ATG7_SORMK
ID ATG7_SORMK Reviewed; 699 AA.
AC F7W4M2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 48.
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:19351563};
GN Name=ATG7 {ECO:0000303|PubMed:19351563}; ORFNames=SMAC_06539;
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
RC {ECO:0000312|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000312|EMBL:CCC12459.1};
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19351563; DOI=10.1016/j.fgb.2009.03.008;
RA Nolting N., Bernhards Y., Poeggeler S.;
RT "SmATG7 is required for viability in the homothallic ascomycete Sordaria
RT macrospora.";
RL Fungal Genet. Biol. 46:531-542(2009).
RN [3]
RP INTERACTION WITH ATG12.
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: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and autophagy
CC (PubMed:19351563). Activates ATG12 for its conjugation with ATG5 and
CC ATG8 for its conjugation with phosphatidylethanolamine (By similarity).
CC Both systems are needed for the ATG8 association to Cvt vesicles and
CC autophagosomes membranes (By similarity). Autophagy is essential for
CC maintenance of amino acid levels and protein synthesis under nitrogen
CC starvation. Required for selective autophagic degradation of the
CC nucleus (nucleophagy) as well as for mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production (By similarity). Required for
CC normal mycelial growth and conidiogenesis (PubMed:19351563).
CC {ECO:0000250|UniProtKB:P38862, ECO:0000269|PubMed:19351563}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG8 through a
CC thioester bond between Cys-550 and the C-terminal Gly of ATG8 and with
CC ATG12 through a thioester bond between Cys-550 and the C-terminal Gly
CC of ATG12 (PubMed:27309377). Interacts also with ATG3 (By similarity).
CC {ECO:0000250|UniProtKB:P38862, ECO:0000269|PubMed:27309377}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38862}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:P38862}.
CC -!- INDUCTION: Up-regulated under amino acid starvation conditions and at
CC late stages during sexual development (PubMed:19351563).
CC {ECO:0000269|PubMed:19351563}.
CC -!- DOMAIN: The C-terminal residues 653 to 691 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: Leads to lethality (PubMed:19351563).
CC Heterokaryotic delta-ATG7/ATG7 strains and RNAi mutants produce
CC aberrant fruiting-bodies (PubMed:19351563).
CC {ECO:0000269|PubMed:19351563}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; CABT02000028; CCC12459.1; -; Genomic_DNA.
DR RefSeq; XP_003345985.1; XM_003345937.1.
DR AlphaFoldDB; F7W4M2; -.
DR SMR; F7W4M2; -.
DR STRING; 771870.F7W4M2; -.
DR EnsemblFungi; CCC12459; CCC12459; SMAC_06539.
DR GeneID; 10803355; -.
DR KEGG; smp:SMAC_06539; -.
DR VEuPathDB; FungiDB:SMAC_06539; -.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; F7W4M2; -.
DR OMA; VQTWRYS; -.
DR OrthoDB; 549762at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Reference proteome; Transport.
FT CHAIN 1..699
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000443884"
FT REGION 653..691
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT MOTIF 370..375
FT /note="GXGXXG motif"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT ACT_SITE 550
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:W0TA05"
SQ SEQUENCE 699 AA; 78377 MW; 091FDAD054D406F5 CRC64;
MDLKFATFSS EIELPFYSAL FSSKLDHDKL DSSARPVLGL YEPRSQANPE ASTRMQILGS
ALTSDQDESG PLGMTRAEGY IKNVNTIEEF KNTDKNAMIK KAGEQIWDAI QDGTIYSCPS
LLASFRILSY ADLKKYRFTY WFAFPALHSE PQWKRTEPIG RLNSDESTAL VERIGTWRYM
VDRREHGFFL AKKVRGEASG PRSSLDDPGV DIGYRWDIGS LRDFETGFFN DAAEEDRYVA
FVDPSNYPEY PSWPLRNLLI LVRQRYRLNK VQILCYRDTQ PRRHEARSII LPLAMDQVGD
VELKSMPKVT GWERNGNGDL RPRVANLAEY MDPTRLADQA VDLNLKLMKW RLAPNLDLDT
IKNTKCLLLG AGTLGSYVSR NLLGWGVRKI TFIDYGSVSF SNPVRQPLFK FEDCHNGGKP
KAIQAAEALR EIYPGVDVEG YALSVPMLDH PIHNEAKTKA EFDKLKELID SHDAIFLLMD
TRESRWLPTL MGKAANKIVM NAALGFDTYV VMRHGAKPLD DSEDTLGCYF CNDVVVAADS
MKDQTLDQQC TVTRPGVAAI ASALLVELLT SILQHPLKQH APAPISAGTG SAVSYERDPH
DHPLGLVPHQ VRGFLSNFQN MIIRGKSYPQ CSACSKPVLD AYREGGWDFV KTALASRDYV
AELSGLAEVQ RLAEKAAAEM QWSEDEEGMG EEEGEGELI
