ATG5_YEAST
ID ATG5_YEAST Reviewed; 294 AA.
AC Q12380; D6W3M0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Autophagy protein 5;
GN Name=ATG5; Synonyms=APG5; OrderedLocusNames=YPL149W; ORFNames=P2601;
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=8921905; DOI=10.1016/0378-1119(96)00354-x;
RA Kametaka S., Matsuura A., Wada Y., Ohsumi Y.;
RT "Structural and functional analyses of APG5, a gene involved in autophagy
RT in yeast.";
RL Gene 178:139-143(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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, CONJUGATION TO ATG12, AND MUTAGENESIS OF LYS-149.
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 [7]
RP FUNCTION, AND INTERACTION WITH ATG12 AND ATG16.
RX PubMed=10406794; DOI=10.1093/emboj/18.14.3888;
RA Mizushima N., Noda T., Ohsumi Y.;
RT "Apg16p is required for the function of the Apg12p-Apg5p conjugate in the
RT yeast autophagy pathway.";
RL EMBO J. 18:3888-3896(1999).
RN [8]
RP FUNCTION.
RX PubMed=10712513; DOI=10.1091/mbc.11.3.969;
RA George M.D., Baba M., Scott S.V., Mizushima N., Garrison B.S., Ohsumi Y.,
RA Klionsky D.J.;
RT "Apg5p functions in the sequestration step in the cytoplasm-to-vacuole
RT targeting and macroautophagy pathways.";
RL Mol. Biol. Cell 11:969-982(2000).
RN [9]
RP SUBCELLULAR LOCATION.
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 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 IDENTIFICATION IN A COMPLEX WITH ATG12 AND ATG16.
RX PubMed=11897782; DOI=10.1074/jbc.m111889200;
RA Kuma A., Mizushima N., Ishihara N., Ohsumi Y.;
RT "Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric
RT complex, mediated by Apg16 oligomerization, is essential for autophagy in
RT yeast.";
RL J. Biol. Chem. 277:18619-18625(2002).
RN [12]
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 [13]
RP CONJUGATION TO ATG12.
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 [14]
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 [15]
RP FUNCTION.
RX PubMed=15247238; DOI=10.1074/jbc.m406960200;
RA Kissova I., Deffieu M., Manon S., Camougrand N.M.;
RT "Uth1p is involved in the autophagic degradation of mitochondria.";
RL J. Biol. Chem. 279:39068-39074(2004).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=15155809; DOI=10.1091/mbc.e04-02-0147;
RA Stromhaug P.E., Reggiori F., Guan J., Wang C.-W., Klionsky D.J.;
RT "Atg21 is a phosphoinositide binding protein required for efficient
RT lipidation and localization of Atg8 during uptake of aminopeptidase I by
RT selective autophagy.";
RL Mol. Biol. Cell 15:3553-3566(2004).
RN [17]
RP FUNCTION, CONJUGATION TO ATG12, AND INTERACTION WITH ATG16.
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 [18]
RP FUNCTION.
RX PubMed=15947785; DOI=10.1038/sj.cdd.4401697;
RA Priault M., Salin B., Schaeffer J., Vallette F.M., di Rago J.P.,
RA Martinou J.C.;
RT "Impairing the bioenergetic status and the biogenesis of mitochondria
RT triggers mitophagy in yeast.";
RL Cell Death Differ. 12:1613-1621(2005).
RN [19]
RP CRYSTALLIZATION OF THE ATG5-ATG16 COMPLEX.
RX PubMed=17012802; DOI=10.1107/s1744309106036232;
RA Matsushita M., Suzuki N.N., Fujioka Y., Ohsumi Y., Inagaki F.;
RT "Expression, purification and crystallization of the Atg5-Atg16 complex
RT essential for autophagy.";
RL Acta Crystallogr. F 62:1021-1023(2006).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
RA Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
RT "Hierarchy of Atg proteins in pre-autophagosomal structure organization.";
RL Genes Cells 12:209-218(2007).
RN [21]
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 [22]
RP FUNCTION OF THE ATG12-ATG5 CONJUGATE, AND INTERACTION WITH ATG3.
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 [23]
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 [24]
RP FUNCTION.
RX PubMed=18625846; DOI=10.1083/jcb.200711112;
RA Geng J., Baba M., Nair U., Klionsky D.J.;
RT "Quantitative analysis of autophagy-related protein stoichiometry by
RT fluorescence microscopy.";
RL J. Cell Biol. 182:129-140(2008).
RN [25]
RP CONJUGATION TO ATG12, AND FUNCTION OF THE ATG12-ATG5 CONJUGATE.
