ATG21_YEAS7
ID ATG21_YEAS7 Reviewed; 496 AA.
AC A6ZWF0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Autophagy-related protein 21;
GN Name=ATG21; ORFNames=SCY_5627;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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. Essential for maturation of proaminopeptidase I (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Vacuole membrane
CC {ECO:0000250}. Note=And perivacuolar punctate structures.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC to phosphatidylinositol 3,5-bisphosphate (PIP2).
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; AAFW02000135; EDN61042.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZWF0; -.
DR SMR; A6ZWF0; -.
DR EnsemblFungi; EDN61042; EDN61042; SCY_5627.
DR HOGENOM; CLU_025895_5_2_1; -.
DR Proteomes; UP000007060; 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; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Membrane; Phosphoprotein; Protein transport; Repeat;
KW Transport; Vacuole; WD repeat.
FT CHAIN 1..496
FT /note="Autophagy-related protein 21"
FT /id="PRO_0000318013"
FT REPEAT 1..35
FT /note="WD 1"
FT REPEAT 148..190
FT /note="WD 2"
FT REPEAT 294..334
FT /note="WD 3"
FT REPEAT 346..385
FT /note="WD 4"
FT REPEAT 448..488
FT /note="WD 5"
FT REGION 41..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 342..346
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q02887"
FT COMPBIAS 43..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02887"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02887"
SQ SEQUENCE 496 AA; 55138 MW; 4EB31964F6437CEB CRC64;
MKVLQFNQDA TCCVVAASSH QISIFNCDPF GKCFEIDTKN SKKKTSNNNG TASNSESRNN
EESILITNGS RDRTDAEEEE DNEDNALVTG NILKEGEFVI EMLFSTSLIA IADRGQGLNK
GKKLKIVNTK RKSTICEIVF PHEIVDVVMN RKRMCVLLES DQIFIYDISC MKPLETIDLW
EDHYKRSQAN SFSNASNTGT LEGDSANLNR VATNLLANAT QKSVNGSNPS VRTRRNSLRS
KIRPRMVLSN DDRSILCFTA YSSPKKNKPN SEALYDVVIY DTLNVTPVNY LNSVHKGNVA
CLAVSHDGKL LATASDKGTI IRVFHTGVDS DYMSSRSLFK EFRRGTRLCN LYQLAFDKSM
TMIGCVGDTD TIHLFKLDDA SNSLPGDNSS NGHWNEEEDI LASNSNPSMG TPKEIPLSKP
RIANYFSKKI KSSIPNQNLS RNFAYITVNE SNRSCLGFPD EFPNQVYIAS DDGTFSIYSI
PSKPGECVLT KNNKFT