ATG2_YEAST
ID ATG2_YEAST Reviewed; 1592 AA.
AC P53855; D6W0V1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Autophagy-related protein 2;
DE AltName: Full=Sporulation-specific protein 72;
GN Name=ATG2; Synonyms=APG2, AUT8, SPO72; OrderedLocusNames=YNL242W;
GN ORFNames=N1106;
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].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [2]
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 [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=10029994;
RX DOI=10.1002/(sici)1097-0061(19990130)15:2<155::aid-yea342>3.0.co;2-u;
RA Saiz J.E., de Los Angeles Santos M., Vazquez de Aldana C.R., Revuelta J.L.;
RT "Disruption of six unknown open reading frames from Saccharomyces
RT cerevisiae reveals two genes involved in vacuolar morphogenesis and one
RT gene required for sporulation.";
RL Yeast 15:155-164(1999).
RN [6]
RP FUNCTION.
RX PubMed=11675007; DOI=10.1016/s0378-1119(01)00614-x;
RA Barth H., Thumm M.;
RT "A genomic screen identifies AUT8 as a novel gene essential for autophagy
RT in the yeast Saccharomyces cerevisiae.";
RL Gene 274:151-156(2001).
RN [7]
RP FUNCTION.
RX PubMed=11382760; DOI=10.1074/jbc.m102342200;
RA Wang C.-W., Kim J., Huang W.-P., Abeliovich H., Stromhaug P.E.,
RA Dunn W.A. Jr., Klionsky D.J.;
RT "Apg2 is a novel protein required for the cytoplasm to vacuole targeting,
RT autophagy, and pexophagy pathways.";
RL J. Biol. Chem. 276:30442-30451(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-83.
RX PubMed=11382761; DOI=10.1074/jbc.m102346200;
RA Shintani T., Suzuki K., Kamada Y., Noda T., Ohsumi Y.;
RT "Apg2p functions in autophagosome formation on the perivacuolar
RT structure.";
RL J. Biol. Chem. 276:30452-30460(2001).
RN [9]
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 [10]
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14723849; DOI=10.1016/s1534-5807(03)00402-7;
RA Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
RT "The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from
RT the pre-autophagosomal structure.";
RL Dev. Cell 6:79-90(2004).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG18.
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 [13]
RP FUNCTION, INTERACTION WITH ATG18, AND SUBCELLULAR LOCATION.
RX PubMed=18586673; DOI=10.1074/jbc.m803180200;
RA Obara K., Sekito T., Niimi K., Ohsumi Y.;
RT "The Atg18-Atg2 complex is recruited to autophagic membranes via
RT phosphatidylinositol 3-phosphate and exerts an essential function.";
RL J. Biol. Chem. 283:23972-23980(2008).
RN [14]
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 [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18829864; DOI=10.1091/mbc.e08-05-0544;
RA He C., Baba M., Cao Y., Klionsky D.J.;
RT "Self-interaction is critical for Atg9 transport and function at the
RT phagophore assembly site during autophagy.";
RL Mol. Biol. Cell 19:5506-5516(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP FUNCTION.
RX PubMed=19371383; DOI=10.1111/j.1365-2443.2009.01299.x;
RA Sekito T., Kawamata T., Ichikawa R., Suzuki K., Ohsumi Y.;
RT "Atg17 recruits Atg9 to organize the pre-autophagosomal structure.";
RL Genes Cells 14:525-538(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=20444982; DOI=10.1091/mbc.e09-04-0345;
RA van der Vaart A., Griffith J., Reggiori F.;
RT "Exit from the Golgi is required for the expansion of the autophagosomal
RT phagophore in yeast Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 21:2270-2284(2010).
RN [20]
RP FUNCTION.
RX PubMed=19995911; DOI=10.1128/mcb.01344-09;
RA Kamada Y., Yoshino K., Kondo C., Kawamata T., Oshiro N., Yonezawa K.,
RA Ohsumi Y.;
RT "Tor directly controls the Atg1 kinase complex to regulate autophagy.";
RL Mol. Cell. Biol. 30:1049-1058(2010).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22728243; DOI=10.1016/j.febslet.2012.06.008;
RA Kobayashi T., Suzuki K., Ohsumi Y.;
RT "Autophagosome formation can be achieved in the absence of Atg18 by
RT expressing engineered PAS-targeted Atg2.";
RL FEBS Lett. 586:2473-2478(2012).
