ID ATG20_YEAST Reviewed; 640 AA. AC Q07528; D6VRN7; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Autophagy-related protein 20; DE AltName: Full=Cytoplasm to vacuole targeting protein 20; DE AltName: Full=Sorting nexin-42; GN Name=ATG20; Synonyms=CVT20, SNX42; OrderedLocusNames=YDL113C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] 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 [3] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG17 AND SNX4, AND RP MUTAGENESIS OF TYR-193. RX PubMed=12048214; DOI=10.1074/jbc.m204736200; RA Nice D.C. III, Sato T.K., Stromhaug P.E., Emr S.D., Klionsky D.J.; RT "Cooperative binding of the cytoplasm to vacuole targeting pathway RT proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre- RT autophagosomal structure is required for selective autophagy."; RL J. Biol. Chem. 277:30198-30207(2002). RN [4] 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 [5] RP FUNCTION, AND INTERACTION WITH SNX4. RX PubMed=12554655; DOI=10.1093/emboj/cdg062; RA Hettema E.H., Lewis M.J., Black M.W., Pelham H.R.B.; RT "Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval RT pathways from yeast endosomes."; RL EMBO J. 22:548-557(2003). RN [6] 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 [7] 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 [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ATG11. RX PubMed=15659643; DOI=10.1091/mbc.e04-11-1035; RA Yorimitsu T., Klionsky D.J.; RT "Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to RT vacuole targeting pathway."; RL Mol. Biol. Cell 16:1593-1605(2005). RN [9] RP FUNCTION. RX PubMed=15901835; DOI=10.1091/mbc.e04-10-0894; RA Cheong H., Yorimitsu T., Reggiori F., Legakis J.E., Wang C.W., RA Klionsky D.J.; RT "Atg17 regulates the magnitude of the autophagic response."; RL Mol. Biol. Cell 16:3438-3453(2005). RN [10] RP FUNCTION. RX PubMed=16138904; DOI=10.1111/j.1600-0854.2005.00327.x; RA Berger A.C., Hanson P.K., Wylie Nichols J., Corbett A.H.; RT "A yeast model system for functional analysis of the Niemann-Pick type C RT protein 1 homolog, Ncr1p."; RL Traffic 6:907-917(2005). RN [11] RP FUNCTION. RX PubMed=17132049; DOI=10.1371/journal.pbio.0040423; RA Bernales S., McDonald K.L., Walter P.; RT "Autophagy counterbalances endoplasmic reticulum expansion during the RT unfolded protein response."; RL PLoS Biol. 4:E423-E423(2006). RN [12] 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 [13] RP FUNCTION. RX PubMed=19793921; DOI=10.1091/mbc.e09-03-0225; RA Kanki T., Wang K., Baba M., Bartholomew C.R., Lynch-Day M.A., Du Z., RA Geng J., Mao K., Yang Z., Yen W.L., Klionsky D.J.; RT "A genomic screen for yeast mutants defective in selective mitochondria RT autophagy."; RL Mol. Biol. Cell 20:4730-4738(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-363, AND RP IDENTIFICATION BY 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 [15] RP FUNCTION. RX PubMed=20861302; DOI=10.1091/mbc.e10-05-0457; RA Ohashi Y., Munro S.; RT "Membrane delivery to the yeast autophagosome from the Golgi-endosomal RT system."; RL Mol. Biol. Cell 21:3998-4008(2010). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt), pexophagy CC and mitophagy. Also involved in endoplasmic reticulum-specific CC autophagic process and is essential for the survival of cells subjected CC to severe ER stress. Functions in protein retrieval from the endocytic CC pathway. Required for proper sorting of the v-SNARE protein SNC1. CC {ECO:0000269|PubMed:12048214, ECO:0000269|PubMed:12554655, CC ECO:0000269|PubMed:15901835, ECO:0000269|PubMed:16138904, CC ECO:0000269|PubMed:17132049, ECO:0000269|PubMed:19793921, CC ECO:0000269|PubMed:20861302}. CC -!- SUBUNIT: Forms a complex with SNX4 and ATG17. CC -!