ID   ATG21_ASHGO             Reviewed;         409 AA.
AC   Q75D34;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21; OrderedLocusNames=ABR189W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 198-201.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50961.2; -; Genomic_DNA.
DR   RefSeq; NP_983137.2; NM_208490.2.
DR   AlphaFoldDB; Q75D34; -.
DR   SMR; Q75D34; -.
DR   STRING; 33169.AAS50961; -.
DR   EnsemblFungi; AAS50961; AAS50961; AGOS_ABR189W.
DR   GeneID; 4619247; -.
DR   KEGG; ago:AGOS_ABR189W; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q75D34; -.
DR   OMA; MNRKRMC; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0016050; P:vesicle organization; IEA:EnsemblFungi.
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; 3.
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..409
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050875"
FT   REPEAT          1..35
FT                   /note="WD 1"
FT   REPEAT          221..261
FT                   /note="WD 2"
FT   REPEAT          273..312
FT                   /note="WD 3"
FT   REPEAT          361..402
FT                   /note="WD 4"
FT   MOTIF           269..273
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
SQ   SEQUENCE   409 AA;  46000 MW;  8A635B20FCD7F3F6 CRC64;
     MKVLRFNQDA SCFSAVSRPH SMTIYNCDPF GKCFELENSV VTSESCDTEC LTKAQGDQCS
     NFVTEMLFAT SLIAVVNRDQ GLQKARKLRI VNTKRKTTIC ELTFPHEVVD IVMNRKRMCV
     LLSSDQIFIY DISCMKLLQT ISVLEDKLKM AVSDQGHVST SVVGRQLQGE TSMVRIALCS
     DDKSILCYTA YCRTNKNSYI LNDLVVYDAL NMTPLNYLNT VHKGNVACLC ISNDGKMVAT
     ASDKGTIVRI FSTGDENTLQ SGNTLLHEFR RGTRPCSIYE MKIDPTRRYL ACVGHTDTIH
     IFDLERQGQQ NKSLSDSQST ALLREGKLSK ESTLQFASFL SKKVISKIPN QNMERHFAHI
     KVDDSVRHCL GFPDEFSDRV YVASNNGEFQ VWNIPQSGGE CILVKKSKF