ATG9_GIBZE
ID ATG9_GIBZE Reviewed; 888 AA.
AC I1S9X9; A0A1C3YLP0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000303|PubMed:28894236};
GN Name=ATG9 {ECO:0000303|PubMed:28894236}; ORFNames=FGRAMPH1_01T26133;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30044782; DOI=10.1371/journal.pgen.1007546;
RA Zheng H., Miao P., Lin X., Li L., Wu C., Chen X., Abubakar Y.S.,
RA Norvienyeku J., Li G., Zhou J., Wang Z., Zheng W.;
RT "Small GTPase Rab7-mediated FgAtg9 trafficking is essential for autophagy-
RT dependent development and pathogenicity in Fusarium graminearum.";
RL PLoS Genet. 14:E1007546-E1007546(2018).
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. 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). Autophagy is required for proper vegetative growth,
CC asexual/sexual reproduction, and full virulence (PubMed:28894236,
CC PubMed:30044782). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). Required for aerial hyphae development
CC and lipid droplet degradation in response to starvation
CC (PubMed:30044782). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:28894236, ECO:0000269|PubMed:30044782}.
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 (By similarity). ATG1 phosphorylation is
CC required for ATG18 interaction and preautophagosome elongation (By
CC similarity). {ECO:0000250|UniProtKB:Q12142}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC reduces conidiation (PubMed:28894236). Blocks autophagy
CC (PubMed:30044782). {ECO:0000269|PubMed:28894236,
CC ECO:0000269|PubMed:30044782}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB65354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970335; SCB65354.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011327831.1; XM_011329529.1.
DR AlphaFoldDB; I1S9X9; -.
DR SMR; I1S9X9; -.
DR STRING; 5518.FGSG_13660P0; -.
DR GeneID; 23560466; -.
DR KEGG; fgr:FGSG_13660; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR InParanoid; I1S9X9; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0000421; C:autophagosome membrane; EXP:PHI-base.
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; EXP:PHI-base.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IPI:PHI-base.
DR GO; GO:1905691; P:lipid droplet disassembly; IMP:PHI-base.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; IMP:PHI-base.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..888
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000443897"
FT TOPO_DOM 1..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..422
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 512..532
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 533..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..611
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 643..663
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 664..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 100819 MW; 76DC530B5D9DB4F2 CRC64;
MASNIFSRIK SPSGGSQSFY QQLRSGEDPE YDPGLDEENL GHRFDDFQAE GMDIGDSSMT
VESVAPGSKG KGKATFRPTA HARSSGITSP RWQQDDDGDN EVPASLLMEP KDLDPPASPP
NKRATNPGSS RTPASVGPSS ARTRAQWEAA TAQQQLHQDH PYTTPMGPQP IPVARGTMSN
NPREKALWRW VNTSNLDSFM RDVYDYFEGG GLWCILCANA LWLFQCIDYS RVPDSRSLHE
VIVPQCTRKM SGLWNFAIWL YTFFFIWKCV QYFVEIRRLT YIRDFYIYLL DIPEQDMQTI
SWQDVVARIM ALREENPKTA TNISPRLRQF MGSQSKERLD ALDIANRLMR KENYLIAMIN
KDILDLSLPV PFLRGRQMFS KTMEWYLQYC ILDMAFNELG QVQQDFLRPD RRRLLSQKLR
QRFLFAGFLN LLFAPVVLAY VVIVYFFTYY YEYQKDPKQA AARKYTSLAE WKFRQFNELP
HIFYERLHMS YPFATRYIDQ FPKRITEAVA RTIAFMSGAI TAILAIGSVL DSELFLNFEI
TKDRPVIFYL GVFAAIWATT RGMVSEETLV FNPEYALRNV IEYTRYVPDH WKNKLHSSEV
KQEFSELYKM KVVIFLEEMM GIVTTPMLLL FSLPRCSDQI VDFFREFTIH VDGLGYVCSF
AVFDFQKGPG NTGPQGPRPD VREDYYSTKH GKMAASYYGF LDNYAANPKT GIPGHLPPGP
KPSFHPPPSF PGIGSPTLAA DMQGSHIGRT GTETGRARSR APGGRGPRIG VMPQPSPMAS
MLLDQHHQPP GGNMVARSLH ASRYPRGYRG ESQIIEETEA SSIRRNGEDD ELYEPGGALG
ESVWETSPAR GVTRENSAAN TEDPEAGVLG LIYQLQQTQR PRRGGGMV