RN [22]
RP INTERACTION WITH ATG18.
RX PubMed=22851171; DOI=10.1074/jbc.m112.397570;
RA Watanabe Y., Kobayashi T., Yamamoto H., Hoshida H., Akada R., Inagaki F.,
RA Ohsumi Y., Noda N.N.;
RT "Structure-based analyses reveal distinct binding sites for Atg2 and
RT phosphoinositides in Atg18.";
RL J. Biol. Chem. 287:31681-31690(2012).
RN [23]
RP FUNCTION.
RX PubMed=23337777; DOI=10.1016/j.exger.2013.01.006;
RA Aris J.P., Alvers A.L., Ferraiuolo R.A., Fishwick L.K., Hanvivatpong A.,
RA Hu D., Kirlew C., Leonard M.T., Losin K.J., Marraffini M., Seo A.Y.,
RA Swanberg V., Westcott J.L., Wood M.S., Leeuwenburgh C., Dunn W.A. Jr.;
RT "Autophagy and leucine promote chronological longevity and respiration
RT proficiency during calorie restriction in yeast.";
RL Exp. Gerontol. 48:1107-1119(2013).
RN [24]
RP INTERACTION WITH ATG18, AND FUNCTION.
RX PubMed=23230146; DOI=10.1242/jcs.115725;
RA Rieter E., Vinke F., Bakula D., Cebollero E., Ungermann C.,
RA Proikas-Cezanne T., Reggiori F.;
RT "Atg18 function in autophagy is regulated by specific sites within its
RT beta-propeller.";
RL J. Cell Sci. 126:593-604(2013).
RN [25]
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 [26]
RP SUBCELLULAR LOCATION.
RX PubMed=23904270; DOI=10.1091/mbc.e13-07-0381;
RA Graef M., Friedman J.R., Graham C., Babu M., Nunnari J.;
RT "ER exit sites are physical and functional core autophagosome biogenesis
RT components.";
RL Mol. Biol. Cell 24:2918-2931(2013).
RN [27]
RP PHOSPHORYLATION AT SER-249 AND SER-1086, AND MUTAGENESIS OF SER-249 AND
RP SER-1086.
RX PubMed=24440502; DOI=10.1016/j.molcel.2013.12.011;
RA Papinski D., Schuschnig M., Reiter W., Wilhelm L., Barnes C.A.,
RA Maiolica A., Hansmann I., Pfaffenwimmer T., Kijanska M., Stoffel I.,
RA Lee S.S., Brezovich A., Lou J.H., Turk B.E., Aebersold R., Ammerer G.,
RA Peter M., Kraft C.;
RT "Early steps in autophagy depend on direct phosphorylation of Atg9 by the
RT Atg1 kinase.";
RL Mol. Cell 53:471-483(2014).
RN [28]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28704456; DOI=10.1371/journal.pone.0181047;
RA Hirata E., Ohya Y., Suzuki K.;
RT "Atg4 plays an important role in efficient expansion of autophagic
RT isolation membranes by cleaving lipidated Atg8 in Saccharomyces
RT cerevisiae.";
RL PLoS ONE 12:e0181047-e0181047(2017).
RN [29]
RP INTERACTION WITH ATG9, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=29848619; DOI=10.1083/jcb.201710116;
RA Gomez-Sanchez R., Rose J., Guimaraes R., Mari M., Papinski D., Rieter E.,
RA Geerts W.J., Hardenberg R., Kraft C., Ungermann C., Reggiori F.;
RT "Atg9 establishes Atg2-dependent contact sites between the endoplasmic
RT reticulum and phagophores.";
RL J. Cell Biol. 217:2743-2763(2018).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG18, DOMAIN, AND
RP MUTAGENESIS OF 1352-PHE--ILE-1355.
RX PubMed=30254161; DOI=10.1073/pnas.1806727115;
RA Kotani T., Kirisako H., Koizumi M., Ohsumi Y., Nakatogawa H.;
RT "The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the
RT endoplasmic reticulum for autophagosome formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:10363-10368(2018).
