ATG18_CRYNJ
ID ATG18_CRYNJ Reviewed; 423 AA.
AC P0CS28; Q55SA5; Q5KGQ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Autophagy-related protein 18;
GN Name=ATG18; OrderedLocusNames=CNE02750;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017345; AAW43831.1; -; Genomic_DNA.
DR RefSeq; XP_571138.1; XM_571138.1.
DR AlphaFoldDB; P0CS28; -.
DR SMR; P0CS28; -.
DR STRING; 5207.AAW43831; -.
DR PaxDb; P0CS28; -.
DR EnsemblFungi; AAW43831; AAW43831; CNE02750.
DR GeneID; 3257960; -.
DR KEGG; cne:CNE02750; -.
DR VEuPathDB; FungiDB:CNE02750; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; P0CS28; -.
DR OMA; PSRDFAW; -.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000002149; Chromosome 5.
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: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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
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 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..423
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000050864"
FT REPEAT 200..240
FT /note="WD 1"
FT REPEAT 245..284
FT /note="WD 2"
FT REGION 281..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..245
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
SQ SEQUENCE 423 AA; 45276 MW; 1CA50732B697B823 CRC64;
MSRLAKRHPD LLSCNFNQDY SCIAVGHKKG YTILNCDPFG KVHSNNDQGA TGIVEMLFCT
SLVALVGAAE NQPSNSPRKL QIVNTKRQST ICELIFPTSV LAVKMNRKRL IVVLENEIYI
YDISTMKLLH TIETGPNPNA VCALSSSSER SYLAYPSPVP SASSTPLSSS AIPAPPPAPT
TGDVLLFDTI SLTALNVIQA HKTPIAALAL NSTGTMLATA SDKGTVVRVF SVPDAKKLWQ
FRRGSSSARI FSINFNLMST LLAVSSDTST IHIYRLASSR KGGKDADDAS TEEARSPTPS
ETPLASSPPL AAGKLDSHSA ASSLRRRSYH LGKSFVGGVG GYLPKSVSEM WEPQRDFAFI
KLRGNHGRTV VAMSATVPQV MVISSEGLFQ AYNIDLENGG ECSLMKEFAL LGSEDFGNGS
NGI
