ATG12_KLUMD
ID ATG12_KLUMD Reviewed; 195 AA.
AC W0T4C1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Ubiquitin-like protein ATG12 {ECO:0000250|UniProtKB:P38316};
DE AltName: Full=Autophagy-related protein 12 {ECO:0000303|PubMed:26442587};
GN Name=ATG12 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_10251;
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA Limtong S., Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT structural and biochemical studies of autophagy.";
RL J. Biol. Chem. 290:29506-29518(2015).
CC -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC transport (Cvt), autophagy vesicles formation, mitophagy, and
CC nucleophagy (PubMed:26442587). Conjugation with ATG5 through a
CC ubiquitin-like conjugating system involving also ATG7 as an E1-like
CC activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC essential for its function (By similarity). The ATG12-ATG5 conjugate
CC acts as an E3-like enzyme which is required for lipidation of ATG8 and
CC ATG8 association to the vesicle membranes (By similarity). ATG12-ATG5
CC rearranges the ATG3 catalytic center and enhances its E2 activity (By
CC similarity). {ECO:0000250|UniProtKB:P38316,
CC ECO:0000269|PubMed:26442587}.
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 (By similarity). The ATG12-ATG5
CC conjugate forms a complex with several units of ATG16 (By similarity).
CC The ATG12-ATG5 conjugate associates also with ATG3 (By similarity).
CC {ECO:0000250|UniProtKB:P38316}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P38316}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P38316}. Note=Localizes to the isolation
CC membrane (IM), a membrane sac which is generated from the pre-
CC autophagosomal structure (PAS) (By similarity). Ultimately, the IM
CC expands to become a mature autophagosome (By similarity). Localizes
CC also to a dot at the junction between the IM and the vacuolar membrane,
CC termed the vacuole-IM contact site (VICS) (By similarity).
CC {ECO:0000250|UniProtKB:P38316}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of preautophagosomal
CC structures (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC and have a more ordered secondary structure than their S.cerevisiae
CC counterparts, which might contribute to the superior thermotolerance
CC and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC as a new model organism for further elucidation of the molecular
CC details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
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; AP012213; BAO37873.1; -; Genomic_DNA.
DR AlphaFoldDB; W0T4C1; -.
DR SMR; W0T4C1; -.
DR EnsemblFungi; BAO37873; BAO37873; KLMA_10251.
DR OrthoDB; 1525971at2759; -.
DR Proteomes; UP000065495; Chromosome 1.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019776; F:Atg8 ligase activity; IEA:EnsemblFungi.
DR GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblFungi.
DR GO; GO:0031386; F:protein tag; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IEA:EnsemblFungi.
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; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..195
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000443905"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-145 in ATG5)"
FT /evidence="ECO:0000250|UniProtKB:P38316"
SQ SEQUENCE 195 AA; 21388 MW; 7C839BAABDE082B7 CRC64;
MNSGVLLSES ETDTSETSER QSGLLSAQGS IKGKLEEFSA KLDRLRLDDE NSEEEHALKS
QSVSVNSEGN ISRSASASAS ASASASAKLR NSQSPVQEYT SDTNPETDAS FRVKIRLRPI
GSIPQIQPRV CQISSHQNFS ALVKFLCKRL KRNHVHCYIN NAFAPSLNQT IGDLWSQFKT
NDELIVSYCE TVAFG
