ATG9_PHANO
ID ATG9_PHANO Reviewed; 899 AA.
AC Q0UYL2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=SNOG_03152;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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.
CC {ECO:0000250|UniProtKB:Q12142}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT89883.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445328; EAT89883.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001793733.1; XM_001793681.1.
DR AlphaFoldDB; Q0UYL2; -.
DR SMR; Q0UYL2; -.
DR STRING; 13684.SNOT_03152; -.
DR PRIDE; Q0UYL2; -.
DR GeneID; 5970590; -.
DR KEGG; pno:SNOG_03152; -.
DR eggNOG; KOG2173; Eukaryota.
DR InParanoid; Q0UYL2; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
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:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..899
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317912"
FT TOPO_DOM 1..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..270
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 442..462
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 463..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..552
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 630..650
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 651..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101537 MW; 5EBF6F7F15217BB1 CRC64;
MASNLLSRLL PSASDDLLEQ EASNNQNRRT SSSTDERPDM DIDEENFGAR FEAQDLNDLL
AEASSSHMTT ESRAASPEAR RNAPPGINTA ARAPAWRQPA PARAVPLDDD DDVPQSLLLE
GGLDPPPNPH PRPDGLPPPV PGPSTRHTRA QWETTRQQQR LHGDDRGGAP VRDWGAIGRG
GQFTADPKEK ASWLWVNQTD LDTYMREVYE YYVGSGIYSM ILRRTLSLLQ SAFVVGFMTF
LGWCIDYSKL SGSNKLSQVL VPKCTKEIHG FWIFALWVFT IYWLYSFYGL LTDIPRLRAM
HDFYHYLLDV PDRDIQTIQW QQIVSRIMAL RDLNLTTASN LSPETRKLLD SKSRQRLDAV
DIASRLMRRD NYLIALFNKE ILDVTVPIPF LGNRFIFSET TGWHVNLAVM EFVFSGPNGQ
FNQDFLKERN RRELVRRLRG RFFWTGIISI ICAPFAVVFV LASYLFKYFT EYHKDPGQLS
NRDFTTFAQW KFREFNELPH LFNRRRNMAY PYANLYLAQF PKDKTEQISS FVAFIAGAFA
SVLVAFTLLD SELFLTFEIS PGKTAIFWIG VLTTIYRVAR GSSPQEDQVT DPSYYLDHVI
YHTRYKPDSW QDRLHTDEVR AEFAKLYQPK ILIFAEEILS MVVTPFLLMF RLPQCSERIV
DFFREFSIVV DGLGVTCSYS MFPFKKGTQN VNNAPANRSG AHKDDGDLRE DYFMAKDNKM
LASYYGFLDT YATTGKGNSA RLPGRAGFHP PPQFPNAFGA MSQTAQPVDV GARGTSRGPA
GRQPLQRRTP RSGPAGRDEP IASVLLDPHH QPSSASILRG SPRTGPSGRY RTPLQPVADT
PGTRIEEEST IGDSWRTSRL AQDDDEEEEA PGANRGGVLQ LLQQFSKAQA EGRGAGVGV
