ATG18_SCHPO
ID ATG18_SCHPO Reviewed; 373 AA.
AC Q9HDZ7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Autophagy-related protein 18;
GN Name=atg18; Synonyms=atg18a; ORFNames=SPAC589.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH
RP ATG5, DOMAIN, AND MUTAGENESIS OF ARG-228 AND ARG-229.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(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
CC preautophagosomal structure. Might also be involved in premeiotic DNA
CC replication (By similarity). Required for the recruitment of the atg5-
CC atg12/atg16 complex to the preautophagosomal structure. {ECO:0000250,
CC ECO:0000269|PubMed:23950735}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex (By similarity).
CC Interacts with atg5. {ECO:0000250, ECO:0000269|PubMed:23950735}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:23950735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23950735}. Vacuole membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {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:0000269|PubMed:23950735}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; CU329670; CAC19764.1; -; Genomic_DNA.
DR RefSeq; NP_594055.1; NM_001019479.2.
DR AlphaFoldDB; Q9HDZ7; -.
DR SMR; Q9HDZ7; -.
DR BioGRID; 278655; 53.
DR STRING; 4896.SPAC589.07c.1; -.
DR MaxQB; Q9HDZ7; -.
DR PaxDb; Q9HDZ7; -.
DR EnsemblFungi; SPAC589.07c.1; SPAC589.07c.1:pep; SPAC589.07c.
DR GeneID; 2542180; -.
DR KEGG; spo:SPAC589.07c; -.
DR PomBase; SPAC589.07c; -.
DR VEuPathDB; FungiDB:SPAC589.07c; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; Q9HDZ7; -.
DR OMA; TLGQIFP; -.
DR PhylomeDB; Q9HDZ7; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR PRO; PR:Q9HDZ7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; ISO:PomBase.
DR GO; GO:0005768; C:endosome; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
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:0006914; P:autophagy; IMP:PomBase.
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:0016236; P:macroautophagy; IMP:PomBase.
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:0006623; P:protein targeting to vacuole; ISO:PomBase.
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; 1.
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 1: Evidence at protein level;
KW Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..373
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000050872"
FT REPEAT 144..183
FT /note="WD 1"
FT REPEAT 186..226
FT /note="WD 2"
FT REPEAT 231..270
FT /note="WD 3"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 227..231
FT /note="L/FRRG motif"
FT /evidence="ECO:0000303|PubMed:23950735"
FT MUTAGEN 228
FT /note="R->T: Impairs localization and pre-autophagosomal
FT structure formation; when associated with Thr-229."
FT /evidence="ECO:0000269|PubMed:23950735"
FT MUTAGEN 229
FT /note="R->T: Impairs localization and pre-autophagosomal
FT structure formation; when associated with Thr-228."
FT /evidence="ECO:0000269|PubMed:23950735"
SQ SEQUENCE 373 AA; 41109 MW; B7609062573AF159 CRC64;
MHFFVRKYRG KAALLSIGTF DGYKIYNCDP FGKCFHKIQG ATSIVEMLFS TSLVALVEKD
DGNNRKLKLI NTKKSTTICE LTFPTPLLAV KLNRKRLLAV LEEQIYVYDI SNMLLLHTIE
TTSNVFAVCA LSPNSENCYL AYPDSRDHEP RTEGESSSPN VSNSAVSGQV ILWDVINCKQ
ITKIEAHKDS LACLAFNSDG TMLATASDNG RIIRVFAIPS GQRLYQFRRG SLPAQIYSIA
FHPDSSLLTV TSSTQTVHIF RLKEVYSNLE RQGLLPSSPP PKESLLRRSS RSLIGTVGGY
LPQSVSGMLD PERDFAYAHI PGDKVTSIAA FGPDNTIVNV ATYDGNLYSF RVNLRTGGEC
AMVNHFCVGL TAA