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 [26]
RP CRYSTALLIZATION OF THE ATG12-ATG5 CONJUGATE BOUND TO ATG16.
RX PubMed=18421155; DOI=10.1107/s0909049507054799;
RA Noda N.N., Fujioka Y., Ohsumi Y., Inagaki F.;
RT "Crystallization of the Atg12-Atg5 conjugate bound to Atg16 by the free-
RT interface diffusion method.";
RL J. Synchrotron Radiat. 15:266-268(2008).
RN [27]
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 [28]
RP CONJUGATION TO ATG12.
RX PubMed=21703229; DOI=10.1016/j.bbrc.2011.06.061;
RA Yamagata M., Obara K., Kihara A.;
RT "Sphingolipid synthesis is involved in autophagy in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 410:786-791(2011).
RN [29]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE ATG5-ATG12/ATG16 COMPLEX.
RX PubMed=23064152; DOI=10.1038/emboj.2012.278;
RA Romanov J., Walczak M., Ibiricu I., Schuchner S., Ogris E., Kraft C.,
RA Martens S.;
RT "Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16
RT complex during autophagosome formation.";
RL EMBO J. 31:4304-4317(2012).
RN [30]
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 [31]
RP SUBCELLULAR LOCATION.
RX PubMed=23549786; DOI=10.1242/jcs.122960;
RA Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.;
RT "Fine mapping of autophagy-related proteins during autophagosome formation
RT in Saccharomyces cerevisiae.";
RL J. Cell Sci. 126:2534-2544(2013).
RN [32]
RP FUNCTION OF THE ATG12-ATG5 CONJUGATE, AND INTERACTION WITH ATG3.
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 [33]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH ATG16.
RX PubMed=17192262; DOI=10.1074/jbc.m609876200;
RA Matsushita M., Suzuki N.N., Obara K., Fujioka Y., Ohsumi Y., Inagaki F.;
RT "Structure of Atg5.Atg16, a complex essential for autophagy.";
RL J. Biol. Chem. 282:6763-6772(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-284 IN CONJUGATION WITH ATG12.
RX PubMed=23238393; DOI=10.1038/embor.2012.208;
RA Noda N.N., Fujioka Y., Hanada T., Ohsumi Y., Inagaki F.;
RT "Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating
RT Atg8-PE conjugation.";
RL EMBO Rep. 14:206-211(2013).
CC -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC autophagic vesicle formation. Autophagy is essential for maintenance of
CC amino acid levels and protein synthesis under nitrogen starvation.
CC Required for selective autophagic degradation of the nucleus
CC (nucleophagy). Also required for mitophagy, which eliminates defective
CC or superfluous mitochondria in order to fulfill cellular energy
CC requirements and prevent excess ROS production. Conjugation with ATG12,
CC through a ubiquitin-like conjugating system involving ATG7 as an E1-
CC like activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC essential for its function. The ATG12-ATG5 conjugate acts as an E3-like
CC enzyme which is required for lipidation of ATG8 and ATG8 association to
CC the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center
CC and enhances its E2 activity. Plays a role in the regulation of
CC filamentous growth and chronological longevity.
CC {ECO:0000269|PubMed:10406794, ECO:0000269|PubMed:10712513,
CC ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:15247238,
CC ECO:0000269|PubMed:15947785, ECO:0000269|PubMed:16874032,
CC ECO:0000269|PubMed:17890363, ECO:0000269|PubMed:17986448,
CC ECO:0000269|PubMed:18625846, ECO:0000269|PubMed:18701704,
CC ECO:0000269|PubMed:18725539, ECO:0000269|PubMed:22768199,
CC ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23503366,
CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:8921905,
CC ECO:0000269|PubMed:9759731}.
CC -!- SUBUNIT: Conjugated with ATG12. The ATG5-ATG12 conjugate forms a
CC complex with several units of ATG16. The ATG12-ATG5 conjugate
CC associates also with ATG3. {ECO:0000269|PubMed:11897782,
CC ECO:0000269|PubMed:17192262}.
CC -!- INTERACTION:
CC Q12380; P38316: ATG12; NbExp=9; IntAct=EBI-2664, EBI-2692;
CC Q12380; Q03818: ATG16; NbExp=4; IntAct=EBI-2664, EBI-27344;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:15155809,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18497569,
CC ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11689437,
CC ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:17295840,
CC ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:23064152,
CC ECO:0000269|PubMed:23549786}. Note=Localizes to the isolation membrane
CC (IM), a membrane sac which is generated from the pre-autophagosomal
CC structure (PAS). Ultimately, the IM expands to become a mature
CC autophagosome. Localizes also to a dot at the junction between the IM
CC and the vacuolar membrane, termed the vacuole-IM contact site (VICS).
