ID   ATG21_VANPO             Reviewed;         422 AA.
AC   A7TTC8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21; ORFNames=Kpol_242p8;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480559; EDO14485.1; -; Genomic_DNA.
DR   RefSeq; XP_001642343.1; XM_001642293.1.
DR   AlphaFoldDB; A7TTC8; -.
DR   SMR; A7TTC8; -.
DR   STRING; 436907.A7TTC8; -.
DR   EnsemblFungi; EDO14485; EDO14485; Kpol_242p8.
DR   GeneID; 5542483; -.
DR   KEGG; vpo:Kpol_242p8; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; A7TTC8; -.
DR   OMA; MNRKRMC; -.
DR   OrthoDB; 1216824at2759; -.
DR   PhylomeDB; A7TTC8; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..422
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000318012"
FT   REPEAT          1..35
FT                   /note="WD 1"
FT   REPEAT          102..153
FT                   /note="WD 2"
FT   REPEAT          166..206
FT                   /note="WD 3"
FT   REPEAT          228..268
FT                   /note="WD 4"
FT   REPEAT          280..319
FT                   /note="WD 5"
FT   REPEAT          374..414
FT                   /note="WD 6"
FT   MOTIF           276..280
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
SQ   SEQUENCE   422 AA;  46848 MW;  1C73A277633BB814 CRC64;
     MGLSRFNQDA TCFVTSSEGN SVTIYNCDPF GKCFEMVDED TQNIGDDDAR GDDNSGGDDD
     LLVEMLFSTN LVAIVHRKQG ILKSKKLKIV NIKRKTIICE LSFPHPIQDV VMNRKRVCVL
     LNSDQIHIYD ISCMKHLHTI DIWDSQVKSI TGQGVDSLSN SGTSNMTSLR ERSSTFSKSI
     SPKICLSNDD RSILAFNCYS TSSKSVILND VVIFDALNIS PLNYINSVHK GNVASLAISP
     DGKFIATASE KGTLVRIFNT GAETESELLT PLLYEFRRGN RPCNINQLTF NSDSTLLGCV
     GDSDTIHIFK LDSTSRLLSM SVNSEDNSHI TSEDIKALRK DPNSKQFTKL ISKTIKKSIP
     SQALRRDFAH ITIKNTKTKH ILGFPKEFMN QVYVLSNDGS FFIYSLPSTS GSCVLSKQND
     FK