ID   ATG20_CANAL             Reviewed;         731 AA.
AC   Q59TN9; A0A1D8PLW6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Autophagy-related protein 20;
GN   Name=ATG20; OrderedLocusNames=CAALFM_C403810WA;
GN   ORFNames=CaO19.1297, CaO19.8877;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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 to the perivacuolar
CC       punctate structures. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; CP017626; AOW29134.1; -; Genomic_DNA.
DR   RefSeq; XP_709938.2; XM_704846.2.
DR   AlphaFoldDB; Q59TN9; -.
DR   STRING; 237561.Q59TN9; -.
DR   PRIDE; Q59TN9; -.
DR   GeneID; 3645350; -.
DR   KEGG; cal:CAALFM_C403810WA; -.
DR   CGD; CAL0000183168; orf19.12503.
DR   VEuPathDB; FungiDB:C4_03810W_A; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_748017_0_0_1; -.
DR   InParanoid; Q59TN9; -.
DR   OMA; CRRMKEV; -.
DR   OrthoDB; 632390at2759; -.
DR   PRO; PR:Q59TN9; -.
DR   Proteomes; UP000000559; Chromosome 4.
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   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   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..731
FT                   /note="Autophagy-related protein 20"
FT                   /id="PRO_0000213820"
FT   DOMAIN          164..340
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   BINDING         207
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         231
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         306
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   731 AA;  81256 MW;  5C441552D93D9866 CRC64;
     MSSVLRNQDN PPTISEVSST TKENTDNSNS KQEEKEKEKE ISSTIENPTF VDDEEDNNPF
     SHHGEGLTSF MTANSFNEGP NTKSDKRTTK ENNNSSSNNN RGDNNDDDDD DSLLLYNTSN
     NNKSNNVSRV NPMLKSTGEV FKTVNMNFES RVTKLLKPNT KIRIQITEAG NSNEGMSNSS
     KKYTVYTIKL INLEDPNNDI LTRRRYSDFE SLRDVLTKIF PLIVIPPIPP KNYFDFSMLN
     GLVGSNHENS SLSVAGSNGN SGGSGGGGAS GGAGSGSGNG SIITSPKTYS YINSTHLTKG
     KLIEHRKRLL TNFLNNCLEI KQIRSLEFFA KFLDPNANWG DEIALIQSQL PKSIYLSNPE
     NGLKTDPIYS NLPNPSNKNT ISFFKDNKKK LTKKTNKLLS NGSENHDIGV GGGGGSIGNG
     GNGVNGNGTN SQSQYIANTS MLDDINKRIM ENYIGLSNDY SKLGSTFNSF SLILAETTTT
     TTTGVSSATK KSNDNELNLI FDKIGQVFDR SYITINSLIG ELETKFSEPL GEIVQYTSII
     HYVAKYQSKK IKQKSMLDNE IKDKRKTLED LLKIERESNR IENAINSQVK PKNGKYNLEQ
     QQSSTVSPAP PPGPPPSSSS SSSSSSKFKF PSFKKITQYV SEIIDQNPEV TRKQKITNLQ
     EKIQILEKCQ NIMLADLSFI TDEVNKNIQS FQKRQLKMIY KILLLYNKQL IGWAKKNIDI
     WEEVRDEIAK M