387148.1.
DR   AlphaFoldDB; A3GI31; -.
DR   SMR; A3GI31; -.
DR   STRING; 4924.XP_001387185.2; -.
DR   EnsemblFungi; EAZ63162; EAZ63162; PICST_29200.
DR   GeneID; 4851930; -.
DR   KEGG; pic:PICST_29200; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   HOGENOM; CLU_883121_0_0_1; -.
DR   InParanoid; A3GI31; -.
DR   OrthoDB; 1525971at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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..247
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317940"
FT   REGION          1..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        247
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-144 in ATG5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   247 AA;  26831 MW;  431D726F050BFEA5 CRC64;
     MFLSERVKEP SRIPLSNESE EAVGGSAENA NTVDDEDAKT EVSNDRIDNE NNTATASSGA
     VHNEYTSIDA EGPEKEPLAT HGLSMELISD ISTSKEVQKH LEKTEPETTS TSKYSIQSDT
     SSKSDSSPNS GTAPKRASSL KPGLDSDSTL KADSSPKSAS EAKTTIRFVP IGSTPRINPL
     VFTISSNQTV SILIKFLAKK LKTKDHVYLY IQNSFQPTPD EKLSDLYNLF RTNNELIVSY
     CESVAFG