ATG18_PENRW
ID ATG18_PENRW Reviewed; 427 AA.
AC A7KAM8; B6HJP2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Autophagy-related protein 18;
GN Name=atg18; ORFNames=Pc21g06730;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Necessary for proper vacuole morphology. Plays an important role in
CC osmotically-induced vacuole fragmentation. Required for cytoplasm to
CC vacuole transport (Cvt) vesicle formation, pexophagy and starvation-
CC induced autophagy. Involved in correct atg9 trafficking to the pre-
CC autophagosomal structure. Might also be involved in premeiotic DNA
CC replication (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17204848}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- DOMAIN: The N-terminus might form a beta-propeller domain involved in
CC specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2),
CC leading to the association of the protein to the membrane.
CC {ECO:0000250}.
CC -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC transport (Cvt) pathway, for the recruitment of atg8 and atg16 to the
CC PAS in nutrient-rich medium, and for its recruitment to and
CC dissociation from the PAS under starvation conditions.
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; EF110894; ABO31315.1; -; Genomic_DNA.
DR EMBL; AM920436; CAP95570.1; -; Genomic_DNA.
DR RefSeq; XP_002567717.1; XM_002567671.1.
DR AlphaFoldDB; A7KAM8; -.
DR SMR; A7KAM8; -.
DR STRING; 1108849.XP_002567717.1; -.
DR EnsemblFungi; CAP95570; CAP95570; PCH_Pc21g06730.
DR GeneID; 8314111; -.
DR KEGG; pcs:Pc21g06730; -.
DR VEuPathDB; FungiDB:PCH_Pc21g06730; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR OMA; PSRDFAW; -.
DR OrthoDB; 1216824at2759; -.
DR BioCyc; PCHR:PC21G06730-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
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; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..427
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318004"
FT REPEAT 1..36
FT /note="WD 1"
FT REPEAT 69..114
FT /note="WD 2"
FT REPEAT 184..224
FT /note="WD 3"
FT REPEAT 229..268
FT /note="WD 4"
FT REPEAT 308..354
FT /note="WD 5"
FT REPEAT 366..406
FT /note="WD 6"
FT REGION 262..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 225..229
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 262..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46100 MW; D5372FE2D6FF7D69 CRC64;
MAMNFVTFNQ DYSYLAVATS KGFQIFTTEP FAKSYEAKEG NIAVIEMLFS TSLVALILSP
RRLQIQNTKR QCTICELTFP TTVLAVKLNR KRLVIVLEDQ IYLYDIQTMK LLSTIDTSPN
PNAICALAPS SENCYMAYPL PQKAPAAAST PAHAPPGTTH VSPTTGDVLI FDAVKLEAIN
VIEAHRSPLA LIALNSDGTL LATASDKGTI IRIFSVPDGH KLYQFRRGSM PSRIYSMSFN
TTSTLLCVSS STETVHIFKL AQQGPSSDGS SSHSPPSRDH GSPPNTYGYA HEEDEAVGDA
GSDSSLRKHN GTLMGMIRRT SQNVGGAVAA RMGGYLPKGV SEMWEPARDF AWIKLPRSNP
GPGGNTGAGP LRSVVAMSSN TPQVMVVTSD GNFYVFNIDL SKGGEGTLTK QYSVVDSTDR
LGYTTEY