- INTERACTION: CC Q07528; P47057: SNX4; NbExp=7; IntAct=EBI-36894, EBI-17610; CC Q07528; P53039: YIP1; NbExp=2; IntAct=EBI-36894, EBI-25295; CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein. CC Preautophagosomal structure membrane; Peripheral membrane protein. CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is CC necessary for peripheral membrane localization of ATG20 to the CC perivacuolar punctate structures. CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the sorting nexin 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; Z74161; CAA98681.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11747.1; -; Genomic_DNA. DR PIR; S67656; S67656. DR RefSeq; NP_010170.1; NM_001180172.1. DR AlphaFoldDB; Q07528; -. DR SMR; Q07528; -. DR BioGRID; 31949; 119. DR ComplexPortal; CPX-1377; SNX4-ATG20 sorting nexin complex. DR DIP; DIP-1593N; -. DR IntAct; Q07528; 13. DR MINT; Q07528; -. DR STRING; 4932.YDL113C; -. DR iPTMnet; Q07528; -. DR MaxQB; Q07528; -. DR PaxDb; 4932-YDL113C; -. DR PeptideAtlas; Q07528; -. DR EnsemblFungi; YDL113C_mRNA; YDL113C; YDL113C. DR GeneID; 851445; -. DR KEGG; sce:YDL113C; -. DR AGR; SGD:S000002271; -. DR SGD; S000002271; ATG20. DR VEuPathDB; FungiDB:YDL113C; -. DR eggNOG; KOG2273; Eukaryota. DR HOGENOM; CLU_014456_2_1_1; -. DR InParanoid; Q07528; -. DR OMA; ICNTDIT; -. DR OrthoDB; 5475877at2759; -. DR BioCyc; YEAST:G3O-29513-MONOMER; -. DR BioGRID-ORCS; 851445; 3 hits in 10 CRISPR screens. DR PRO; PR:Q07528; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q07528; Protein. DR GO; GO:0010009; C:cytoplasmic side of endosome membrane; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005768; C:endosome; IDA:SGD. DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD. DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD. DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD. DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD. DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:SGD. DR GO; GO:0006886; P:intracellular protein transport; IDA:ComplexPortal. DR GO; GO:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:ComplexPortal. DR CDD; cd07629; BAR_Atg20p; 1. DR CDD; cd06867; PX_SNX41_42; 1. DR DisProt; DP01744; -. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR044106; PX_Snx41/Atg20. DR PANTHER; PTHR46979:SF1; AUTOPHAGY-RELATED PROTEIN 20; 1. DR PANTHER; PTHR46979; SORTING NEXIN-41; 1. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF64268; PX domain; 1. DR PROSITE; PS50195; PX; 1. PE 1: Evidence at protein level; KW Acetylation; Autophagy; Coiled coil; Endosome; Lipid-binding; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..640 FT /note="Autophagy-related protein 20" FT /id="PRO_0000213824" FT DOMAIN 140..301 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT REGION 1..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 126..156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 475..512 FT /evidence="ECO:0000255" FT COILED 562..593 FT /evidence="ECO:0000255" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..152 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 192 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250" FT BINDING 218 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250" FT BINDING 267 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MUTAGEN 193 FT /note="Y->A: Abolishes the intracellular punctate FT localization and decreases the cytoplasm to vacuole FT transport." FT /evidence="ECO:0000269|PubMed:12048214" SQ SEQUENCE 640 AA; 72546 MW; 160977A8BECB6D93 CRC64; MSDLNDVQEN AKLNSETRNT GKAEPPHGTT EYVAEAEISK NGVGSPKKSP KKGKVGKGDN NKVETELVHT ALLEKDNPFM EEGPTGFTKS ALLEIPGMRS HNLKNPNEDY EDDSEGLLPL NQESNAETCR TSLSGSINSM NGETSASEEP SVSNRKKSAR IHILEAKRVS EGQGRAYIAY VIQFENSTVQ RRYSDFESLR SILIRLFPMT LIPPIPEKQS IKNYGKSITG SSSKYLLPSE GSGSVDLSLS VIHASVNNSD EKLIRHRIRM LTEFLNKLLT NEEITKTSII TDFLDPNNHN WHEFVNSSST FSSLPKSILQ CNPLDPTNTT RIHAMLPIPG SSSQLLLNKE SNDKKMDKER SKSFTNIEQD YKQYENLLDN GIYKYNRRTT KTYHDLKSDY NEIGEVFAQF AHEQAQVGEL AEQLSYLSNA FSGSSISLEK LVGRLYYNIN EPLNESVHMA TSARELIKYR KLKYLQNEMI KKSLNSKRAQ LEKLEAQNNE YKDVDKIIDN EMSKSHTINL ERPNNNTGSG GKSYGGKLFN GFNKLASMVK DSVKYQETDP HTASINLKKE IEQLSESLEV TENDLEVISK VIKNDQLPKF SKEREVDLSE ILKHYSRYMR NYARQNLEIW KEVKRHQDFA //