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ATG21_KLULA
ID   ATG21_KLULA             Reviewed;         392 AA.
AC   Q6CLZ2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21; OrderedLocusNames=KLLA0E24354g;
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) 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; CR382125; CAH00134.1; -; Genomic_DNA.
DR   RefSeq; XP_455047.1; XM_455047.1.
DR   PDB; 6RGO; X-ray; 3.70 A; A/B=1-392.
DR   PDBsum; 6RGO; -.
DR   AlphaFoldDB; Q6CLZ2; -.
DR   SMR; Q6CLZ2; -.
DR   STRING; 28985.XP_455047.1; -.
DR   EnsemblFungi; CAH00134; CAH00134; KLLA0_E24333g.
DR   GeneID; 2894332; -.
DR   KEGG; kla:KLLA0_E24333g; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q6CLZ2; -.
DR   OMA; MNRKRMC; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-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:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006497; P:protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
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; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Cytoplasm; Membrane; Protein transport;
KW   Reference proteome; Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..392
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050879"
FT   REPEAT          200..240
FT                   /note="WD 1"
FT   REPEAT          250..289
FT                   /note="WD 2"
FT   MOTIF           246..250
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
SQ   SEQUENCE   392 AA;  43555 MW;  87E70690D13D0EEC CRC64;
     MALKLLGFNQ DATCFSVISS NKGVTIYNCD PFGKCFELEK STSNDEELDF LVEMLFSTSL
     IAVVDKTIGA SKRKKLKIVN TKRKATICEL TFPHEIMDVI MNRKIICVVL KSDQIFVYDI
     SCMKLLRTID VRGEKLKSTS KFRNSEAVGD IGVRVSLSTD NNSILCYSSY SKSDKENAPL
     NDIVVFDALK CIQINVLPAV HQSNIVCIAC SPDGMLMATA SEKGTIIRVF KTIDTENDEP
     ILVNEFRRGS RPSRISEMKF NHDNTLLACV GESDTIHIFA LPVTTTEADA NEDDTLQQSS
     HSLSSSINGL QYISKGLANR FGKIIVSKIP TQSQQRHVAY IKIPENAKYR IGFPKDTTNT
     IHICGEDGNY LVYSIPRNEV GPCTLVKSNT FD
 
 
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