ATG7_MOUSE
ID ATG7_MOUSE Reviewed; 698 AA.
AC Q9D906; Q3TCD9; Q8K4Q5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
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;
DE Short=mAGP7;
DE AltName: Full=Ubiquitin-activating enzyme E1-like protein;
GN Name=Atg7; Synonyms=Apg7l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE
RP CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, AND
RP MUTAGENESIS OF CYS-567.
RC TISSUE=Brain;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, Spleen, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP INTERACTION WITH ATG10 AND ATG12.
RX PubMed=12482611; DOI=10.1016/s0014-5793(02)03739-0;
RA Mizushima N., Yoshimori T., Ohsumi Y.;
RT "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-
RT mediated yeast two-hybrid method.";
RL FEBS Lett. 532:450-454(2002).
RN [5]
RP FUNCTION.
RX PubMed=15131264; DOI=10.1126/science.1096645;
RA Yu L., Alva A., Su H., Dutt P., Freundt E., Welsh S., Baehrecke E.H.,
RA Lenardo M.J.;
RT "Regulation of an ATG7-beclin 1 program of autophagic cell death by
RT caspase-8.";
RL Science 304:1500-1502(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15866887; DOI=10.1083/jcb.200412022;
RA Komatsu M., Waguri S., Ueno T., Iwata J., Murata S., Tanida I., Ezaki J.,
RA Mizushima N., Ohsumi Y., Uchiyama Y., Kominami E., Tanaka K., Chiba T.;
RT "Impairment of starvation-induced and constitutive autophagy in Atg7-
RT deficient mice.";
RL J. Cell Biol. 169:425-434(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH GABARAPL1.
RX PubMed=16704426; DOI=10.1111/j.1742-4658.2006.05260.x;
RA Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.;
RT "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation
RT mediated by human Atg4B, Atg7 and Atg3.";
RL FEBS J. 273:2553-2562(2006).
RN [8]
RP FUNCTION.
RX PubMed=17726112; DOI=10.1073/pnas.0701311104;
RA Komatsu M., Wang Q.J., Holstein G.R., Friedrich V.L. Jr., Iwata J.,
RA Kominami E., Chait B.T., Tanaka K., Yue Z.;
RT "Essential role for autophagy protein Atg7 in the maintenance of axonal
RT homeostasis and the prevention of axonal degeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14489-14494(2007).
RN [9]
RP FUNCTION.
RX PubMed=19417210; DOI=10.1182/blood-2008-04-151639;
RA Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M., Cleveland J.L.,
RA Ney P.A.;
RT "Mitochondrial clearance is regulated by Atg7-dependent and -independent
RT mechanisms during reticulocyte maturation.";
RL Blood 114:157-164(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [12]
RP FUNCTION.
RX PubMed=19855132; DOI=10.1172/jci39228;
RA Singh R., Xiang Y., Wang Y., Baikati K., Cuervo A.M., Luu Y.K., Tang Y.,
RA Pessin J.E., Schwartz G.J., Czaja M.J.;
RT "Autophagy regulates adipose mass and differentiation in mice.";
RL J. Clin. Invest. 119:3329-3339(2009).
RN [13]
RP FUNCTION.
RX PubMed=19910529; DOI=10.1073/pnas.0906048106;
RA Zhang Y., Goldman S., Baerga R., Zhao Y., Komatsu M., Jin S.;
RT "Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice
RT reveals a role in adipogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19860-19865(2009).
RN [14]
RP FUNCTION.
RX PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
RA Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
RA Debnath J.;
RT "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell
RT death.";
RL Cell 142:590-600(2010).
RN [15]
RP FUNCTION.
RX PubMed=21617129; DOI=10.1161/circresaha.110.237339;
RA Pattison J.S., Osinska H., Robbins J.;
RT "Atg7 induces basal autophagy and rescues autophagic deficiency in
RT CryABR120G cardiomyocytes.";
RL Circ. Res. 109:151-160(2011).
RN [16]
RP FUNCTION.
RX PubMed=21339326; DOI=10.1084/jem.20101145;
RA Mortensen M., Soilleux E.J., Djordjevic G., Tripp R., Lutteropp M.,
RA Sadighi-Akha E., Stranks A.J., Glanville J., Knight S., Jacobsen S.E.,
RA Kranc K.R., Simon A.K.;
RT "The autophagy protein Atg7 is essential for hematopoietic stem cell
RT maintenance.";
RL J. Exp. Med. 208:455-467(2011).
