ATG9_PENRW
ID ATG9_PENRW Reviewed; 948 AA.
AC A7KAM0; B6HSL8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=Pc22g04040;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation (PubMed:17204848). Cycles
CC between the preautophagosomal structure/phagophore assembly site (PAS)
CC and the cytoplasmic vesicle pool and supplies membrane for the growing
CC autophagosome. Lipid scramblase activity plays a key role in
CC preautophagosomal structure/phagophore assembly by distributing the
CC phospholipids that arrive through atg2 from the cytoplasmic to the
CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane
CC expansion. Required for mitophagy. Also involved in endoplasmic
CC reticulum-specific autophagic process and is essential for the survival
CC of cells subjected to severe ER stress. Different machineries are
CC required for anterograde trafficking to the PAS during either the Cvt
CC pathway or bulk autophagy and for retrograde trafficking (By
CC similarity). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:17204848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088;
CC Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:O74312}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer. Acts as a lipid scramblase that uses its central pore to
CC function: the central pore opens laterally to accommodate lipid
CC headgroups, thereby enabling lipid flipping and redistribution of
CC lipids added to the outer leaflet of atg9-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:O74312}.
CC -!- PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for
CC preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; EF107742; ABO31080.1; -; Genomic_DNA.
DR EMBL; AM920437; CAP97692.1; -; Genomic_DNA.
DR RefSeq; XP_002564443.1; XM_002564397.1.
DR AlphaFoldDB; A7KAM0; -.
DR SMR; A7KAM0; -.
DR STRING; 1108849.XP_002564443.1; -.
DR EnsemblFungi; CAP97692; CAP97692; PCH_Pc22g04040.
DR GeneID; 8306163; -.
DR KEGG; pcs:Pc22g04040; -.
DR VEuPathDB; FungiDB:PCH_Pc22g04040; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR BioCyc; PCHR:PC22G04040-MON; -.
DR Proteomes; UP000000724; Contig Pc00c22.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..948
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317911"
FT TOPO_DOM 1..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..287
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 455..475
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 476..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..576
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 644..664
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 665..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 107622 MW; 31E38DBB322C8A13 CRC64;
MMSSNILSRF LPPTGSPSVY ETIRQHDAGS EYSDLEERAG LVIEDQQEQY SDRELEDALA
DAQDSEIVSP STALLNQARS VKAPEERASP SGTRRRKSSR PRWMAQESPL GYELDDHDED
VPQSLLVEGH HEDLKPRLPP PPQSHNRSDR RRTPSPGPSS RPTEARWNER GVHQQPPPSE
SGHPIGRWFT GQHPGLANVD PKKKAMWRWA NVEDLDNFLK DVYVYFLGNG IWSILLTRVL
NLLTFAFVVG FSTFLTNCID YPKVRRSKTL NDILVPQCTA NMSGSSTFLL WLFSFFWIGK
LFQYLLDIRR LKHLHDFYLY LLGVSDAEVQ TISWQEVVSR LMALRDSNPS TAAAVSAKHR
RFLGSQSKQR MDAHDIANRL MRKENYMIAL VNKDILDLTL PIPFLKNRQL FSRTMEWNLN
LCVMDYVFNE QGQLRTLFLK DTHRRALSDG LRRRFIFAGV MNIFVAPFIV VYFMMHYFFR
YFNEFKKNPG QIGSRQYTPM AEWKFREFNE LWHLFERRIN MSYPFASRYI DQFPKDKTVQ
VARFVAFISG ALASVLALAS VIDPELFLGF EITHDRTVLF YLGIFGTVWA FARGLAPEET
DVFDPEYALL ELIDFTHYFP SGWKGRLHSD DVRKEFAILY QMKIVIFLEE ILSMIFTPFV
LWFSLPKCSD RLIDFFREFT VHVDGVGYLC SFAVFDFKKG TNVLSQAGPG RRDPGKQDLR
TDYFSTKDGK MLASYYGFLD NYGTTHQATS RRPFHPPPTL PTLGSPTAGG FGALPDRPDH
LQTRLGPTPG APFGPQSMIG TSKPRQMGGF DHRSPAPSIL LDPHHQPSTT GFRAAARIAP
QQHQRSRLGR SHHPSTDPID DEEEPLSQDG HDSTTRQSGA RTGTSSAGAG TSDSNLGDSW
RMNPLSNDED EGDEGENIDA IAGGGGVLGL IQQFQKANTE GRRTNVGI
