ATG3_YEAST
ID ATG3_YEAST Reviewed; 310 AA.
AC P40344; D6W1I2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN Name=ATG3; Synonyms=APG3, AUT1; OrderedLocusNames=YNR007C; ORFNames=N2040;
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.
RX PubMed=9023185; DOI=10.1128/jb.179.4.1068-1076.1997;
RA Schlumpberger M., Schaeffeler E., Straub M., Bredschneider M., Wolf D.H.,
RA Thumm M.;
RT "AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 179:1068-1076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=8050581; DOI=10.1016/0014-5793(94)00672-5;
RA Thumm M., Egner R., Koch B., Schlumpberger M., Straub M., Veenhuis M.,
RA Wolf D.H.;
RT "Isolation of autophagocytosis mutants of Saccharomyces cerevisiae.";
RL FEBS Lett. 349:275-280(1994).
RN [7]
RP FUNCTION.
RX PubMed=11058089; DOI=10.1242/jcs.113.22.4025;
RA Suriapranata I., Epple U.D., Bernreuther D., Bredschneider M.,
RA Sovarasteanu K., Thumm M.;
RT "The breakdown of autophagic vesicles inside the vacuole depends on
RT Aut4p.";
RL J. Cell Sci. 113:4025-4033(2000).
RN [8]
RP FUNCTION, INTERACTION WITH ATG8, AND MUTAGENESIS OF CYS-234.
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 FUNCTION.
RX PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
RA Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
RT "The pre-autophagosomal structure organized by concerted functions of APG
RT genes is essential for autophagosome formation.";
RL EMBO J. 20:5971-5981(2001).
RN [10]
RP INTERACTION WITH ATG7.
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [12]
RP FUNCTION, AND INTERACTION WITH ATG7.
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 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 [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [15]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF CYS-234.
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 [17]
RP CRYSTALLIZATION.
RX PubMed=17012800; DOI=10.1107/s1744309106036098;
RA Yamada Y., Suzuki N.N., Fujioka Y., Ichimura Y., Ohsumi Y., Inagaki F.;
RT "Crystallization and preliminary X-ray analysis of Atg3.";
RL Acta Crystallogr. F 62:1016-1017(2006).
RN [18]
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 [19]
RP INDUCTION.
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 [20]
RP FUNCTION, AND INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
RX PubMed=17986448; DOI=10.1074/jbc.c700195200;
RA Hanada T., Noda N.N., Satomi Y., Ichimura Y., Fujioka Y., Takao T.,
RA Inagaki F., Ohsumi Y.;
RT "The Atg12-Atg5 conjugate has a novel E3-like activity for protein
RT lipidation in autophagy.";
RL J. Biol. Chem. 282:37298-37302(2007).
RN [21]
RP FUNCTION.
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 [22]
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 [23]
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 [24]
RP ACETYLATION BY THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
RX PubMed=19303850; DOI=10.1016/j.cell.2009.01.033;
RA Lin Y.Y., Lu J.Y., Zhang J., Walter W., Dang W., Wan J., Tao S.C., Qian J.,
RA Zhao Y., Boeke J.D., Berger S.L., Zhu H.;
RT "Protein acetylation microarray reveals that NuA4 controls key metabolic
RT target regulating gluconeogenesis.";
RL Cell 136:1073-1084(2009).
RN [25]
RP FUNCTION, INTERACTION WITH ATG8, LIPIDATION, AND DOMAIN.
RX PubMed=19285500; DOI=10.1016/j.febslet.2009.03.009;
RA Hanada T., Satomi Y., Takao T., Ohsumi Y.;
RT "The amino-terminal region of Atg3 is essential for association with
RT phosphatidylethanolamine in Atg8 lipidation.";
RL FEBS Lett. 583:1078-1083(2009).
RN [26]
RP INDUCTION.
RX PubMed=19235764; DOI=10.1002/yea.1655;
RA Roberts G.G. III, Hudson A.P.;
RT "Rsf1p is required for an efficient metabolic shift from fermentative to
RT glycerol-based respiratory growth in S. cerevisiae.";
RL Yeast 26:95-110(2009).
RN [27]
RP FUNCTION, INTERACTION WITH ATG8, DOMAIN, AND MUTAGENESIS OF TRP-270;
RP ASP-272 AND LEU-273.
RX PubMed=20615880; DOI=10.1074/jbc.m110.113670;
RA Yamaguchi M., Noda N.N., Nakatogawa H., Kumeta H., Ohsumi Y., Inagaki F.;
RT "Autophagy-related protein 8 (Atg8) family interacting motif in Atg3
RT mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-
RT vacuole targeting pathway.";
RL J. Biol. Chem. 285:29599-29607(2010).
RN [28]
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 [29]
RP INTERACTION WITH ATG7 AND ATG8.
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 [30]
RP INTERACTION WITH ATG7.
