ATG20_DEBHA
ID ATG20_DEBHA Reviewed; 625 AA.
AC Q6BZE1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Autophagy-related protein 20;
GN Name=ATG20; OrderedLocusNames=DEHA2A02046g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 to the perivacuolar
CC punctate structures. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CR382133; CAG84380.2; -; Genomic_DNA.
DR RefSeq; XP_456428.2; XM_456428.1.
DR AlphaFoldDB; Q6BZE1; -.
DR STRING; 4959.XP_456428.2; -.
DR PRIDE; Q6BZE1; -.
DR EnsemblFungi; CAG84380; CAG84380; DEHA2A02046g.
DR GeneID; 2899969; -.
DR KEGG; dha:DEHA2A02046g; -.
DR VEuPathDB; FungiDB:DEHA2A02046g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_025790_0_0_1; -.
DR InParanoid; Q6BZE1; -.
DR OMA; WIKECLK; -.
DR OrthoDB; 632390at2759; -.
DR Proteomes; UP000000599; Chromosome A.
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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; 3.30.1520.10; -; 1.
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 Autophagy; Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..625
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000213822"
FT DOMAIN 79..202
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
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 120
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 144
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 167
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 625 AA; 72009 MW; BCB5C09DEED10087 CRC64;
MNPNDNNLFG DIEQDNNPSF YGNQSFLRDP YGKSKQTCPP SVTSNGDPSI TNDDNNSAHN
NDLVSNSIVL SKKIEQMVND PNLQINVISS ERMINSSVVA YSIELSSFDD NRMIVKRRYS
EFKSLRDNLQ ILFPTLVIPP IPEKHTLFTY LINSIDNSKE LNIIETRKRC FANFLKDIIF
DSNVALKSCV LVHKFLDPNY ELCWNNAVNE PPVSLIPNNL LLANPVNPTD QNGLYSLLPI
VNGFELNSNI DNISSLHKLN EDLHKLNEQV HVFELRKEQN ERRHPSEPTT SLFTEIPISL
IDFEKNFHQN IKVLTELNKL NSRSVKNFKS IINTLIELGG NLNNFSLQIH ELNTDSNALS
SLIEKFGSTI DSNFLGYEAF LMNDIIPEWQ EPISQLVQYY LTSLQLIKFY KFKIIQYKLV
YKLKFNKYQE LANISTNFES QSKLKDLRNL DIDSPSINEA IKKIELNQKR LKNRKISSKK
SWYGLFGGNS KPTFNLREDL PASTIPSEGT GIRRERTPLV SDENMSYPVN PSANLENTNI
DINSHYKHKI NQIEKELTKL DQLIDLTNTD ISTLTQELNL NFNDFLVRVE KKWLVIMLEF
IKNGKQLFKD NLQNWNECKV FINDL
