ATG7_YEAST
ID ATG7_YEAST Reviewed; 630 AA.
AC P38862; D3DLC0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
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 AltName: Full=Cytoplasm to vacuole targeting protein 2;
GN Name=ATG7; Synonyms=APG7, CVT2; OrderedLocusNames=YHR171W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=9759731; DOI=10.1038/26506;
RA Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D.,
RA Klionsky D.J., Ohsumi M., Ohsumi Y.;
RT "A protein conjugation system essential for autophagy.";
RL Nature 395:395-398(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e;
RA Tsukada M., Ohsumi Y.;
RT "Isolation and characterization of autophagy-defective mutants of
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 333:169-174(1993).
RN [5]
RP FUNCTION.
RX PubMed=7593182; DOI=10.1083/jcb.131.3.591;
RA Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.;
RT "Isolation and characterization of yeast mutants in the cytoplasm to
RT vacuole protein targeting pathway.";
RL J. Cell Biol. 131:591-602(1995).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10233148; DOI=10.1091/mbc.10.5.1337;
RA Kim J., Dalton V.M., Eggerton K.P., Scott S.V., Klionsky D.J.;
RT "Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting,
RT macroautophagy, and peroxisome degradation pathways.";
RL Mol. Biol. Cell 10:1337-1351(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG12, AND MUTAGENESIS OF
RP GLY-333 AND CYS-507.
RX PubMed=10233150; DOI=10.1091/mbc.10.5.1367;
RA Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y.,
RA Kominami E.;
RT "Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy.";
RL Mol. Biol. Cell 10:1367-1379(1999).
RN [8]
RP FUNCTION, INTERACTION WITH ATG8, AND MUTAGENESIS OF GLY-333 AND CYS-507.
RX PubMed=11100732; DOI=10.1038/35044114;
RA Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N.,
RA Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.;
RT "A ubiquitin-like system mediates protein lipidation.";
RL Nature 408:488-492(2000).
RN [9]
RP HOMODIMERIZATION, AND INTERACTION WITH ATG3; ATG8 AND ATG12.
RX PubMed=11139573; DOI=10.1074/jbc.m007737200;
RA Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.;
RT "The C-terminal region of an Apg7p/Cvt2p is required for homodimerization
RT and is essential for its E1 activity and E1-E2 complex formation.";
RL J. Biol. Chem. 276:9846-9854(2001).
RN [10]
RP FUNCTION.
RX PubMed=11149920; DOI=10.1083/jcb.152.1.51;
RA Kim J., Huang W.-P., Klionsky D.J.;
RT "Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole
RT targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation
RT complex.";
RL J. Cell Biol. 152:51-64(2001).
RN [11]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
RN [12]
RP FUNCTION.
RX PubMed=12965207; DOI=10.1016/s0014-5793(03)00899-8;
RA Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.;
RT "The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8
RT lipidation, but not for Apg12 conjugation.";
RL FEBS Lett. 551:71-77(2003).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF CYS-507.
RX PubMed=15277523; DOI=10.1074/jbc.m405860200;
RA Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.;
RT "In vivo and in vitro reconstitution of atg8 conjugation essential for
RT autophagy.";
RL J. Biol. Chem. 279:40584-40592(2004).
RN [14]
RP INTERACTION WITH ATG12.
RX PubMed=16874032; DOI=10.4161/auto.1.2.1858;
RA Hanada T., Ohsumi Y.;
RT "Structure-function relationship of Atg12, a ubiquitin-like modifier
RT essential for autophagy.";
RL Autophagy 1:110-118(2005).
RN [15]
RP FUNCTION.
RX PubMed=16027116; DOI=10.1074/jbc.m506736200;
RA Onodera J., Ohsumi Y.;
RT "Autophagy is required for maintenance of amino acid levels and protein
RT synthesis under nitrogen starvation.";
RL J. Biol. Chem. 280:31582-31586(2005).
RN [16]
RP FUNCTION.
