ATG12_SORMK
ID ATG12_SORMK Reviewed; 159 AA.
AC F7W503;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Ubiquitin-like protein ATG12 {ECO:0000250|UniProtKB:P38316};
DE AltName: Full=Autophagy-related protein 12 {ECO:0000303|PubMed:27309377};
GN Name=ATG12 {ECO:0000303|PubMed:27309377}; ORFNames=SMAC_06998;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ATG3 AND ATG7.
RX PubMed=27309377; DOI=10.1371/journal.pone.0157960;
RA Werner A., Herzog B., Frey S., Poeggeler S.;
RT "Autophagy-Associated Protein SmATG12 Is Required for Fruiting-Body
RT Formation in the Filamentous Ascomycete Sordaria macrospora.";
RL PLoS ONE 11:E0157960-E0157960(2016).
CC -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC transport (Cvt), autophagy vesicles formation, mitophagy, and
CC nucleophagy (By similarity). Conjugation with ATG5 through a ubiquitin-
CC like conjugating system involving also ATG7 as an E1-like activating
CC enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its
CC function (By similarity). The ATG12-ATG5 conjugate acts as an E3-like
CC enzyme which is required for lipidation of ATG8 and ATG8 association to
CC the vesicle membranes (PubMed:27309377). ATG12-ATG5 rearranges the ATG3
CC catalytic center and enhances its E2 activity (By similarity). plays a
CC role in sexual development and perithecia formation (PubMed:27309377).
CC {ECO:0000250|UniProtKB:P38316, ECO:0000269|PubMed:27309377}.
CC -!- SUBUNIT: Forms a conjugate with ATG5 (By similarity). Forms a thioester
CC bond with the 'Cys-116' of ATG10 (By similarity). Interacts with the
CC ATG7 C-terminal 40 amino acids domain (PubMed:27309377). The ATG12-ATG5
CC conjugate forms a complex with several units of ATG16 (By similarity).
CC The ATG12-ATG5 conjugate associates also with ATG3 (PubMed:27309377).
CC {ECO:0000250|UniProtKB:P38316, ECO:0000269|PubMed:27309377}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:27309377}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P38316}. Cytoplasm
CC {ECO:0000269|PubMed:27309377}. Note=Localizes to the isolation membrane
CC (IM), a membrane sac which is generated from the pre-autophagosomal
CC structure (PAS) (By similarity). Ultimately, the IM expands to become a
CC mature autophagosome (By similarity). Localizes also to a dot at the
CC junction between the IM and the vacuolar membrane, termed the vacuole-
CC IM contact site (VICS) (By similarity). {ECO:0000250|UniProtKB:P38316}.
CC -!- DISRUPTION PHENOTYPE: Displays slower vegetative growth under nutrient
CC starvation conditions and leads to the inability to form fruiting
CC bodies (PubMed:27309377). {ECO:0000269|PubMed:27309377}.
CC -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCC12591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305|PubMed:27309377};
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DR EMBL; CABT02000029; CCC12591.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; F7W503; -.
DR SMR; F7W503; -.
DR STRING; 771870.F7W503; -.
DR EnsemblFungi; CCC12591; CCC12591; SMAC_06998.
DR eggNOG; KOG3439; Eukaryota.
DR HOGENOM; CLU_106795_1_1_1; -.
DR InParanoid; F7W503; -.
DR OrthoDB; 1525971at2759; -.
DR Proteomes; UP000001881; 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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Isopeptide bond; Membrane; Protein transport;
KW Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..159
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000443906"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-218 in ATG5)"
FT /evidence="ECO:0000250|UniProtKB:P38316"
SQ SEQUENCE 159 AA; 17139 MW; EC4F59C43028C734 CRC64;
MASPQPPFGG GSNSNSNTAS PSNNLSPTAS PLLEGRDSPN LPLTMTASTV LMTLPRDATA
ALAEAGKFGQ EKVVIRFKPV GSAPALRREQ VKVSSTERFD TVMTYIRKTL KCRESDSVFL
YVNSVFAPAL DEVVGNLWRC FKDSTNQLNV SYSMTPSFG
