ATG7_KLUMD
ID ATG7_KLUMD Reviewed; 606 AA.
AC W0TA05;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000250|UniProtKB:P38862};
DE AltName: Full=ATG12-activating enzyme E1 ATG7 {ECO:0000250|UniProtKB:P38862};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000303|PubMed:26442587};
GN Name=ATG7 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_40433;
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).
RN [3]
RP MUTAGENESIS OF CYS-488, ACTIVE SITE, AND FUNCTION.
RX PubMed=22682742; DOI=10.1016/j.str.2012.04.018;
RA Yamaguchi M., Noda N.N., Yamamoto H., Shima T., Kumeta H., Kobashigawa Y.,
RA Akada R., Ohsumi Y., Inagaki F.;
RT "Structural insights into Atg10-mediated formation of the autophagy-
RT essential Atg12-Atg5 conjugate.";
RL Structure 20:1244-1254(2012).
CC -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and autophagy
CC (PubMed:26442587, PubMed:22682742). Activates ATG12 for its conjugation
CC with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine
CC (By similarity). Both systems are needed for the ATG8 association to
CC Cvt vesicles and autophagosomes membranes (By similarity). Autophagy is
CC essential for maintenance of amino acid levels and protein synthesis
CC under nitrogen starvation. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production (By
CC similarity). {ECO:0000250|UniProtKB:P38862,
CC ECO:0000269|PubMed:22682742, ECO:0000269|PubMed:26442587}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG8 through a
CC thioester bond between Cys-488 and the C-terminal Gly of ATG8 and with
CC ATG12 through a thioester bond between Cys-488 and the C-terminal Gly
CC of ATG12 (By similarity). Interacts also with ATG3 (By similarity).
CC {ECO:0000250|UniProtKB:P38862, ECO:0000269|PubMed:26442587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38862}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:P38862}.
CC -!- DOMAIN: The C-terminal residues 567 to 606 are required for
CC homodimerization, as well as the interactions with ATG3, ATG8 and
CC ATG12; and the C-terminal 17 residues are required for the ATG8
CC lipidation (By similarity). {ECO:0000250|UniProtKB:P38862}.
CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC through binding with ATP (By similarity).
CC {ECO:0000250|UniProtKB:P38862}.
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 ATG7 family. {ECO:0000305}.
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DR EMBL; AP012216; BAO40457.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TA05; -.
DR SMR; W0TA05; -.
DR EnsemblFungi; BAO40457; BAO40457; KLMA_40433.
DR OrthoDB; 549762at2759; -.
DR Proteomes; UP000065495; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IEA:EnsemblFungi.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0006501; P:C-terminal protein lipidation; 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:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IEA:EnsemblFungi.
DR Gene3D; 3.40.140.100; -; 1.
DR Gene3D; 3.40.140.70; -; 1.
DR InterPro; IPR006285; Atg7.
DR InterPro; IPR032197; Atg7_N.
DR InterPro; IPR042522; Atg7_N_1.
DR InterPro; IPR042523; Atg7_N_2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Transport.
FT CHAIN 1..606
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000443883"
FT REGION 567..606
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT MOTIF 316..321
FT /note="GXGXXG motif"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT ACT_SITE 488
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 488
FT /note="C->A: Impairs the formation of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
SQ SEQUENCE 606 AA; 68259 MW; 812BA25B338175A5 CRC64;
MVSDLKFAPS FQSFVDSSFF HELSRLKLDI FKLDSDEKAL YTQLDLNQFT SNVLAISLRD
DSFQKPDNDE HNIILKGYLL NFNTIELFKN CNKIQFIKEK GQELLQRGLE NDLNEIISFY
MISFADLKKY KFYYWICMPS FQSDGATYQI ISSKVIASDS DISVSFIKQN VIIACVISGV
IQKATPDNLK VCEKVVFKDF SHLKDIPSAV TKNILTVWSK LSPRETYTIC FLRSDESSFE
AEIIINNGNN PSLKVSGWEK NGLGKLAPKS IDLSSLMDPV KIADQAVDLN LKLMKWRIAP
KIDLDGIRNT KALLLGSGTL GCYVSRVLLA WGVRHISFVD NSTVSFSNPV RQSLYNFEDC
GKPKAQIASE ALKRIFPSVE SSGYQLEIPM IGHPVTNEKK QRQDYEALED LIKSHDVIFL
LMDARETRWL PSVLGRLHNK IVINAALGFD SYLVMRHGND DDKLGCYFCN DILAPSDSLT
DRTLDQMCTV TRPGVALLAA SQAVELLVTY LQPTPNVLGT SPHQIRGFLN EFKTVSQSTP
EYEHCCAGNK SVISALQENG WNFVRQALDD YKCVEKLSGL SKVQEEAELA LEEDFDFSED
DEFVTG
