ATG9_MAGO7
ID ATG9_MAGO7 Reviewed; 917 AA.
AC Q51WZ9; A4QUK6; G4N1A4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000303|PubMed:19556868};
GN Name=ATG9 {ECO:0000303|PubMed:19556868}; ORFNames=MGG_09559;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=19556868; DOI=10.4161/auto.5.7.9161;
RA Dong B., Liu X.H., Lu J.P., Zhang F.S., Gao H.M., Wang H.K., Lin F.C.;
RT "MgAtg9 trafficking in Magnaporthe oryzae.";
RL Autophagy 5:946-953(2009).
RN [3]
RP FUNCTION, INTERACTION WITH HAT1, SUBCELLULAR LOCATION, ACETYLATION AT
RP LYS-621, AND MUTAGENESIS OF LYS-621.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation. Cycles between the
CC preautophagosomal structure/phagophore assembly site (PAS) and the
CC 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 (By similarity). Different
CC machineries are required for anterograde trafficking to the PAS during
CC either the Cvt pathway or bulk autophagy and for retrograde trafficking
CC (PubMed:30776962). Plays a role in appressorium formation and
CC pathogenicity (PubMed:30776962). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:30776962}.
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 (By similarity). Interacts
CC with HAT1 (PubMed:30776962). {ECO:0000250|UniProtKB:O74312,
CC ECO:0000269|PubMed:30776962}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:19556868, ECO:0000269|PubMed:30776962}; Multi-pass
CC membrane protein {ECO:0000303|PubMed:19556868}. Cytoplasmic vesicle
CC membrane {ECO:0000269|PubMed:19556868}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:19556868}. Vacuole membrane
CC {ECO:0000269|PubMed:19556868}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:19556868}. 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}. Note=Concurrent with the cytoplasmic
CC punctation, localizes on the central vacuole of the submerged hyphae
CC from the conidia cultured in rich media. ATG1, ATG2 and ATG18, but not
CC ATG13, are required for ATG9-cycling through the multiple localization
CC sites. {ECO:0000269|PubMed:19556868}.
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: Acetylated by HAT1 at Lys-621, which increases the ability to bind
CC vesicles during nutrient starvation induction.
CC {ECO:0000269|PubMed:30776962}.
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; CM001233; EHA52375.1; -; Genomic_DNA.
DR RefSeq; XP_003712182.1; XM_003712134.1.
DR AlphaFoldDB; Q51WZ9; -.
DR SMR; Q51WZ9; -.
DR STRING; 318829.MGG_09559T0; -.
DR iPTMnet; Q51WZ9; -.
DR PRIDE; Q51WZ9; -.
DR EnsemblFungi; MGG_09559T0; MGG_09559T0; MGG_09559.
DR GeneID; 2680457; -.
DR KEGG; mgr:MGG_09559; -.
DR VEuPathDB; FungiDB:MGG_09559; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR InParanoid; Q51WZ9; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR PHI-base; PHI:2066; -.
DR PHI-base; PHI:2077; -.
DR PHI-base; PHI:8264; -.
DR Proteomes; UP000009058; Chromosome 3.
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:0005774; C:vacuolar 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 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Germination; Glycoprotein; Golgi apparatus; Lipid transport; Membrane;
KW Phosphoprotein; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport; Vacuole; Virulence.
FT CHAIN 1..917
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119833"
FT TOPO_DOM 1..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..275
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 443..463
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 464..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..564
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 634..654
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 655..917
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 621
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:30776962"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 621
FT /note="K->R: Disturbs the acetylation levels of ATG9 and
FT impairs the binding ability to vesicles during nutrient
FT starvation induction."
FT /evidence="ECO:0000269|PubMed:30776962"
SQ SEQUENCE 917 AA; 104559 MW; AAD88818CDB2B46A CRC64;
MASNIFSRLV PQDRGRSFYE DLRQTDPDAD LESRAGIDID EENLNRSYHD YDLDEAERLA
GDESHISHSR GDVAGANTVH RRGQKANTAR WLGAGVEDDV DNDVPESLLV ETPRAPQHLL
LSPSRAGPSH PRPTAVPGPS TRQNQAQWEA TRHQQRLHND DTMPHGPFSG RAGQGRPEPP
PVGLMAGDPY EQAMWRWVNV SNLDNFIKDV YAYYRAAGFW CIIVQRILEL VNAAFVAVFL
TFLSQCVDYH KLPHSKKMED IIIPKCTQNM SLVWNVGLWL FAIYFICRCF GLIIQLRQLK
HLRDFYTHLL KIPEADMQSV SWQDVVGRIM ALRDSHPRTA GNLTRVQRAW IGSQSKERLD
AHDIANRIMR RENFMIAMLN KDVLDLTIPL PFFRNKQHMS ECVVLAISFS ILDFVFDNQG
QVNPEFLKAS RRRQLSQKLK SRFFFAGLMI FVMSPFIALY LILVYFLTYF HEFRNDPGAL
GARTYNSLAK WKFREFNELD HLFNDRMNMS HPFAKRYIDM FPKRKTEQVA RTVSFITGSI
VAVLGLATIF DSEAFLTFEI TPDRSVLFYV SILATLWAVA RGNISDDNEV YDPEFAMKSI
IEFTHYEPDH WRGRLHSTEV KNEFSELYKP RPQIFLEEIL SILLTPLVLL VSLPNSTDQI
VDFFREFTIH VDGLGYVCLF SVFNFQQGHA NQKQAAAADA PDNREEYYST KHGKMAASFY
GFLDHYVINP KTGLPGNQLP GSRQQFQHPP SFPGLQSPTL AADMRHSRMM RERGRSSGVQ
IQGSQGRTPQ FRTPMPQPSP MASILLDPHH QPAPGAFGSR SMHRSRQMAV PHRGGYMSDR
DIIEEAVTED GQDDARFGKL GDEDIDESGG ALDESTWQTS PTKTLSRENS GANPQETEVG
VLGLIHQFQQ AHMHLRR
