ATG21_CANGA
ID ATG21_CANGA Reviewed; 453 AA.
AC Q6FRU4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Autophagy-related protein 21;
GN Name=ATG21; OrderedLocusNames=CAGL0H05841g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380954; CAG59983.1; -; Genomic_DNA.
DR RefSeq; XP_447050.1; XM_447050.1.
DR AlphaFoldDB; Q6FRU4; -.
DR SMR; Q6FRU4; -.
DR STRING; 5478.XP_447050.1; -.
DR EnsemblFungi; CAG59983; CAG59983; CAGL0H05841g.
DR GeneID; 2888594; -.
DR KEGG; cgr:CAGL0H05841g; -.
DR CGD; CAL0131660; CAGL0H05841g.
DR VEuPathDB; FungiDB:CAGL0H05841g; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; Q6FRU4; -.
DR OMA; MNRKRMC; -.
DR Proteomes; UP000002428; Chromosome H.
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; IPR036322; WD40_repeat_dom_sf.
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..453
FT /note="Autophagy-related protein 21"
FT /id="PRO_0000050877"
FT REPEAT 4..137
FT /note="WD 1"
FT REPEAT 252..347
FT /note="WD 2"
FT REPEAT 419..453
FT /note="WD 3"
FT REGION 177..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..314
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q02887"
FT COMPBIAS 187..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50374 MW; 5131FED90AD550E9 CRC64;
MKVLRFNQDA SCCVVNSGAN ELTVYNCDPF GKCFEFNISN VNGDSNDNGI GYDSLEAGSS
SIESQVIAEM LFSTSLLAVV DKGQGINTGK KLKIVNIKKR SLICEIAFPS LIVDVVMNRK
RICVLLDNDQ IFIYDISCMK LMETLDLWES NNEGNLNDHI KVGERASNMI NENLKNGNEL
DRIRSKSNNN NDQTNSDNGR SRTYSINGSH KIKPQLTLSG NDNSILCYSK YSSSKQNPAR
ILNDIVVYDA LNLKPINYLN SVHKGCVLKT SVSIDGKLLA TASEKGTIIR IHKTGVDSDF
ASGPLLYKEF RRGSRPSHIH QLLFNKDSTL LVCVGDSDTI HIFRTDDDGL ALDGIDGDIG
SDSGGSLELI KNRIPHEQVK KFFSRKIKSH IPNQNLHRDF AHINMDRIVH TVVGFPEEFD
NKIYVASDDG SFKTYTIPSK HGQCVLNKTS HFI
