ID A0A2I3ST48_PANTR Unreviewed; 704 AA.
AC A0A2I3ST48;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSPTRP00000079740.1,
GN ECO:0000313|VGNC:VGNC:11326};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000079740.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000079740.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000079740.1}
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 EMBL; AACZ04000084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04000085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3ST48; -.
DR Ensembl; ENSPTRT00000103862.1; ENSPTRP00000079740.1; ENSPTRG00000014625.6.
DR VGNC; VGNC:11326; ATG7.
DR GeneTree; ENSGT00390000017509; -.
DR InParanoid; A0A2I3ST48; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000014625; Expressed in bone marrow and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IBA:GO_Central.
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:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
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:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
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:UP000002277};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 13..323
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 339..599
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT COILED 444..471
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 572
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 704 AA; 77980 MW; 82863924489CD7DC CRC64;
MAAATGDPGL SKLQFAPFSS ALDVGFWHEL TQKKLNEYRL DEAPKDIKGY YYNGDSAGLP
ARLTLEFSAF DMSAPTPARC CPAIGTLYNT NTLESFKTAD KKLLLEQAAN EIWESIKSGA
ALENPVLLNK FLLLTFADLK KYHFYYWFCY PALCLPESLP LIQGPVGLDQ RFSLKQIEAL
ECAYDNLCQT EGVTALPYFL IKYDENTVLV SLLKHYSDFF QGQRTKITIG VYDPCNLAQY
PGWPLRNFLV LAAHRWSSSF QSVEVVCFRD RTMQGARDVA HSIIFEVKLP EMAFSPDCPK
AVGWEKNQKG GMGPRMVNLS ECMDPKRLAE SSVDLNLKLM CWRLVPTLDL DKVVSVKCLL
LGAGTLGCNV ARTLMGWGVR HITFVDNAKI SYSNPVRQPL YEFEDCLGGG KPKALAAADR
LQKIFPGVNA RGFSMSIPMP GHPVNFSSVT LEQARRDVEQ LEQLIESHDV VFLLMDTRES
RWLPAVIAAS KRKLVINAAL GFDTFVVMRH GLKKPKQQGA GDLCPNHLVA SADLLGSSLF
ANIPGYKLGC YFCNDVVAPG DSTRDRTLDQ QCTVSRPGLA MIAGALAVEL MVSVLQHPEG
GYAIASSSDD RMNEPPTSLG LVPHQIRGFL SRFDNVLPVS LAFDKCTACS SKVLDQYERE
GFNFLAKVFN SSHSFLEDLT GLTLLHQETQ AAEVRTKQAF CSED
//
