ATG20_ASHGO
ID ATG20_ASHGO Reviewed; 577 AA.
AC Q75B65;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Autophagy-related protein 20;
GN Name=ATG20; OrderedLocusNames=ADL293W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {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. {ECO:0000250}.
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; AE016817; AAS51627.1; -; Genomic_DNA.
DR RefSeq; NP_983803.1; NM_209156.1.
DR AlphaFoldDB; Q75B65; -.
DR SMR; Q75B65; -.
DR STRING; 33169.AAS51627; -.
DR EnsemblFungi; AAS51627; AAS51627; AGOS_ADL293W.
DR GeneID; 4619938; -.
DR KEGG; ago:AGOS_ADL293W; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_0_0_1; -.
DR InParanoid; Q75B65; -.
DR OMA; CRRMKEV; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0010009; C:cytoplasmic side of endosome membrane; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0034498; P:early endosome to Golgi transport; IEA:EnsemblFungi.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; -; 1.
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; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..577
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000213819"
FT DOMAIN 95..239
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
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 133
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 157
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 205
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"
SQ SEQUENCE 577 AA; 63967 MW; 26F8BA003E0D93E8 CRC64;
MTEQSEHSNG GVCASSIQPA RNGGLCGHGG VGGVGEAEGD PVHTQIIQED NPFVEHGQSY
VAPHSGGGRT SSGSSSSASL QEGLLAPPLA KSSAGEQGRV RILEASKVSE GQGRSYITYT
ISYRDRVVRR RYSEFESLRK ILIKLFPMTL IPPIPEKQSL TSYGKSIAGS NANYVLPSEA
AGCDLAVSVI NGSVNLNDQK MIRHRIRMLT SFLNRLLQNE EVTKTSIIGD FLDPNNANWN
DVITTSATIS SLPKSVLQCN PLDPTNTTPA HASLPIPPLS SAPQLMGKDG VGTSTKPSAE
DMEFSRIEYE YKKYEQLLHT GVYKYNRRIT RTMHELKQDL ADLSEAFAEF AVEQSKGGDL
AELLSYLSNA NDEAAAVLDD LVGKIYYNIN EPLSEAVHIA GAARELIQYR RLKFAQRDML
KKSLLGKEGH LKRLQEQEDD AKAIDQLVDQ HLGEGTRINL QRPSEASPNT YKRKLFSRFN
KLANIVKETV TYQEQDPKVN IKTVQEDIEQ IKESLDVSAS DLDVITATIR DVQLPAFSRN
RDKELYDILK NYSKYMKEYA AKNLEIWKDL RKQEENA
