ATG12_SCLS1
ID ATG12_SCLS1 Reviewed; 120 AA.
AC A7EAE5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Ubiquitin-like protein ATG12;
DE AltName: Full=Autophagy-related protein 12;
GN Name=atg12; ORFNames=SS1G_02277;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN99423.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476623; EDN99423.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001596061.1; XM_001596011.1.
DR AlphaFoldDB; A7EAE5; -.
DR SMR; A7EAE5; -.
DR STRING; 665079.A7EAE5; -.
DR GeneID; 5492567; -.
DR KEGG; ssl:SS1G_02277; -.
DR InParanoid; A7EAE5; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
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..120
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000317941"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-97 in ATG5)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 120 AA; 13250 MW; 9FC11894886D2778 CRC64;
MTSSLLLTNL PHDSSSALEH AFSFPTAKIT VRFQPIGSAP ILQRPVSKIS SSQQRFETVV
AYLRRVLKLD RKGGEGDSVF LYVNSCFAPA LDEVVGNLHR CFKDSKDQLI VTYSMTPAFG