ATG20_VANPO
ID ATG20_VANPO Reviewed; 667 AA.
AC A7TIP6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Autophagy-related protein 20;
GN Name=ATG20; ORFNames=Kpol_1043p28;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 (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}.
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DR EMBL; DS480397; EDO17838.1; -; Genomic_DNA.
DR RefSeq; XP_001645696.1; XM_001645646.1.
DR AlphaFoldDB; A7TIP6; -.
DR STRING; 436907.A7TIP6; -.
DR EnsemblFungi; EDO17838; EDO17838; Kpol_1043p28.
DR GeneID; 5546092; -.
DR KEGG; vpo:Kpol_1043p28; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_2_1_1; -.
DR InParanoid; A7TIP6; -.
DR OMA; ICNTDIT; -.
DR OrthoDB; 632390at2759; -.
DR PhylomeDB; A7TIP6; -.
DR Proteomes; UP000000267; 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; -; 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; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..667
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000317992"
FT DOMAIN 185..331
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..652
FT /evidence="ECO:0000255"
FT COMPBIAS 12..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 222
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 224
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 248
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 297
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 667 AA; 74885 MW; 46EAABE7704036A5 CRC64;
MKQKKNRFGS GKRITDQSSV DGDLIAPGNS SMDKRRNSSS SRSSSTQESK ELTESLASVH
TSDMHQSNIH ERIDGDDNPF LDQDDESFKS TRANTSATKL TDVVNPNAEY KDNDSDNDEE
ILTATAPDTS ITEGIVSTEA DGGNDVVTAS VEDKEGTVTD TAVGLDNANN TVDQKVKESI
IPDIKLINDR VQILEANKVS EGQGRAYVAY TIKWGDQSVR RRYSDFESLR SVLMKLFPTS
LLPPIPEKQT LKNYSKSIAG SKSNYLLPSE GTGSVDLVLS VINGTVTNND EKLIRHRIRM
LTSFLNKLLQ DEEILKTPII YDFLDPNNIN WNDFINSSAT FSMLPKSVLQ CNPLDPTNTT
RIHACLPVPS TSHILPSKEK VSDTKTIERK DGFDIIEQEH KQYESLLKSG FYKHNTQITK
SLYGMQHDMK DLSDTFAHFA SAQACEAELA EQLTYMSNAY DDAASNLEAL VGLLYYNINE
PLGESVRMAG SAKELIKYRK LKGVQLEILI NSLESKRQQL HKLELQRGVQ PRNGNTASGA
SGNDESSVKK PQASKSQSSS YGGKFLNRFN KIAAMVKETI NYQEQDPQTT MANLIKEIEQ
LNESEQVARH DLEDISKIIK EDRLTKFSEE REKELNEILR NYSKYLKDYA KKNLELWKEI
KTRQEQL
