ID   ATG18_CANAL             Reviewed;         558 AA.
AC   Q5ABA6; A0A1D8PC80;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; OrderedLocusNames=CAALFM_C100430WA;
GN   ORFNames=CaO19.13485, CaO19.6064;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW25741.1; -; Genomic_DNA.
DR   RefSeq; XP_719026.2; XM_713933.2.
DR   AlphaFoldDB; Q5ABA6; -.
DR   SMR; Q5ABA6; -.
DR   STRING; 237561.Q5ABA6; -.
DR   EnsemblFungi; C1_00430W_A-T; C1_00430W_A-T-p1; C1_00430W_A.
DR   GeneID; 3639285; -.
DR   KEGG; cal:CAALFM_C100430WA; -.
DR   CGD; CAL0000198706; orf19.13485.
DR   VEuPathDB; FungiDB:C1_00430W_A; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q5ABA6; -.
DR   OrthoDB; 391429at2759; -.
DR   PRO; PR:Q5ABA6; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0070772; C:PAS complex; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IEA:EnsemblFungi.
DR   GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR   GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0044090; P:positive regulation of vacuole organization; IEA:EnsemblFungi.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006624; P:vacuolar protein processing; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR048720; PROPPIN.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR11227:SF17; WD REPEAT DOMAIN PHOSPHOINOSITIDE-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR11227; WD-REPEAT PROTEIN INTERACTING WITH PHOSPHOINOSIDES WIPI -RELATED; 1.
DR   Pfam; PF21032; PROPPIN; 2.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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..558
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000050862"
FT   REPEAT          247..287
FT                   /note="WD 1"
FT   REPEAT          292..331
FT                   /note="WD 2"
FT   REGION          344..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           288..292
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        370..390
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  61694 MW;  F9293487492E473C CRC64;
     MLQTSSSSAT ASLQQQLSKQ YANSFSNDGS SFSSKNNQQY SEIVNYISFN QDASCITIGL
     KNGYKIFNCQ PNFGRSFQFK NDESTGIVEM LYCTSLLATV AQGEEIGSSP RKLKIINTKT
     KSTICDLIFP STILQVKLTN TRLIVVLEDQ IYLYDITTMK LLHTIETSPN LSGLSAISYD
     DSNSYLAYPS PPKTITHDSL LASGINTNGG SNSTQNNISS VSNTPNRVGD VIIFNLTSLQ
     PISVIEAHKS TIASMAFSNN GLYLATASDK GTIVRIFEVA TGTKLYQFRR GTYPTKIYSL
     RFSADDKYVL ATSSSLTVHI FRLGEEEALE TKHKKKKIPA VATILEEETE GSQSNEQTKS
     IKRNSEEFED IRDDGDDSDV DDEDGDIDDE SLEVIPAKQR KLSQGSTNSY TSVNSEDVQS
     NSPKTEPLID QNRLSMARII RRSSQTLGRK AAQKMGDFLP SRFSSILEPT RNFASLKINA
     HSKDTKSVAV MNNVLQQDLI PQTYLASDNA SAKQDFMEVS LFHIYVVTTE GMLYTYGLDP
     ERGGDCILLN SHCILDEY
//