RX PubMed=17632063; DOI=10.1016/j.cell.2007.05.021;
RA Nakatogawa H., Ichimura Y., Ohsumi Y.;
RT "Atg8, a ubiquitin-like protein required for autophagosome formation,
RT mediates membrane tethering and hemifusion.";
RL Cell 130:165-178(2007).
RN [17]
RP FUNCTION.
RX PubMed=17890363; DOI=10.1534/genetics.107.076596;
RA Ma J., Jin R., Jia X., Dobry C.J., Wang L., Reggiori F., Zhu J., Kumar A.;
RT "An interrelationship between autophagy and filamentous growth in budding
RT yeast.";
RL Genetics 177:205-214(2007).
RN [18]
RP INTERACTION WITH ATG3.
RX PubMed=17227760; DOI=10.1074/jbc.m611473200;
RA Yamada Y., Suzuki N.N., Hanada T., Ichimura Y., Kumeta H., Fujioka Y.,
RA Ohsumi Y., Inagaki F.;
RT "The crystal structure of Atg3, an autophagy-related ubiquitin carrier
RT protein (E2) enzyme that mediates Atg8 lipidation.";
RL J. Biol. Chem. 282:8036-8043(2007).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=18497569; DOI=10.4161/auto.6308;
RA Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.;
RT "Localization of autophagy-related proteins in yeast using a versatile
RT plasmid-based resource of fluorescent protein fusions.";
RL Autophagy 4:792-800(2008).
RN [20]
RP FUNCTION, AND INTERACTION WITH ATG8.
RX PubMed=18544538; DOI=10.1074/jbc.m801836200;
RA Oh-oka K., Nakatogawa H., Ohsumi Y.;
RT "Physiological pH and acidic phospholipids contribute to substrate
RT specificity in lipidation of Atg8.";
RL J. Biol. Chem. 283:21847-21852(2008).
RN [21]
RP FUNCTION.
RX PubMed=18725539; DOI=10.1083/jcb.200801035;
RA Cao Y., Cheong H., Song H., Klionsky D.J.;
RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae.";
RL J. Cell Biol. 182:703-713(2008).
RN [22]
RP FUNCTION.
RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA Millen J., Goldfarb D.S., Thumm M.;
RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT genes.";
RL Mol. Biol. Cell 19:4492-4505(2008).
RN [23]
RP FUNCTION.
RX PubMed=19302372; DOI=10.1111/j.1474-9726.2009.00469.x;
RA Alvers A.L., Fishwick L.K., Wood M.S., Hu D., Chung H.S., Dunn W.A. Jr.,
RA Aris J.P.;
RT "Autophagy and amino acid homeostasis are required for chronological
RT longevity in Saccharomyces cerevisiae.";
RL Aging Cell 8:353-369(2009).
RN [24]
RP FUNCTION.
RX PubMed=19061865; DOI=10.1016/j.bbrc.2008.11.084;
RA Kageyama T., Suzuki K., Ohsumi Y.;
RT "Lap3 is a selective target of autophagy in yeast, Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 378:551-557(2009).
RN [25]
RP SUBUNIT.
RX PubMed=21193819;
RA Bae J.Y., Park H.H.;
RT "Purification and characterization of a ubiquitin-like system for
RT autophagosome formation.";
RL J. Microbiol. Biotechnol. 20:1647-1652(2010).
RN [26]
RP FUNCTION.
RX PubMed=22785534; DOI=10.1038/cddis.2012.90;
RA Clapp C., Portt L., Khoury C., Sheibani S., Norman G., Ebner P., Eid R.,
RA Vali H., Mandato C.A., Madeo F., Greenwood M.T.;
RT "14-3-3 protects against stress-induced apoptosis.";
RL Cell Death Dis. 3:E348-E348(2012).
RN [27]
RP FUNCTION.
RX PubMed=22768199; DOI=10.1371/journal.pone.0040013;
RA Mijaljica D., Prescott M., Devenish R.J.;
RT "A late form of nucleophagy in Saccharomyces cerevisiae.";
RL PLoS ONE 7:E40013-E40013(2012).
RN [28]
RP FUNCTION.