RN [31]
RP FUNCTION.
RX PubMed=32883836; DOI=10.1126/science.aaz7714;
RA Sawa-Makarska J., Baumann V., Coudevylle N., von Buelow S., Nogellova V.,
RA Abert C., Schuschnig M., Graef M., Hummer G., Martens S.;
RT "Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds
RT for membrane formation.";
RL Science 369:0-0(2020).
CC -!- FUNCTION: Lipid transfer protein required for autophagosome completion
CC and peroxisome degradation (PubMed:8224160, PubMed:10029994,
CC PubMed:11382760, PubMed:11382761, PubMed:11675007, PubMed:18586673,
CC PubMed:18625846, PubMed:19371383, PubMed:19995911, PubMed:22728243,
CC PubMed:23230146). Tethers the edge of the isolation membrane (IM) to
CC the endoplasmic reticulum (ER) and mediates direct lipid transfer from
CC ER to IM for IM expansion (PubMed:28704456, PubMed:29848619,
CC PubMed:30254161). ATG2 binds to the ER exit site (ERES), which is the
CC membrane source for autophagosome formation, using basic residues in
CC its N-terminal region (NR) and to the expanding edge of the IM through
CC its C-terminal region (PubMed:30254161). The latter binding is assisted
CC by an ATG18-PtdIns3P interaction (PubMed:30254161). ATG2 then extracts
CC phospholipids from the membrane source using its NR and transfers them
CC to ATG9 to the IM through its predicted beta-sheet-rich structure for
CC membrane expansion (PubMed:30254161). ATG2 is also involved in the
CC recruitment of lipids to a restricted region close to the vacuole,
CC termed the vacuole-isolation membrane contact site (VICS), which is
CC also essential for autophagosome formation (PubMed:28704456). Necessary
CC for the localization of ATG18 to the preautophagosomal structure (PAS)
CC and the binding of ATG18 to ATG9 (PubMed:14723849, PubMed:18586673,
CC PubMed:18625846, PubMed:19371383, PubMed:23230146). ATG2 is the most
CC downstream ATG protein in the preautophagosomal structure organization
CC process (PubMed:17295840). Involved in correct ATG9 trafficking through
CC the preautophagosomal structure and in peroxisome degradation
CC (PubMed:14723849). Plays a significant role in life span extension
CC (PubMed:23337777). {ECO:0000269|PubMed:10029994,
CC ECO:0000269|PubMed:11382760, ECO:0000269|PubMed:11382761,
CC ECO:0000269|PubMed:11675007, ECO:0000269|PubMed:14723849,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18586673,
CC ECO:0000269|PubMed:18625846, ECO:0000269|PubMed:19371383,
CC ECO:0000269|PubMed:19995911, ECO:0000269|PubMed:22728243,
CC ECO:0000269|PubMed:23230146, ECO:0000269|PubMed:23337777,
CC ECO:0000269|PubMed:28704456, ECO:0000269|PubMed:29848619,
CC ECO:0000269|PubMed:30254161, ECO:0000269|PubMed:8224160}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- SUBUNIT: Interacts with ATG18 (PubMed:17295840, PubMed:18586673,
CC PubMed:22851171, PubMed:23230146, PubMed:30254161). Interacts with ATG9
CC (PubMed:29848619). {ECO:0000269|PubMed:17295840,
CC ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:22851171,
CC ECO:0000269|PubMed:23230146, ECO:0000269|PubMed:29848619,
CC ECO:0000269|PubMed:30254161}.
CC -!- INTERACTION:
CC P53855; P43601: ATG18; NbExp=5; IntAct=EBI-29212, EBI-22968;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:11382761, ECO:0000269|PubMed:14723849,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18586673,
CC ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:20444982,
CC ECO:0000269|PubMed:22728243}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11382761, ECO:0000269|PubMed:14723849,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18586673,
CC ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:20444982,
CC ECO:0000269|PubMed:22728243, ECO:0000269|PubMed:30254161}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:23549786,
CC ECO:0000269|PubMed:23904270}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23549786, ECO:0000269|PubMed:23904270}.
