ID G3X2I8_SARHA Unreviewed; 708 AA.
AC G3X2I8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000256|ARBA:ARBA00017647, ECO:0000256|RuleBase:RU366022};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000256|RuleBase:RU366022};
GN Name=ATG7 {ECO:0000313|Ensembl:ENSSHAP00000021893.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000021893.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000021893.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000021893.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and
CC autophagy. Activates ATG12 for its conjugation with ATG5 as well as the
CC ATG8 family proteins for their conjugation with
CC phosphatidylethanolamine. Both systems are needed for the ATG8
CC association to Cvt vesicles and autophagosomes membranes. Required for
CC autophagic death induced by caspase-8 inhibition. Required for
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production.
CC Modulates p53/TP53 activity to regulate cell cycle and survival during
CC metabolic stress. {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366022}.
CC Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000256|ARBA:ARBA00010931,
CC ECO:0000256|RuleBase:RU366022}.
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DR RefSeq; XP_012399054.1; XM_012543600.1.
DR AlphaFoldDB; G3X2I8; -.
DR STRING; 9305.ENSSHAP00000021893; -.
DR Ensembl; ENSSHAT00000022068.2; ENSSHAP00000021893.1; ENSSHAG00000022602.1.
DR GeneID; 100933380; -.
DR KEGG; shr:100933380; -.
DR CTD; 10533; -.
DR eggNOG; KOG2337; Eukaryota.
DR GeneTree; ENSGT00390000017509; -.
DR HOGENOM; CLU_012998_1_0_1; -.
DR InParanoid; G3X2I8; -.
DR OMA; RQIWDAI; -.
DR OrthoDB; 1128973at2759; -.
DR TreeFam; TF105689; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0031401; P:positive regulation of protein modification process; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR CDD; cd01486; Apg7; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 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 NCBIfam; TIGR01381; E1_like_apg7; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU366022};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU366022};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU366022};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 19..329
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 345..604
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..477
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 577
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 708 AA; 78780 MW; A7F17924E5B7E804 CRC64;
MATATGEICR SLGSGLSKLQ FAPFSSALDA GFWHELTQKK LNEYRLDEAP KDIKGYYYNG
DSAGLPARLT LEFSAFDINA PTPAHCCPAI GTLFNTNTLE SFKTSDKKLL LEKAAQEIWE
SIKSGAALEN PVLLNKFLLL TFSDLKKYYF YYWFCYPALC LPEGIPLLQE PIRLDQKFSP
SQIQALECAY DNLCQAEGVT ALPYFLIKYD VNSVLISLLK DYNDFFQDQR KKITIGVYDP
CNLGQYPGWP LRNLLVLAAY RWSDRFQSVE VLCFRDRTLQ GMRDITHSII FEIQLPELAY
NSDCPKAVGW EKNQKGGMGP RMVNLSECMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV
SVKCLLLGAG TLGCNVARTL MGWGVRHITF VDNAKISYSN PVRQPLYEFE DCLGGGKAKA
LAAAERLQKI FPGVNAAGFN MSIPMPGHPV NFSNVTMEQA QKDVEQLERL IEDHDVIFLL
MDTRESRWLP AVIAASKRKL VINAALGFDT FVVMRHGLKQ PKHQGAGDPH PSHATAPSDL
GSSLFSNIPG YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAMIAGS LAVELMVSVL
QHPEGGYAVA SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDH VLPVSLAFDK CTACSTKVLD
QYEKEGFNFL AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDDDTI
//