RN [17]
RP FUNCTION.
RX PubMed=22291845; DOI=10.1155/2012/278059;
RA Wittkopf N., Gunther C., Martini E., Waldner M., Amann K.U., Neurath M.F.,
RA Becker C.;
RT "Lack of intestinal epithelial atg7 affects paneth cell granule formation
RT but does not compromise immune homeostasis in the gut.";
RL Clin. Dev. Immunol. 2012:278059-278059(2012).
RN [18]
RP FUNCTION.
RX PubMed=22499945; DOI=10.1126/science.1218395;
RA Lee I.H., Kawai Y., Fergusson M.M., Rovira I.I., Bishop A.J., Motoyama N.,
RA Cao L., Finkel T.;
RT "Atg7 modulates p53 activity to regulate cell cycle and survival during
RT metabolic stress.";
RL Science 336:225-228(2012).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29937374; DOI=10.1016/j.cmet.2018.05.023;
RA Toledo M., Batista-Gonzalez A., Merheb E., Aoun M.L., Tarabra E., Feng D.,
RA Sarparanta J., Merlo P., Botre F., Schwartz G.J., Pessin J.E., Singh R.;
RT "Autophagy regulates the liver clock and glucose metabolism by degrading
RT CRY1.";
RL Cell Metab. 28:268-281(2018).
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. Facilitates
CC LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is
CC found on autophagosomal membranes (By similarity). 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. Also plays a key role in the maintenance of axonal
CC homeostasis, the prevention of axonal degeneration, the maintenance of
CC hematopoietic stem cells, the formation of Paneth cell granules, as
CC well as in adipose differentiation. 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
CC (PubMed:29937374). {ECO:0000250|UniProtKB:O95352,
CC ECO:0000269|PubMed:11890701, ECO:0000269|PubMed:15131264,
CC ECO:0000269|PubMed:15866887, ECO:0000269|PubMed:16704426,
CC ECO:0000269|PubMed:17726112, ECO:0000269|PubMed:19417210,
CC ECO:0000269|PubMed:19855132, ECO:0000269|PubMed:19910529,
CC ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:21339326,
CC ECO:0000269|PubMed:21617129, ECO:0000269|PubMed:22291845,
CC ECO:0000269|PubMed:22499945, ECO:0000269|PubMed:29937374}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG3, FOXO1 and EP300
CC acetyltransferase. The complex, composed of ATG3 and ATG7, plays a role
CC in the conjugation of ATG12 to ATG5. Interacts with FOXO1 (By
CC similarity). Forms intermediate conjugates with ATG8 family proteins
CC such as GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, or GABARAPL1.
CC Interacts with ATG12. {ECO:0000250, ECO:0000269|PubMed:11890701,
CC ECO:0000269|PubMed:12482611, ECO:0000269|PubMed:16704426}.
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:0000269|PubMed:24089209}.
CC -!- TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver,
CC lymph nodes and bone marrow. {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 -!- DISRUPTION PHENOTYPE: Leads to hepatomegaly in liver and accumulation
CC of abnormal organelles in hepatic cells (PubMed:15866887). Liver-
CC specific knockout leads to loss of autophagy, increased accumulation of
CC CRY1, decreased blood glucose levels due to impaired gluconeogenesis
CC and the disruption of the circadian clock in the liver
CC (PubMed:29937374). {ECO:0000269|PubMed:15866887,
CC ECO:0000269|PubMed:29937374}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; AB079385; BAC10416.1; -; mRNA.
DR EMBL; AK007484; BAB25060.1; -; mRNA.
DR EMBL; AK035604; BAC29122.1; -; mRNA.
DR EMBL; AK161133; BAE36208.1; -; mRNA.
DR EMBL; AK170769; BAE42018.1; -; mRNA.
DR EMBL; AK172272; BAE42917.1; -; mRNA.
DR EMBL; BC058597; AAH58597.1; -; mRNA.
DR CCDS; CCDS39598.1; -.
DR RefSeq; NP_001240646.1; NM_001253717.1.
DR RefSeq; NP_001240647.1; NM_001253718.1.
DR RefSeq; NP_083111.1; NM_028835.4.
DR RefSeq; XP_006506772.1; XM_006506709.2.
DR RefSeq; XP_006506773.1; XM_006506710.3.
DR RefSeq; XP_011239796.1; XM_011241494.2.
