ATG18_USTMA
ID ATG18_USTMA Reviewed; 453 AA.
AC Q4P4N1; A0A0D1CJN2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Autophagy-related protein 18;
GN Name=ATG18; ORFNames=UMAG_04932;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003154; KIS67063.1; -; Genomic_DNA.
DR RefSeq; XP_011391251.1; XM_011392949.1.
DR AlphaFoldDB; Q4P4N1; -.
DR SMR; Q4P4N1; -.
DR STRING; 5270.UM04932P0; -.
DR EnsemblFungi; KIS67063; KIS67063; UMAG_04932.
DR GeneID; 23564962; -.
DR KEGG; uma:UMAG_04932; -.
DR VEuPathDB; FungiDB:UMAG_04932; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; Q4P4N1; -.
DR OMA; PSRDFAW; -.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000000561; Chromosome 15.
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; 3.
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..453
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000318009"
FT REPEAT 9..49
FT /note="WD 1"
FT REPEAT 204..244
FT /note="WD 2"
FT REPEAT 249..288
FT /note="WD 3"
FT REGION 284..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..249
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 287..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 47807 MW; 5F311E664A7F83E7 CRC64;
MSSSSLPTKS SNALLSVNFN QDHSCIAVGT RDGYSITNCE PFGRVYTNNA GPTSLVEMLF
CTSLVALVAT SDTDPKSNAS PRRLQIVNTK RQSVICELLF PTAILGVKLN RRRLVVVLEQ
EIYIYDISNM KLLHTIETSP NPMAICALSP SSENCFLAYP SPVASPTSPF SNSGASSSAE
ANTTAGDVLI FDLLSLSVTN VIQAHKTPIS ALALNATGTL LATASDKGTV IRVFSIPAAQ
KLHQFRRGSY AARIYSLNFN AVSTLLAVSS DTETVHIFKL SSGAGAGAKG RSSSNGGESP
SLNSFDGSSD SSSPPGSTTN ATRGGYEAFM GKHKAAKSNG ISGTLRRRSM ALGRGITGSV
GGYLPNSLTE MWEPSRDFAF LKLPSQGVSS VVALSSTTPH VMVVTSEGYF YSYAIDLEHG
GECILMKQYS LIDPDLDTTS TARSDTATPS LAD