ATG18_PICGU
ID ATG18_PICGU Reviewed; 568 AA.
AC A5DHI9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Autophagy-related protein 18;
GN Name=ATG18; ORFNames=PGUG_02740;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 -!- 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; CH408157; EDK38642.2; -; Genomic_DNA.
DR RefSeq; XP_001485011.1; XM_001484961.1.
DR AlphaFoldDB; A5DHI9; -.
DR SMR; A5DHI9; -.
DR STRING; 4929.XP_001485011.1; -.
DR EnsemblFungi; EDK38642; EDK38642; PGUG_02740.
DR GeneID; 5126886; -.
DR KEGG; pgu:PGUG_02740; -.
DR VEuPathDB; FungiDB:PGUG_02740; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; A5DHI9; -.
DR OMA; TLGQIFP; -.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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 Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..568
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318006"
FT REPEAT 19..57
FT /note="WD 1"
FT REPEAT 268..308
FT /note="WD 2"
FT REPEAT 313..352
FT /note="WD 3"
FT REPEAT 464..508
FT /note="WD 4"
FT REPEAT 518..558
FT /note="WD 5"
FT REGION 162..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 309..313
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 162..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60933 MW; 2E37CA73BE5D7AB6 CRC64;
MLKSQIAPIP SYESQPVHKP SSSVNFITFN QDGSCIAVGN NKGYSIFTTN PFTKCYDSPP
GEAIGIVEML YSTSLVVVVA LGEETGSSPR KLKIINTKRG STICDLVFPS TILKVKLTRS
RMIVLLEEQI YLYDISTMKL LHTIETSPNM AGICAISADQ GSTDTSNSAD NSGSIGSGPA
SGSGAGSGSA SMTSTDSTPD AQSHSYLAYP SPPKTAMHDS LLVAGINTNG GSHSKQNNIQ
SVSNAPNRVG DVIIFDTDSL QPLCVIEAHK SALAAISLSS DGRLLATASD KGTIVRVFSV
STGAKLYQFR RGTYPTKVYS VAFSPDNRYV VTTSASGTVH IFRLGEDESL ESKHKRKRAS
RQHETIAEET SATQDLDDEI EDDGDDSDVD DVESLEVVPS KQRKLSQGSS NSYTSMNSGI
SGMSEDGKEP KIDPIVDHAR LSVARMIRRS SQTLGRKAAQ KMGDFLPSKF ASILEPTRHF
ASLKIASASK DVKSIAVLDS QVVHDMVPQM FLHSKDAAPA SALDTQSMTE MALLHIFVVT
SDGYLYVYGL DPERGGDCIL LQQHSFDI
