ATG20_KLULA
ID ATG20_KLULA Reviewed; 636 AA.
AC Q6CNX6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Autophagy-related protein 20;
GN Name=ATG20; OrderedLocusNames=KLLA0E09141g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99450.1; -; Genomic_DNA.
DR RefSeq; XP_454363.1; XM_454363.1.
DR AlphaFoldDB; Q6CNX6; -.
DR SMR; Q6CNX6; -.
DR STRING; 28985.XP_454363.1; -.
DR PRIDE; Q6CNX6; -.
DR EnsemblFungi; CAG99450; CAG99450; KLLA0_E09175g.
DR GeneID; 2894747; -.
DR KEGG; kla:KLLA0_E09175g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_2_1_1; -.
DR InParanoid; Q6CNX6; -.
DR OMA; CRRMKEV; -.
DR Proteomes; UP000000598; Chromosome E.
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..636
FT /note="Autophagy-related protein 20"
FT /id="PRO_0000213823"
FT DOMAIN 160..305
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..163
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 25..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196
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 198
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 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 271
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 636 AA; 72225 MW; ED55D1FA454016D6 CRC64;
MQINFEPMPN SVTHLENNSP SRLKNNKTVE EHKEHEPDLQ TQSEMRRESN GSPKDTAVTN
QNGDQPHENV IHTQIIKKDN PFFNYMQDNV DGSDENGKND DDDENAKNAG SDDNEDQLLQ
PNRRKNSKER RRSSVATSKD SSPDVPYNTL NHNASGMTKE GKKRAQILEA SKVSEGQGRT
YIAYAIKYGD SIVKRRYSDF ESLRKVLVKL FPISLIPPIP EKQSLKSYGK AMTYSKSSYL
LPTESGDSVD LSLSVINGPV TTNDEKLIRH RIRMLTSFLN RLLKNQEITK TSIVYDFLDP
NNKNWNDLIT SSLTISSLPK SVLQCNPIDP TNTTKAHSYL PVPSSSTQLL ASKDNHSASD
ADEFTKIEAE FKNYEQLIHS GLYKYSRATT KEVNYLREDL KGISSEFAQL STDETKNESG
LAELLSHSSD AYGTLQEILE TLVGNLHYNI NEPLSECAHM ATAVRDLIHY RRLKLIQKDI
LERTILYKRG QLIKFQQQEN DHKQIDNMVK EELGTNGAVN LENPAGPQSY SGKFINKFTQ
LAIIIKDSVS YQEQDPAAAA RSLEKELIQL DETLKVATSD LVVISETLKN TELPNFIKER
DEELTQIFKN YAKYMKENAT RNLEIWKELH NRIQEA