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 [31]
RP FUNCTION.
RX PubMed=22240591; DOI=10.4161/auto.8.2.18373;
RA Nakatogawa H., Ishii J., Asai E., Ohsumi Y.;
RT "Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome
RT biogenesis.";
RL Autophagy 8:177-186(2012).
RN [32]
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 [33]
RP ACETYLATION AT LYS-19 AND LYS-48, DEACETYLATION BY RPD3, AND FUNCTION.
RX PubMed=22539722; DOI=10.1126/science.1216990;
RA Yi C., Ma M., Ran L., Zheng J., Tong J., Zhu J., Ma C., Sun Y., Zhang S.,
RA Feng W., Zhu L., Le Y., Gong X., Yan X., Hong B., Jiang F.J., Xie Z.,
RA Miao D., Deng H., Yu L.;
RT "Function and molecular mechanism of acetylation in autophagy regulation.";
RL Science 336:474-477(2012).
RN [34]
RP FUNCTION, MUTAGENESIS OF THR-213, INTERACTION WITH THE ATG12-ATG5
RP CONJUGATE, AND ACTIVITY REGULATION.
RX PubMed=23503366; DOI=10.1038/nsmb.2527;
RA Sakoh-Nakatogawa M., Matoba K., Asai E., Kirisako H., Ishii J., Noda N.N.,
RA Inagaki F., Nakatogawa H., Ohsumi Y.;
RT "Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its
RT catalytic site.";
RL Nat. Struct. Mol. Biol. 20:433-439(2013).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, DOMAIN, AND INTERACTION
RP WITH ATG7 AND ATG8.
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 [36]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 128-144 IN COMPLEX WITH ATG7.
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 [37]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATG7.
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: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy. 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. Responsible
CC for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3
CC and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine
CC (PE). This step is required for the membrane association of ATG8. The
CC formation of the ATG8-phosphatidylethanolamine conjugate is essential
CC for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC ATG8-PE conjugate mediates tethering between adjacent membranes and
CC stimulates membrane hemifusion, leading to expansion of the
CC autophagosomal membrane during autophagy. {ECO:0000269|PubMed:11058089,
CC ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11149920,
CC ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:12965207,
CC ECO:0000269|PubMed:15277523, ECO:0000269|PubMed:17227760,
CC ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:17986448,
CC ECO:0000269|PubMed:18544538, ECO:0000269|PubMed:18701704,
CC ECO:0000269|PubMed:18725539, ECO:0000269|PubMed:19285500,
CC ECO:0000269|PubMed:20615880, ECO:0000269|PubMed:22240591,
CC ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:22768199,
CC ECO:0000269|PubMed:23503366, ECO:0000269|PubMed:8050581,
CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9023185}.
CC -!- ACTIVITY REGULATION: ATG12-ATG5 induces reorientation of the ATG3
CC structure, increasing conjugation activity of ATG3.
CC {ECO:0000269|PubMed:23503366}.
CC -!- SUBUNIT: Monomer. Interacts with ATG8 through an intermediate thioester
CC bond between Cys-234 and the C-terminal Gly of ATG8. Also interacts
CC with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme.
CC Interacts also with the ATG12-ATG5 conjugate.
CC {ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11139573,
CC ECO:0000269|PubMed:12965207, ECO:0000269|PubMed:17227760,
CC ECO:0000269|PubMed:17986448, ECO:0000269|PubMed:19285500,
CC ECO:0000269|PubMed:20615880, ECO:0000269|PubMed:21193819,
CC ECO:0000269|PubMed:22055190, ECO:0000269|PubMed:22055191,
CC ECO:0000269|PubMed:22056771, ECO:0000269|PubMed:23142976,
CC ECO:0000269|PubMed:23503366}.
CC -!- INTERACTION:
CC P40344; P38862: ATG7; NbExp=10; IntAct=EBI-3381, EBI-2677;
CC P40344; P38182: ATG8; NbExp=9; IntAct=EBI-3381, EBI-2684;
CC P40344; Q9GZQ8: MAP1LC3B; Xeno; NbExp=2; IntAct=EBI-3381, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11149920,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is increased during filamentous growth and
CC controlled by the RSF2 transcription factor.
CC {ECO:0000269|PubMed:17890363, ECO:0000269|PubMed:19235764}.
CC -!- DOMAIN: The N-terminal region (residues 1-7) is involved in
CC phosphatidylethanolamine-binding and is required for ATG8-PE
CC conjugation.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-
CC vacuole targeting pathway.
CC -!- PTM: Acetylated by NuA4 complex acetyltransferase ESA1 at Lys-19 and
CC Lys-48. Acetylation regulates autophagy by controlling ATG8 interaction
CC and lipidation. Deacetylated by histone deacetylase RPD3.
CC {ECO:0000269|PubMed:19303850, ECO:0000269|PubMed:22539722}.