CC Correct localization to the PAS requires ATG21.
CC -!- PTM: Conjugated to ATG12; which is essential for autophagy. Conjugation
CC with ATG12 involves ATG7 as an E1-like activating enzyme and ATG10 as
CC an E2-like conjugating enzyme.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Small amount of ATG5-ATG12 conjugate is enough to
CC perform normal autophagy.
CC -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR EMBL; D83519; BAA11937.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65572.1; -; Genomic_DNA.
DR EMBL; Z73505; CAA97854.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11286.1; -; Genomic_DNA.
DR PIR; S65160; S65160.
DR RefSeq; NP_015176.1; NM_001183963.1.
DR PDB; 2DYM; X-ray; 2.20 A; A/C/E/G=1-294.
DR PDB; 2DYO; X-ray; 1.97 A; A=1-294.
DR PDB; 3W1S; X-ray; 2.60 A; A=1-284.
DR PDBsum; 2DYM; -.
DR PDBsum; 2DYO; -.
DR PDBsum; 3W1S; -.
DR AlphaFoldDB; Q12380; -.
DR SMR; Q12380; -.
DR BioGRID; 36034; 169.
DR ComplexPortal; CPX-1848; ATG12-ATG5 complex.
DR ComplexPortal; CPX-1849; ATG12-ATG5-ATG16 complex.
DR DIP; DIP-1195N; -.
DR IntAct; Q12380; 30.
DR MINT; Q12380; -.
DR STRING; 4932.YPL149W; -.
DR MaxQB; Q12380; -.
DR PaxDb; Q12380; -.
DR PRIDE; Q12380; -.
DR EnsemblFungi; YPL149W_mRNA; YPL149W; YPL149W.
DR GeneID; 855954; -.
DR KEGG; sce:YPL149W; -.
DR SGD; S000006070; ATG5.
DR VEuPathDB; FungiDB:YPL149W; -.
DR eggNOG; KOG2976; Eukaryota.
DR GeneTree; ENSGT00390000004766; -.
DR HOGENOM; CLU_051894_2_0_1; -.
DR InParanoid; Q12380; -.
DR OMA; KWHYPLG; -.
DR BioCyc; YEAST:G3O-34046-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy.
DR EvolutionaryTrace; Q12380; -.
DR PRO; PR:Q12380; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12380; protein.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IDA:SGD.
DR GO; GO:0005776; C:autophagosome; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0061908; C:phagophore; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:1990234; C:transferase complex; IDA:ComplexPortal.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD.
DR GO; GO:0140355; F:cargo receptor ligand activity; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
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: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; IDA:ComplexPortal.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006497; P:protein lipidation; IDA:ComplexPortal.
DR GO; GO:0061912; P:selective autophagy; IMP:SGD.
DR Gene3D; 1.10.246.190; -; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR IDEAL; IID50256; -.
DR InterPro; IPR007239; Atg5.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR042527; Atg5_UblA_dom.
DR PANTHER; PTHR13040; PTHR13040; 1.
DR Pfam; PF04106; APG5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Hydrolase; Isopeptide bond; Membrane;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..294
FT /note="Autophagy protein 5"
FT /id="PRO_0000219010"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT MUTAGEN 149
FT /note="K->R: Loss of conjugation."
FT /evidence="ECO:0000269|PubMed:9759731"
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2DYO"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3W1S"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2DYM"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2DYO"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2DYM"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2DYM"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2DYO"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2DYO"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:2DYO"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:2DYO"
SQ SEQUENCE 294 AA; 33560 MW; BE513A631DEAA0A1 CRC64;
MNDIKQLLWN GELNVLVSID PSFLMKGSPR EIAVLRIRVP RETYLVNYMP LIWNKIKSFL
SFDPLTDSEK YFWFEHNKTP IPWNYPVGVL FDCLAGKSAT FTTSFENQVK DVLTFLRIHL
VMGDSLPPTI IPIASSKTQA EKFWFHQWKQ VCFILNGSSK AIMSLSVNEA RKFWGSVITR
NFQDFIEISN KISSSRPRHI PLIIQTSRTS GTFRISQPTI SMTGVNPTLK DIEGDILDVK
EGINGNDVMV ICQGIEIPWH MLLYDLYSKL RSFDGFLYIT LVPIKGGDKA SSEL
