ID B3DL97_XENTR Unreviewed; 705 AA.
AC B3DL97;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
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|EMBL:AAI67363.1,
GN ECO:0000313|RefSeq:NP_001123394.1,
GN ECO:0000313|Xenbase:XB-GENE-940571};
GN Synonyms=apg7-like {ECO:0000313|RefSeq:NP_001123394.1}, apg7l
GN {ECO:0000313|RefSeq:NP_001123394.1}, gsa7
GN {ECO:0000313|RefSeq:NP_001123394.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI67363.1};
RN [1] {ECO:0000313|RefSeq:NP_001123394.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI67363.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole embryo {ECO:0000313|EMBL:AAI67363.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001123394.1}
RP IDENTIFICATION.
RG RefSeq;
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; BC167363; AAI67363.1; -; mRNA.
DR RefSeq; NP_001123394.1; NM_001129922.1.
DR GeneID; 100170158; -.
DR KEGG; xtr:100170158; -.
DR AGR; Xenbase:XB-GENE-940571; -.
DR CTD; 10533; -.
DR Xenbase; XB-GENE-940571; atg7.
DR OMA; RQIWDAI; -.
DR OrthoDB; 1128973at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
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-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 2: Evidence at transcript level;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU366022};
KW Cytoplasm {ECO:0000256|RuleBase:RU366022};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU366022};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 19..327
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 344..601
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT ACT_SITE 574
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 705 AA; 78341 MW; F914DC213A798840 CRC64;
MASGTDPPSD LLAADDAKLQ FVPFTSALDA GFWHQLTQKK LNEYRLDETP KEIKGHYYNG
DPAGLPTRLT LEFSAFDVNT PTPARCCPAL GSLYNTNTLE SFKSCDKKAL LDRAANEIWE
AIQSGAAIED PTHLTKFHLL TFSDLKKYRF YYWFCFPALC LQEGVRLLQP PASLAQRFSE
LQVGALQRSY DELWQKEGTP PPYFLVKYTE TSCAVAPLRA FPDFYKDGDK VTLGFCDPCT
LPQYPGWPLR NLLVLAAYHW GSRVREAEVL CFRDRTLQGE RDVTHSLIFH IQLPEMPANQ
ELPKAVGWEK NQKGQMGPRM VNLSECMDPK RLAESSVDLN LKLMRWRLVP TLDLDKVIHT
KCLLLGAGTL GCNVARALMG WGVRHITFVD NAKISYSNPV RQPLYDFSDC LGGGNPKAEV
AAAKLEKIFP GVNARGFNLS IPMPGHPVHF SQETVQAQRD VEKLEALIGQ HDVVFLLMDT
RESRWLPTVI AASQQKLVIN AALGFDTFVV MRHGLKMPRK AGAAESWADG ANSSDLLGSS
LFSNIPGHRL GCYFCNDVVA PGDSTRDRTL DQQCTVSRPG LAMIAGALAV ELMVSVIQHP
EGGYAVASSS DDRMNEPPTS LGLVPHQIRG FLSRFDNVLP VSLAFDKCTA CSPKVLDQYE
RDGFQFLAKA FNSSHSFLED LTGLTLLHQE TQAAEIWDMS DDEIV
//