CC -!- MISCELLANEOUS: Present with 3610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; X77395; CAA54575.1; -; Genomic_DNA.
DR EMBL; Z71622; CAA96284.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10548.1; -; Genomic_DNA.
DR PIR; S45130; S45130.
DR RefSeq; NP_014404.3; NM_001183184.3.
DR PDB; 2DYT; X-ray; 2.50 A; A=1-310.
DR PDB; 3T7G; X-ray; 2.08 A; C/D=128-144.
DR PDB; 4GSL; X-ray; 2.70 A; C/D=1-310.
DR PDB; 6OJJ; X-ray; 2.41 A; A=19-310.
DR PDBsum; 2DYT; -.
DR PDBsum; 3T7G; -.
DR PDBsum; 4GSL; -.
DR PDBsum; 6OJJ; -.
DR AlphaFoldDB; P40344; -.
DR SMR; P40344; -.
DR BioGRID; 35832; 327.
DR DIP; DIP-1190N; -.
DR ELM; P40344; -.
DR IntAct; P40344; 11.
DR MINT; P40344; -.
DR STRING; 4932.YNR007C; -.
DR iPTMnet; P40344; -.
DR MaxQB; P40344; -.
DR PaxDb; P40344; -.
DR PRIDE; P40344; -.
DR EnsemblFungi; YNR007C_mRNA; YNR007C; YNR007C.
DR GeneID; 855741; -.
DR KEGG; sce:YNR007C; -.
DR SGD; S000005290; ATG3.
DR VEuPathDB; FungiDB:YNR007C; -.
DR eggNOG; KOG2981; Eukaryota.
DR GeneTree; ENSGT00390000010308; -.
DR HOGENOM; CLU_027518_2_0_1; -.
DR InParanoid; P40344; -.
DR OMA; YDKYYQV; -.
DR BioCyc; YEAST:G3O-33325-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR EvolutionaryTrace; P40344; -.
DR PRO; PR:P40344; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40344; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0061908; C:phagophore; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0019776; F:Atg8 ligase activity; IMP:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006501; P:C-terminal protein lipidation; IDA:SGD.
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:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR DisProt; DP02826; -.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Cytoplasm; Protein transport;
KW Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..310
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000213586"
FT REGION 83..163
FT /note="Flexible region"
FT REGION 238..285
FT /note="Handle region"
FT MOTIF 270..273
FT /note="ATG8 interaction motif (AIM)"
FT ACT_SITE 234
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255"
FT BINDING 1..7
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT MOD_RES 19
FT /note="N6-acetyllysine; by ESA1"
FT /evidence="ECO:0000269|PubMed:22539722"
FT MOD_RES 48
FT /note="N6-acetyllysine; by ESA1"
FT /evidence="ECO:0000269|PubMed:22539722"
FT MUTAGEN 213
FT /note="T->A: Decreases ATG8-PE comjugation and autophagy."
FT /evidence="ECO:0000269|PubMed:23503366"
FT MUTAGEN 234
FT /note="C->A: Loss of interaction with ATG8 and defect in
FT autophagy and Cvt pathway."
FT /evidence="ECO:0000269|PubMed:11100732,
FT ECO:0000269|PubMed:15277523"
FT MUTAGEN 234
FT /note="C->S: Instead of the formation of an intermediate
FT complex with a thiol ester bond between ATG3 (E2-like
FT enzyme) and ATG8 (substrate), a stable complex with an O-
FT ester bond is formed."
FT /evidence="ECO:0000269|PubMed:11100732,
FT ECO:0000269|PubMed:15277523"
FT MUTAGEN 270
FT /note="W->A: Decreases interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:20615880"
FT MUTAGEN 272
FT /note="D->A: Decreases interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:20615880"
FT MUTAGEN 273
FT /note="L->A: Decreases interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:20615880"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:6OJJ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4GSL"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6OJJ"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2DYT"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3T7G"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:6OJJ"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:6OJJ"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:6OJJ"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6OJJ"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6OJJ"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 236..255
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6OJJ"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:6OJJ"
SQ SEQUENCE 310 AA; 35887 MW; 52CCFB216B18CF0C CRC64;
MIRSTLSSWR EYLTPITHKS TFLTTGQITP EEFVQAGDYL CHMFPTWKWN EESSDISYRD
FLPKNKQFLI IRKVPCDKRA EQCVEVEGPD VIMKGFAEDG DEDDVLEYIG SETEHVQSTP
AGGTKDSSID DIDELIQDME IKEEDENDDT EEFNAKGGLA KDMAQERYYD LYIAYSTSYR
VPKMYIVGFN SNGSPLSPEQ MFEDISADYR TKTATIEKLP FYKNSVLSVS IHPCKHANVM
KILLDKVRVV RQRRRKELQE EQELDGVGDW EDLQDDIDDS LRVDQYLIVF LKFITSVTPS
IQHDYTMEGW