CC Note=Localizes to the IM-ERES contact site.
CC {ECO:0000269|PubMed:23549786, ECO:0000269|PubMed:23904270}.
CC -!- DOMAIN: The N-terminal region (NR) associates with the endoplasmic
CC reticulum (ER) and is responsible for the formation of the isolation
CC membrane at the PAS. {ECO:0000269|PubMed:30254161}.
CC -!- DOMAIN: The amphipathic helix in the C-terminal region binds to
CC membranes and facilitates ATG18 binding to PtdIns3P to target the ATG2-
CC ATG18 complex to the PAS. {ECO:0000269|PubMed:30254161}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of autophagosomes
CC (PubMed:28704456). Completely blocks the movement of the ER-staining
CC dye R18 from the ER to IM precursors (PubMed:28704456).
CC {ECO:0000269|PubMed:28704456}.
CC -!- MISCELLANEOUS: Present with 876 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR EMBL; Z69381; CAA93356.1; -; Genomic_DNA.
DR EMBL; Z71518; CAA96147.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10317.1; -; Genomic_DNA.
DR PIR; S63208; S63208.
DR RefSeq; NP_014157.1; NM_001183080.1.
DR AlphaFoldDB; P53855; -.
DR BioGRID; 35597; 188.
DR ComplexPortal; CPX-361; ATG2-ATG18 complex.
DR DIP; DIP-2620N; -.
DR IntAct; P53855; 5.
DR MINT; P53855; -.
DR STRING; 4932.YNL242W; -.
DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; P53855; -.
DR MaxQB; P53855; -.
DR PaxDb; P53855; -.
DR PRIDE; P53855; -.
DR EnsemblFungi; YNL242W_mRNA; YNL242W; YNL242W.
DR GeneID; 855479; -.
DR KEGG; sce:YNL242W; -.
DR SGD; S000005186; ATG2.
DR VEuPathDB; FungiDB:YNL242W; -.
DR eggNOG; KOG2993; Eukaryota.
DR GeneTree; ENSGT00620000087966; -.
DR HOGENOM; CLU_000626_3_0_1; -.
DR InParanoid; P53855; -.
DR OMA; YDWKYTR; -.
DR BioCyc; YEAST:G3O-33239-MON; -.
DR PRO; PR:P53855; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53855; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IDA:UniProtKB.
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; IDA:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IDA:ComplexPortal.
DR GO; GO:0120013; F:lipid transfer activity; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0030242; P:autophagy of peroxisome; 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:0016236; P:macroautophagy; IDA:ComplexPortal.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR026885; ATG2_CAD_motif.
DR InterPro; IPR026886; ATG2_fungi/plants.
DR InterPro; IPR015412; Autophagy-rel_C.
DR PANTHER; PTHR13190; PTHR13190; 2.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
DR Pfam; PF13329; ATG2_CAD; 1.
DR Pfam; PF09333; ATG_C; 1.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Endoplasmic reticulum; Lipid transport; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1592
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000215836"
FT REGION 2..21
FT /note="ER-targeting domain"
FT /evidence="ECO:0000305|PubMed:30254161"
FT REGION 264..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1373
FT /note="PAS-targeting domain"
FT /evidence="ECO:0000305|PubMed:30254161"
FT COILED 1049..1075
FT /evidence="ECO:0000255"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 249
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 1086
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 83
FT /note="G->E: Leads to a severely reduced activity of
FT autophagy and a dispersed localization in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:11382761"
FT MUTAGEN 249
FT /note="S->A: Does not affect autophagy; when associated
FT with A-1086."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 249
FT /note="S->D: Phospho-mimetic mutant; does not affect
FT autophagy; when associated with D-1086."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 1086
FT /note="S->A: Does not affect autophagy; when associated
FT with A-249."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 1086
FT /note="S->D: Phospho-mimetic mutant; does not affect
FT autophagy; when associated with D-249."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 1352..1355
FT /note="FMAI->WMAW: Does not affect autophagy."
FT /evidence="ECO:0000269|PubMed:30254161"
FT MUTAGEN 1352..1355
FT /note="Missing: Impaired autophagy."