RX PubMed=23660403; DOI=10.1016/j.febslet.2013.04.030;
RA Eiyama A., Kondo-Okamoto N., Okamoto K.;
RT "Mitochondrial degradation during starvation is selective and temporally
RT distinct from bulk autophagy in yeast.";
RL FEBS Lett. 587:1787-1792(2013).
RN [29]
RP FUNCTION, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-507; ARG-511 AND
RP GLU-524.
RX PubMed=29295865; DOI=10.1096/fj.201701057r;
RA Mashahreh B., Hassouna F., Soudah N., Cohen-Kfir E., Strulovich R.,
RA Haitin Y., Wiener R.;
RT "Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP
RT binding.";
RL FASEB J. 32:2794-2802(2018).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=22055190; DOI=10.1016/j.molcel.2011.08.034;
RA Taherbhoy A.M., Tait S.W., Kaiser S.E., Williams A.H., Deng A., Nourse A.,
RA Hammel M., Kurinov I., Rock C.O., Green D.R., Schulman B.A.;
RT "Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and
RT mechanism in the autophagy pathway.";
RL Mol. Cell 44:451-461(2011).
RN [31]
RP STRUCTURE BY NMR OF 601-630 IN COMPLEX WITH ATG8, X-RAY CRYSTALLOGRAPHY
RP (2.0 ANGSTROMS) IN COMPLEX WITH ARG8, FUNCTION, AND MUTAGENESIS OF ARG-443;
RP SER-466; TYR-486; ASP-490 AND ARG-550.
RX PubMed=22055191; DOI=10.1016/j.molcel.2011.08.035;
RA Noda N.N., Satoo K., Fujioka Y., Kumeta H., Ogura K., Nakatogawa H.,
RA Ohsumi Y., Inagaki F.;
RT "Structural basis of Atg8 activation by a homodimeric E1, Atg7.";
RL Mol. Cell 44:462-475(2011).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH ATG8, AND
RP INTERACTION WITH ATG3.
RX PubMed=22056771; DOI=10.1038/nsmb.2165;
RA Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.;
RT "Insights into noncanonical E1 enzyme activation from the structure of
RT autophagic E1 Atg7 with Atg8.";
RL Nat. Struct. Mol. Biol. 18:1323-1330(2011).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-613 IN COMPLEX WITH ATG3 AND
RP ATG10.
RX PubMed=23142976; DOI=10.1038/nsmb.2415;
RA Kaiser S.E., Mao K., Taherbhoy A.M., Yu S., Olszewski J.L., Duda D.M.,
RA Kurinov I., Deng A., Fenn T.D., Klionsky D.J., Schulman B.A.;
RT "Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and
RT Atg7-Atg10 structures.";
RL Nat. Struct. Mol. Biol. 19:1242-1249(2012).
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 and ATG8 for
CC its conjugation with phosphatidylethanolamine. Both systems are needed
CC for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC Autophagy is essential for maintenance of amino acid levels and protein
CC synthesis under nitrogen starvation. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC 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. Plays a role
CC in the regulation of filamentous growth and chronological longevity.
CC {ECO:0000269|PubMed:10233148, ECO:0000269|PubMed:10233150,
CC ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11149920,
CC ECO:0000269|PubMed:12965207, ECO:0000269|PubMed:15277523,
CC ECO:0000269|PubMed:16027116, ECO:0000269|PubMed:17632063,
CC ECO:0000269|PubMed:17890363, ECO:0000269|PubMed:18544538,
CC ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:18725539,
CC ECO:0000269|PubMed:19061865, ECO:0000269|PubMed:19302372,
CC ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22768199,
CC ECO:0000269|PubMed:22785534, ECO:0000269|PubMed:23660403,
CC ECO:0000269|PubMed:29295865, ECO:0000269|PubMed:7593182,
CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9759731}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for ATP-binding
CC (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with
CC ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-
CC 116' of ATG8 and with ATG12 through a thioester bond between Cys-507
CC and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150,
CC PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191).
