ATG18_PICPA
ID ATG18_PICPA Reviewed; 543 AA.
AC Q8X1F5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=Autophagy-related protein 18;
DE AltName: Full=Glucose-induced selective autophagy protein 12;
GN Name=ATG18; Synonyms=GSA12;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11739783; DOI=10.1091/mbc.12.12.3821;
RA Guan J., Stromhaug P.E., George M.D., Habibzadegah-Tari P., Bevan A.,
RA Dunn W.A. Jr., Klionsky D.J.;
RT "Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and
RT autophagy in Saccharomyces cerevisiae and Pichia pastoris.";
RL Mol. Biol. Cell 12:3821-3838(2001).
RN [2]
RP FUNCTION.
RX PubMed=11533052; DOI=10.1074/jbc.m104087200;
RA Stromhaug P.E., Bevan A., Dunn W.A. Jr.;
RT "GSA11 encodes a unique 208-kDa protein required for pexophagy and
RT autophagy in Pichia pastoris.";
RL J. Biol. Chem. 276:42422-42435(2001).
RN [3]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
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. Involved in correct ATG9
CC trafficking to the pre-autophagosomal structure. Might also be involved
CC in premeiotic DNA replication (By similarity). Required for cytoplasm
CC to vacuole transport (Cvt) vesicle formation, autophagy, glucose-
CC induced micropexophagy and ethanol-induced macropexophagy. Required for
CC the involution of the vacuole that occurs during micropexophagy.
CC Involved in the recruitment of ATG2 to punctate structures when cells
CC are grown on glucose. {ECO:0000250, ECO:0000269|PubMed:11533052,
CC ECO:0000269|PubMed:11739783}.
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:0000269|PubMed:11739783}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11739783}. Endosome membrane {ECO:0000250};
CC 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:0000250|UniProtKB:P43601}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; AF368421; AAL67674.1; -; Genomic_DNA.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
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; Repeat; Transport;
KW Vacuole; WD repeat.
FT CHAIN 1..543
FT /note="Autophagy-related protein 18"
FT /id="PRO_0000050871"
FT REPEAT 225..265
FT /note="WD 1"
FT REPEAT 270..309
FT /note="WD 2"
FT REGION 162..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..270
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:P43601"
FT COMPBIAS 326..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 59893 MW; 4405B0FBB29411B8 CRC64;
MSQPTDEADK STGNAQVTHE SINFANFNQD STCVSVGYQS GYKIFNVEPF TKCLSLADTS
IGIVEMLFSS SLVAIVGLGE LPDSSPRKLK VFNTKRRSII CELTFPTSIL AVKMNRERMV
VLLEDTIYIY DINTMRILHT IETPSNPEGL IALSSSTENN ILAYPSPPKL PNRQETSTKG
TTNDNDRSHL ENIPENVNAN SSNLRNGDVI IFNSHTLQPI SVIEAHKAQL SAIALSSDGT
LLATASNKGT IVRVFDVETG VKLYQFRRGT YPTKIYCLSF SQDNRFVCAS SATETVHIFR
LGQDEANNTM PSRWSKNQKL ALQRYKQSMK QXQGSKPSSL VDSDSDPDVD ELVENDNSDD
DELEEDIDDE LAEERFNSSL TVPRRVSSTT SLGSYGSQES IGDKIEPHVD SARRSVARMI
RRTSQSLGRK AAEKMGPYLH PKFSSLLEPN RHFASLKVPA SKDTKTVVAI GNSVGQGELL
QLGEHEDVDN SSSTSDSTFH QKLLHVMVVS SEGFFYNFGL DTERGGDCTL LSQYSLLTDV
NDG