FT /evidence="ECO:0000269|PubMed:30254161"
SQ SEQUENCE 1592 AA; 178414 MW; 54FDDF56297FFF99 CRC64;
MAFWLPQNIQ KRLLLYVLQQ ISLFSNIDLS NLDVSIGSKS HFSFHDVNLS LDDLNIPNVQ
INEGIVDELV LKLTVSGGVE IDGSGLRFIM TPLYSSGSQE LHSDFLVKSI QDLTNSMLQF
SDPLTTYNRY KEDDISSSDS SSDLNSNIEA SKPAANGSYT LQNMRNKALN VALAKLKIAL
KDVTIRFIVN DRDPSDNIVE VHLESIQLIT TDANLRHINI ENITISSIQK QAVPDSPVHP
FNNDDLSQSV YLSKMEATSL YMSAMEEQSN EDPSEPQVTQ EEQENDKCKE SLMEINNLNI
AFKGLSSVND LRMSNIVIDI QDVHLAIHKI VEIKNSTLKN IIDIIVTHLD ANESFSCQDS
QSPSPDKQEP SALSSVDIKC IYLNLGQDIT VILKSFKLEQ KENNSLAFSL GSFYSNSSPL
TISHKTKPLL TGEQTPQSIA LNMGDELDII ISHDGIAHFF KIFQFVSKCM SFYQNKSKGM
MPQIASDTKR TVQLTSKAVK LSLKFPYFLL CFQVSPFIYD SNRELYIELV DVFKKLPSRC
TKILTMSSIT ISNLQSPLQL GSYDDTLKEA LIYSSVHAII KEVIFNEEYS GIVQLVEDIS
AFGKLFTDSK NSECTGKSKS KRGSFLQRSV RVLNSSRFVY KQSLSANFSL KIDSMKLKVS
EIIGPQFGSV EALLSNNFFA ITDDSQIVYF TKNLKVERKT PSLLEPQEIM SVVLNKAVNE
PVLYVHRRAN GKLKVIFNNI RIHYYARWLE ILKKNIGPDN ASSKDEPVSQ KLSKKQPTSG
FPWELKCLDC SLILHPFRLK SVMVIVLDNL TTGGSSFIPQ AKLLSKANTL FLIDDYQNFK
IQKDKNWPSL INFYAGQGFS AIGKIDTLNF LINKSDGALL LDCKIEQVGL SLCADSFQTF
CQLCIDLKYP QTFPDEEKFR TQLKNPIDVF KDIDCDLFNS AFIRENNHQN DYDSVHLVDS
FLDKTHEFNN GARSKLSSQG SYEMDSSSGT ATGGILLPHE SYLDSAQPKE EDTPPIASKE
QERDVDIRGS IDVEKVVIKL FDGYDWKYTR KFIANTVEKL DKELSKAEAS SSKSNVPQSE
ANIFDSIYIS ANKNNVTDLR RNLDGEIQGV QNSFSDVSKV NLRPSKHYKA LIQLNKVHVN
LKNYRVDEPD ESNSDNSTDV LNRCVVSIYE FEIIDNVPTS TWNKFVTLLK HEPWPHSSPM
FLLDLEFIRP IDFLQAVELV MQLNVAPLRL HVDQDTLEFL IRFLGFKDKR FELIDEYPDI
VFIQKFSTNS IKLRLDYKPK KVDYAGLRSG QTSELMNFFT LDGSKIILKS VVLYGLNGFD
ELNNKLKAIW TPDITKKQLP GVLEGLAPVR SFMAIGSGVK TLVTVLMSEY RQEGHLGRSL
KKGGNVFLKT TTGDFVKLGV KLTSGTQAIL ENTEELFGGV GSNGRVYDAS KFGSADGADS
DTAAVLDLDT LFEEDQLVGS KYSRIRDHEP TAVVIDMSSP GDHNEPTIVS LYADQPLDLP
TGLKEAYSSL EKHMHIAYDA VWRAKGQMKD DKRGGPSAAA VYVARAAPVA IIRPLIGATE
AVSKTLQGIA NQVDKTHNEQ INDKYKSNRT DS