CC Interacts also with ATG3 (PubMed:11139573, PubMed:17227760,
CC PubMed:22056771, PubMed:23142976). {ECO:0000269|PubMed:10233150,
CC ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11139573,
CC ECO:0000269|PubMed:16874032, ECO:0000269|PubMed:17227760,
CC ECO:0000269|PubMed:18544538, ECO:0000269|PubMed:21193819,
CC ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22056771,
CC ECO:0000269|PubMed:23142976, ECO:0000269|PubMed:29295865}.
CC -!- INTERACTION:
CC P38862; Q07879: ATG10; NbExp=7; IntAct=EBI-2677, EBI-36629;
CC P38862; P40344: ATG3; NbExp=10; IntAct=EBI-2677, EBI-3381;
CC P38862; P38862: ATG7; NbExp=3; IntAct=EBI-2677, EBI-2677;
CC P38862; P38182: ATG8; NbExp=12; IntAct=EBI-2677, EBI-2684;
CC P38862; Q9GZQ8: MAP1LC3B; Xeno; NbExp=2; IntAct=EBI-2677, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure.
CC -!- DOMAIN: The C-terminal 40 residues are required for homodimerization,
CC as well as the interactions with ATG3, ATG8 and ATG12; and the C-
CC terminal 17 residues are required for the ATG8 lipidation.
CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC through binding with ATP.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017925; BAA33474.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68016.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06864.1; -; Genomic_DNA.
DR PIR; S48910; S48910.
DR RefSeq; NP_012041.1; NM_001179302.1.
DR PDB; 2LI5; NMR; -; B=601-630.
DR PDB; 3RUI; X-ray; 1.91 A; A=293-630.
DR PDB; 3RUJ; X-ray; 2.10 A; A=1-294.
DR PDB; 3T7E; X-ray; 2.25 A; A=289-630.
DR PDB; 3T7F; X-ray; 1.89 A; A=1-289.
DR PDB; 3T7G; X-ray; 2.08 A; A/B=1-289.
DR PDB; 3T7H; X-ray; 1.60 A; A/B=1-289.
DR PDB; 3VH1; X-ray; 3.00 A; A=1-595.
DR PDB; 3VH2; X-ray; 3.30 A; A=1-613.
DR PDB; 3VH3; X-ray; 2.00 A; A=295-630.
DR PDB; 3VH4; X-ray; 2.65 A; A=295-630.
DR PDB; 4GSJ; X-ray; 1.70 A; A=1-289.
DR PDB; 4GSK; X-ray; 2.90 A; A/B=1-613.
DR PDB; 4GSL; X-ray; 2.70 A; A/B=1-613.
DR PDB; 5YEC; X-ray; 2.15 A; A/C=295-630.
DR PDBsum; 2LI5; -.
DR PDBsum; 3RUI; -.
DR PDBsum; 3RUJ; -.
DR PDBsum; 3T7E; -.
DR PDBsum; 3T7F; -.
DR PDBsum; 3T7G; -.
DR PDBsum; 3T7H; -.
DR PDBsum; 3VH1; -.
DR PDBsum; 3VH2; -.
DR PDBsum; 3VH3; -.
DR PDBsum; 3VH4; -.
DR PDBsum; 4GSJ; -.
DR PDBsum; 4GSK; -.
DR PDBsum; 4GSL; -.
DR PDBsum; 5YEC; -.
DR AlphaFoldDB; P38862; -.
DR BMRB; P38862; -.
DR SMR; P38862; -.
DR BioGRID; 36605; 122.
DR DIP; DIP-1196N; -.
DR IntAct; P38862; 8.
DR MINT; P38862; -.
DR STRING; 4932.YHR171W; -.
DR MaxQB; P38862; -.
DR PaxDb; P38862; -.
DR PRIDE; P38862; -.
DR TopDownProteomics; P38862; -.
DR EnsemblFungi; YHR171W_mRNA; YHR171W; YHR171W.
DR GeneID; 856576; -.
DR KEGG; sce:YHR171W; -.
DR SGD; S000001214; ATG7.
DR VEuPathDB; FungiDB:YHR171W; -.
DR eggNOG; KOG2337; Eukaryota.
DR GeneTree; ENSGT00390000017509; -.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; P38862; -.
DR OMA; VQTWRYS; -.
