ATG23_YEAS7
ID ATG23_YEAS7 Reviewed; 453 AA.
AC A7A1V1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Autophagy-related protein 23;
GN Name=ATG23; ORFNames=SCY_3979;
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) vesicle
CC formation and efficient autophagy. Plays a role in ATG protein
CC retrieval from the pre-autophagosomal structure (PAS) and is especially
CC required for autophagy-dependent cycling of ATG9. Also plays a role in
CC regulation of filamentous growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with ATG9 and ATG27. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=Found in pre-autophagosomal structure and other
CC punctate structures. Correct localization of ATG23 to the membranes is
CC strictly dependent of ATG9. Cycling through the pre-autophagosomal
CC structure and correct location to other punctate structures is
CC ATG1- and ATG13-dependent (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG23 family. {ECO:0000305}.
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DR EMBL; AAFW02000171; EDN59329.1; -; Genomic_DNA.
DR AlphaFoldDB; A7A1V1; -.
DR SMR; A7A1V1; -.
DR PRIDE; A7A1V1; -.
DR EnsemblFungi; EDN59329; EDN59329; SCY_3979.
DR HOGENOM; CLU_051067_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Membrane; Protein transport; Transport.
FT CHAIN 1..453
FT /note="Autophagy-related protein 23"
FT /id="PRO_0000318038"
FT REGION 380..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..213
FT /evidence="ECO:0000255"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 51537 MW; F735C92A9A337380 CRC64;
MELNQVLEKK EQILQYLGTL VGLHEKALSD VNSASQVTSI RKDITICLND LCRINDLLVS
HDGLLKREIG SLLRDKQELL ELNEREQLLW KERKSWHIEQ ETDAAPADYV IDKDAIITIS
SHHRTSLNKY IESVGAENTI LSNTDDSDAM IEEVQNAESS ADQMIRNYKL LQLSHKQAKS
EIIRLETLLR DFKKDNKFIE EELKRQSGRI RSEMGNIDFH LSKIEESKHQ LMKRIGFESP
LTQEKSLSEK IFNLRLSSAD EDYNERQTIN MKNFVHMKDL IELKIEDLQE QLTRNKNESS
TVLTQRELWL DCQKKVGDLE SKLITKLRSS SNSKIPPNEM SEMINSTIQY LNNLLDSSDE
KLTTTLISNE RDVLSKACEE LHSESTTPQD GSSALPSKPI DIHKSHKGSN ASSNLKQPST
PSFLVASKSP PKIGISESVV NANKNDAISK KVE