ATG7_RAT
ID ATG7_RAT Reviewed; 698 AA.
AC Q641Y5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE AltName: Full=ATG12-activating enzyme E1 ATG7;
DE AltName: Full=Autophagy-related protein 7;
DE Short=APG7-like;
GN Name=Atg7; Synonyms=Apg7l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11890701; DOI=10.1006/bbrc.2002.6645;
RA Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H.,
RA Ueno T., Kominami E.;
RT "Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p
RT homologs.";
RL Biochem. Biophys. Res. Commun. 292:256-262(2002).
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. Facilitates LC3-I
CC lipidation with phosphatidylethanolamine to form LC3-II which is found
CC on autophagosomal membranes (By similarity). Required for mitophagy
CC which 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. Modulates
CC p53/TP53 activity to regulate cell cycle and survival during metabolic
CC stress. Also plays a key role in the maintenance of axonal homeostasis,
CC the prevention of axonal degeneration, the maintenance of hematopoietic
CC stem cells, the formation of Paneth cell granules, as well as in
CC adipose differentiation (By similarity). Plays a role in regulating the
CC liver clock and glucose metabolism by mediating the autophagic
CC degradation of CRY1 (clock repressor) in a time-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:O95352,
CC ECO:0000250|UniProtKB:Q9D906}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG3 and ATG12. The complex,
CC composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to
CC ATG5. Forms intermediate conjugates with ATG8 family proteins such as
CC GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, or GABARAPL1. Interacts with
CC EP300 acetyltransferase and FOXO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {ECO:0000250}. Note=Localizes also to discrete punctae along
CC the ciliary axoneme and to the base of the ciliary axoneme.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11890701}.
CC -!- DOMAIN: The C-terminal part of the protein is essential for the
CC dimerization and interaction with ATG3 and ATG12. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal FAP motif (residues 11 to 13) is essential for
CC the formation of the ATG89-PE and ATG5-ATG12 conjugates. {ECO:0000250}.
CC -!- PTM: Acetylated by EP300. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; BC082059; AAH82059.1; -; mRNA.
DR RefSeq; NP_001012097.1; NM_001012097.1.
DR RefSeq; XP_006237095.1; XM_006237033.3.
DR AlphaFoldDB; Q641Y5; -.
DR SMR; Q641Y5; -.
DR STRING; 10116.ENSRNOP00000063617; -.
DR jPOST; Q641Y5; -.
DR PaxDb; Q641Y5; -.
DR PRIDE; Q641Y5; -.
DR GeneID; 312647; -.
DR KEGG; rno:312647; -.
DR UCSC; RGD:1304817; rat.
DR CTD; 10533; -.
DR RGD; 1304817; Atg7.
DR VEuPathDB; HostDB:ENSRNOG00000007486; -.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_1_0_1; -.
DR InParanoid; Q641Y5; -.
DR OMA; VQTWRYS; -.
DR OrthoDB; 549762at2759; -.
DR PhylomeDB; Q641Y5; -.
DR TreeFam; TF105689; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q641Y5; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007486; Expressed in testis and 18 other tissues.
DR Genevisible; Q641Y5; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; ISS:UniProtKB.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0080144; P:amino acid homeostasis; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISS:UniProtKB.
DR GO; GO:0071315; P:cellular response to morphine; IEP:RGD.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; ISO:RGD.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR GO; GO:0061024; P:membrane organization; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; ISO:RGD.
DR GO; GO:0090298; P:negative regulation of mitochondrial DNA replication; IMP:RGD.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:RGD.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISO:RGD.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; ISO:RGD.
DR GO; GO:0039689; P:negative stranded viral RNA replication; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0006996; P:organelle organization; ISO:RGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0070257; P:positive regulation of mucus secretion; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031401; P:positive regulation of protein modification process; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; ISO:RGD.
DR GO; GO:0006497; P:protein lipidation; ISO:RGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:0060284; P:regulation of cell development; ISO:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:1903706; P:regulation of hemopoiesis; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; IMP:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:1902617; P:response to fluoride; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; ISO:RGD.
DR GO; GO:0048511; P:rhythmic process; 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 2: Evidence at transcript level;
KW Acetylation; Autophagy; Biological rhythms; Cytoplasm; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..698
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212808"
FT MOTIF 11..13
FT /note="FAP motif"
FT ACT_SITE 567
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95352"
SQ SEQUENCE 698 AA; 77436 MW; B26001CB18054498 CRC64;
MGDPGLSKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG DSAGLPTRLT
LEFSAFDMSA PTPARCCPAM GTLHNTNTLE AFKTADKKLL LEQSANEIWE AIKSGAALEN
PMLLNKFLLL TFADLKKYHF YYWFCCPALC LPESIPLIRG PVGLDQRLSP KQIQALEHAY
DDLCRTEGVT ALPYFLFKYD DDTVLVSLLK HYSDFFQGQR TKLTVGVYDP CNLTQHPGWP
LRNFLVLAAH RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW
EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV SVKCLLLGAG
TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE DCLGGGKPKA LAAAERLQKI
FPGVNASGFN MSIPMPGHPV NFSDVTMEQA RRDVEQLEEL IDSHDVIFLL MDTRESRWLP
TVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG
YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA
SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSSKVLD QYEQEGFTFL
AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV
