ATG20_YEAS7
ID ATG20_YEAS7 Reviewed; 640 AA.
AC A6ZXL6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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; ORFNames=SCY_0804;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with SNX4 and ATG17. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AAFW02000145; EDN60246.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZXL6; -.
DR SMR; A6ZXL6; -.
DR PRIDE; A6ZXL6; -.
DR EnsemblFungi; EDN60246; EDN60246; SCY_0804.
DR HOGENOM; CLU_014456_2_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:UniProt.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; -; 2.
DR Gene3D; 3.30.1520.10; -; 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 Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Acetylation; Autophagy; Coiled coil; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q07528"
FT CHAIN 2..640
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000317993"
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 135..155
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 135..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:0000250|UniProtKB:Q07528"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07528"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07528"
SQ SEQUENCE 640 AA; 72533 MW; 1261A3AE1607FEDA CRC64;
MSDLNDVQEN AKLNSETRNT GKAEPPHGTT EYVAEAEISK NGVGSPKKSP KKGKVGKGDN
NKVETELVHT ALLEKDNPFM EEGPTGFTKS ALLEIPGMRS HKLKNPNEDY EDDSEGLLPL
NQESNAETCR TSLSGSINSM NGETSASEEP SVSNRKKSAR IHILEAKRVS EGQGRAYIAY
VIQFENSTVQ RRYSDFESLR SILIRLFPMT LIPPIPEKQS IKNYGKSITG SSSKYLLPSE
GSGSVDLSLS VIHASVNNSD EKLIRHRIRM LTEFLNKLLT NEEITKTSII TDFLDPNNHN
WHEFVNSSST FSSLPKSILQ CNPLDPTNTT RIHAMLPIPG SSSQLLLNKE SSDKKMDKER
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