DR RefSeq; XP_011239797.1; XM_011241495.2.
DR AlphaFoldDB; Q9D906; -.
DR SMR; Q9D906; -.
DR BioGRID; 216602; 36.
DR IntAct; Q9D906; 2.
DR MINT; Q9D906; -.
DR STRING; 10090.ENSMUSP00000032457; -.
DR GlyConnect; 2807; 2 N-Linked glycans (1 site).
DR GlyGen; Q9D906; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9D906; -.
DR PhosphoSitePlus; Q9D906; -.
DR SwissPalm; Q9D906; -.
DR EPD; Q9D906; -.
DR jPOST; Q9D906; -.
DR MaxQB; Q9D906; -.
DR PaxDb; Q9D906; -.
DR PRIDE; Q9D906; -.
DR ProteomicsDB; 277127; -.
DR Antibodypedia; 1972; 855 antibodies from 45 providers.
DR DNASU; 74244; -.
DR Ensembl; ENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314.
DR Ensembl; ENSMUST00000182793; ENSMUSP00000138137; ENSMUSG00000030314.
DR Ensembl; ENSMUST00000182902; ENSMUSP00000138651; ENSMUSG00000030314.
DR GeneID; 74244; -.
DR KEGG; mmu:74244; -.
DR UCSC; uc009dhz.2; mouse.
DR CTD; 10533; -.
DR MGI; MGI:1921494; Atg7.
DR VEuPathDB; HostDB:ENSMUSG00000030314; -.
DR eggNOG; KOG2337; Eukaryota.
DR GeneTree; ENSGT00390000017509; -.
DR InParanoid; Q9D906; -.
DR OMA; VQTWRYS; -.
DR OrthoDB; 549762at2759; -.
DR PhylomeDB; Q9D906; -.
DR TreeFam; TF105689; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 74244; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Atg7; mouse.
DR PRO; PR:Q9D906; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D906; protein.
DR Bgee; ENSMUSG00000030314; Expressed in lumbar dorsal root ganglion and 249 other tissues.
DR ExpressionAtlas; Q9D906; baseline and differential.
DR Genevisible; Q9D906; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IDA:MGI.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISS:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IMP:MGI.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0061684; P:chaperone-mediated autophagy; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IMP:MGI.
DR GO; GO:0090298; P:negative regulation of mitochondrial DNA replication; ISO:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IMP:MGI.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IMP:MGI.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IMP:MGI.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0006996; P:organelle organization; IMP:MGI.
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; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031401; P:positive regulation of protein modification process; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006497; P:protein lipidation; ISO:MGI.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IMP:MGI.
DR GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
DR GO; GO:0060284; P:regulation of cell development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:1903706; P:regulation of hemopoiesis; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IMP:MGI.
DR GO; GO:0042594; P:response to starvation; IMP:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:MGI.
DR GO; GO:0039521; P:suppression by virus of host autophagy; ISO:MGI.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:MGI.
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 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_0000212807"
FT MOTIF 11..13
FT /note="FAP motif"
FT ACT_SITE 567
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95352"
FT MUTAGEN 567
FT /note="C->S: Instead of the formation of an intermediate
FT complex with a thiol ester bond between ATG7 (E1-like
FT enzyme) and GABARAPL1 (MAP1LC3, GABARAP or GABARAPL;
FT substrates), a stable complex with an O-ester bond is
FT formed."
FT /evidence="ECO:0000269|PubMed:11890701"
FT CONFLICT 22
FT /note="F -> L (in Ref. 1; BAC10416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 77520 MW; 79D94EA7464C6ADB CRC64;
MGDPGLAKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG DSAGLPTRLT
LEFSAFDMSA STPAHCCPAM GTLHNTNTLE AFKTADKKLL LEQSANEIWE AIKSGAALEN
PMLLNKFLLL TFADLKKYHF YYWFCCPALC LPESIPLIRG PVSLDQRLSP KQIQALEHAY
DDLCRAEGVT ALPYFLFKYD DDTVLVSLLK HYSDFFQGQR TKITVGVYDP CNLAQYPGWP
LRNFLVLAAH RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW
EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV SVKCLLLGAG
TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE DCLGGGKPKA LAAAERLQKI
FPGVNARGFN MSIPMPGHPV NFSDVTMEQA RRDVEQLEQL IDNHDVIFLL MDTRESRWLP
TVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG
YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA
SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSPKVLD QYEREGFTFL
AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV
