ATG18_KLUMD
ID ATG18_KLUMD Reviewed; 513 AA.
AC W0T5P4;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Autophagy-related protein 18 {ECO:0000303|PubMed:26442587};
GN Name=ATG18 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_20474;
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA Limtong S., Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
RN [2]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT structural and biochemical studies of autophagy.";
RL J. Biol. Chem. 290:29506-29518(2015).
CC -!- FUNCTION: Component of the PI(3,5)P2 regulatory complex that regulates
CC both the synthesis and turnover of phosphatidylinositol 3,5-
CC bisphosphate (PtdIns(3,5)P2) (By similarity). Plays an important role
CC in osmotically-induced vacuole fragmentation (By similarity). Required
CC for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy
CC and starvation-induced autophagy (By similarity). Involved in correct
CC ATG9 trafficking to the pre-autophagosomal structure (By similarity).
CC With ATG2, protects ATG8 from ATG4-mediated cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex (By similarity).
CC Interacts with ATG2 and ATG9 (By similarity). The ATG2-ATG18 complex is
CC essential for autophagosome formation (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}. Endosome membrane
CC {ECO:0000250|UniProtKB:P43601}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- DOMAIN: The 377 first amino acids might form a beta-propeller domain
CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate
CC (PIP2), leading to the association of the protein to the membrane (By
CC similarity). Association to the membrane can also occur through binding
CC to phosphatidylinositol 3-monophosphate (PI3P) (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P43601}.
CC -!- DISRUPTION PHENOTYPE: Still forms preautophagosomal structures (PAS) in
CC proximity to the vacuolar membrane (PubMed:26442587).
CC {ECO:0000269|PubMed:26442587}.
CC -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC and have a more ordered secondary structure than their S.cerevisiae
CC counterparts, which might contribute to the superior thermotolerance
CC and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC as a new model organism for further elucidation of the molecular
CC details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; AP012214; BAO38932.1; -; Genomic_DNA.
DR AlphaFoldDB; W0T5P4; -.
DR SMR; W0T5P4; -.
DR EnsemblFungi; BAO38932; BAO38932; KLMA_20474.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000065495; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0030242; P:autophagy of peroxisome; 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:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0016236; P:macroautophagy; 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:0006624; P:vacuolar protein processing; IEA:EnsemblFungi.
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; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Membrane; Protein transport; Repeat; Transport;
KW Vacuole; WD repeat.
FT CHAIN 1..513
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000443919"
FT REPEAT 2..40
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 248..288
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 293..332
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REGION 167..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..292
FT /note="Necessary for proper localization to vacuole
FT membrane"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT REGION 333..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 289..293
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57117 MW; 7B8CD15174B07886 CRC64;
MSDLPIINFI NFNQNGTCIS IGTSQGFKIF NCEPFGRFYQ DDEGGCGIVE MLFSTSLLAV
VGMGENPAMS PRRLRMLNTK RHSVICEVTF PTTILSIKMN KTRLAVLLQE QIYIYDISNM
RLLHTIETSM NAQGLMSMSP NSENNYLVYP SPPKVINSEI KDHATTNNIN IKKSDAAEDP
LRKDHFAYDP SDHSHPQSTT ESTSNNHNRT YSSGNNNNTN SNPNKIIKNG DVIVFNLQTL
QPTMVIEAHK GEIAALKLSA DGTLLATASE KGTIIRVFNV ENGSKVYQFR RGTYSTKISS
LSFSKDNQFL AVCSSSKTVH IFKLGEKIID NTKPNELNSD DDMDDDLLPQ FENGDDEEEV
DEETLDEEAT SLNSSHSNKE PIVDSSRSTV GRMIRKSSQR LSRKAAKTLG AYFPIKVSSI
LEPSRHFASL KISTTTNQPI KAIAAIDDPI SLNTNEYPDL FDTSNQADHQ NTDGLKMIPV
RVLSSEGYMY KYILDPERGG DCILLEQYSL LSE
