ID   ATG21_DEBHA             Reviewed;         532 AA.
AC   Q6BIA1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21; OrderedLocusNames=DEHA2G12364g;
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) vesicles
CC       formation and mitophagy. Involved in binding of
CC       phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to
CC       the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated
CC       cleavage (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Vacuolar
CC       and perivacuolar punctate structures. {ECO:0000250}.
CC   -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC       to phosphatidylinositol 3,5-bisphosphate (PIP2). {ECO:0000250}.
CC   -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC       transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to
CC       the PAS in nutrient-rich medium and in both its recruitment to and
CC       dissociation from the PAS under starvation conditions.
CC       {ECO:0000250|UniProtKB:Q02887}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; CR382139; CAG90556.2; -; Genomic_DNA.
DR   RefSeq; XP_462070.2; XM_462070.1.
DR   AlphaFoldDB; Q6BIA1; -.
DR   SMR; Q6BIA1; -.
DR   STRING; 4959.XP_462070.2; -.
DR   EnsemblFungi; CAG90556; CAG90556; DEHA2G12364g.
DR   GeneID; 2904981; -.
DR   KEGG; dha:DEHA2G12364g; -.
DR   VEuPathDB; FungiDB:DEHA2G12364g; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q6BIA1; -.
DR   OMA; MNRKRMC; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..532
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050878"
FT   REPEAT          265..310
FT                   /note="WD 1"
FT   REPEAT          321..360
FT                   /note="WD 2"
FT   REGION          360..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           317..321
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
FT   COMPBIAS        364..378
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  60219 MW;  91CDE620C8214E45 CRC64;
     MVIINNLTFN QDYSCVSVST TKYHKIFNCD PFGEFYSSYQ GSSGTKGDKP NDNDKEIIID
     KGNGNEYNKI GEDSPTSYLK MLFSTSLTII IPQNESVGNR LLKIYNLKQN MKICELTFPS
     HIIDVKLNRK RLCVILESGQ IYIYDLSCVR LIKVLEISSF SSKDSEEETH QKLFVGDLGA
     EDKSLLVLPI SNITDQTDLF NTENGVNVTR ASDSNILTSL KPLIEFTENK IDKDIITLED
     LQKDSNGWVL IYDTIKLKPR LIYKAHDSSL AKITISNDNK KIATASSKGT IIRVCHLESS
     DDEDVSKPFN ISQIINLRRG HNIAKVNCLS FSLDNSILGC GSESNTIHFF RLSKQPHESF
     EYEEDPANES DPDDEDRSSE DLNQNLANLL ISKTPDASAP DQKDSAKSSY FGVLKKKVEG
     SSRFMNNPYT QTIVRNLPYK NYFENLIWEP PRRAFAYVKL PEYTPPQLFN LHQSKNKVAI
     GFANTNNNGH LIMLASYQTG QFYHYQLPKP SDQPEPSDSR HECNLIAQYS LL