DR BioCyc; YEAST:G3O-31205-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; P38862; -.
DR PRO; PR:P38862; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38862; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IMP:SGD.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0006501; P:C-terminal protein lipidation; IDA:SGD.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IMP:SGD.
DR DisProt; DP02249; -.
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 3D-structure; Autophagy; Cytoplasm; Protein transport; Reference proteome;
KW Transport; Ubl conjugation pathway.
FT CHAIN 1..630
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212822"
FT REGION 591..630
FT /note="Homodimerization"
FT MOTIF 331..336
FT /note="GXGXXG motif"
FT ACT_SITE 507
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000269|PubMed:29295865"
FT MUTAGEN 333
FT /note="G->A: Loss of interaction with ATG8 and ATG12, and
FT no more ATG12-ATG5 conjugate. Defect in Cvt pathway and
FT autophagy."
FT /evidence="ECO:0000269|PubMed:10233150,
FT ECO:0000269|PubMed:11100732"
FT MUTAGEN 443
FT /note="R->A: Loss of interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:22055191"
FT MUTAGEN 466
FT /note="S->A: Loss of interaction with ATG8; when associated
FT with F-486 and A-490."
FT /evidence="ECO:0000269|PubMed:22055191"
FT MUTAGEN 486
FT /note="Y->F: Loss of interaction with ATG8; when associated
FT with A-466 and A-490."
FT /evidence="ECO:0000269|PubMed:22055191"
FT MUTAGEN 490
FT /note="D->A: Loss of interaction with ATG8; when associated
FT with A-466 and F-486."
FT /evidence="ECO:0000269|PubMed:22055191"
FT MUTAGEN 507
FT /note="C->A: Loss of interaction with ATG8 and ATG12 and no
FT more formation of ATG12-ATG5 conjugate. Defect in Cvt
FT pathway and autophagy."
FT /evidence="ECO:0000269|PubMed:10233150,
FT ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:15277523,
FT ECO:0000269|PubMed:29295865"
FT MUTAGEN 507
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 ATG8 (substrate) or between ATG7 and ATG12
FT (substrate), a stable complex with an O-ester bond is
FT formed. No more formation of ATG12-ATG5 conjugate."
FT /evidence="ECO:0000269|PubMed:10233150,
FT ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:15277523"
FT MUTAGEN 511
FT /note="R->A: Impaired homodimerization and ATP-binding.
FT Homodimerization and ATP-binding are recovered when it
FT heterodimerizes with an ATG7 molecule with a R-524
FT mutation."
FT /evidence="ECO:0000269|PubMed:29295865"
FT MUTAGEN 524
FT /note="E->R: Impaired homodimerization and ATP-binding.
FT Homodimerization and ATP-binding are recovered when it
FT heterodimerizes with an ATG7 molecule with a A-511
FT mutation."
FT /evidence="ECO:0000269|PubMed:29295865"
FT MUTAGEN 550
FT /note="R->A: Loss of interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:22055191"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3T7H"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3T7G"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3VH2"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4GSL"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3T7H"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 135..148
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3T7F"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3T7H"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3T7H"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3RUJ"
FT HELIX 294..312
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:3RUI"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3VH1"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4GSK"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3VH4"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 444..452
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:3VH1"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 513..529
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:3RUI"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:3RUI"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:3RUI"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:3RUI"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:2LI5"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:2LI5"
SQ SEQUENCE 630 AA; 71428 MW; 561EEC94F0ED57F5 CRC64;
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN IPKSADQVPL
FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL FLHQRALECW EDGIKDINKC
VSFVIISFAD LKKYRFYYWL GVPCFQRPSS TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV
CILDADDEIV NYDKCIIRKT KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI
IRQNEGSFAL NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK ITFVDNGTVS
YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK LSIPMIGHKL VNEEAQHKDF
DRLRALIKEH DIIFLLVDSR ESRWLPSLLS NIENKTVINA ALGFDSYLVM RHGNRDEQSS
KQLGCYFCHD VVAPTDSLTD RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT
VLGDIPHQIR GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
