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