ATG20_CANGA
ID ATG20_CANGA Reviewed; 753 AA.
AC Q6FR93;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Autophagy-related protein 20;
GN Name=ATG20; OrderedLocusNames=CAGL0H10428g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG60184.1; -; Genomic_DNA.
DR RefSeq; XP_447251.1; XM_447251.1.
DR AlphaFoldDB; Q6FR93; -.
DR STRING; 5478.XP_447251.1; -.
DR PRIDE; Q6FR93; -.
DR EnsemblFungi; CAG60184; CAG60184; CAGL0H10428g.
DR GeneID; 2888784; -.
DR KEGG; cgr:CAGL0H10428g; -.
DR CGD; CAL0130256; CAGL0H10428g.
DR VEuPathDB; FungiDB:CAGL0H10428g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_2_1_1; -.
DR InParanoid; Q6FR93; -.
DR OMA; CRRMKEV; -.
DR Proteomes; UP000002428; Chromosome H.
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; 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..753
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000213821"
FT DOMAIN 283..429
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319
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 321
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 345
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 395
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 753 AA; 84641 MW; B68985FA37415151 CRC64;
MGRSKRSKKK SLAHLQSDGK DKLSSEENIS RGSEVEESPE NFEEAQDYGD SLKDTDEQSD
SITAIRSVTG GTASTITDLN NKFKSQELVD NEKVEINTKS TEEVGCKPST DHSTEALDEG
HDTGISSTNK DDSDVRIIGD DNEDSEAIES VDIKGKVSSG ISDADVLKPQ EELVHTAILE
NDNPFYDANK EISGSKKLDE KVNSVDSMAE TTKVNSGDSK QRMGDLVVRR SENLHNPNLD
YEEEDEILVS NTDTNKHSKE SSSALNNANM KSFGNAVKSY TKKSGKHVRI LEAKKVSEGQ
SRTFVAYFIK YNGHMVRRRY SDFESLRSIL VKLFPLMVIP PIPEKEGLKS YSKAIAGLKH
AKYILPSEQT DSVDLSLSII DQSVSDKEEN IIRHRVRILT KFLNRLLDNT DISSTSLIED
FLNPNNSNWN DFVTSSATFS MLPRNRLQAN PVDPTNTTRV HACLPIPNTS VALGKRDPEL
FVSGNENDDT DGYILLEKEH KRYESIVNNT YKYNRRITKN FNEMKHDYDD LAAAFAELSN
LDISSNPKHV DFCATFDKSS IAMQALVSNL YYNIDEPLNE AIYNTNAVTE LLMFRKLKAV
QLYKVEKSLV GKVHELQKLE KGENKIESEP NQESLTSARR LSPIPAPQKL GGSFFNKISE
IANKVKESVS YQELDVETQI SNLRKEIERL KETSAVTTKD MEVINDTICK EEVPKALKCG
EKELEDILAS YASYMKTYAK QNLEYWKSIQ EAR
