ATG9_ASPFU
ID ATG9_ASPFU Reviewed; 951 AA.
AC Q4WLT9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=AFUA_6G12350;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
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DR EMBL; AAHF01000006; EAL89075.1; -; Genomic_DNA.
DR RefSeq; XP_751113.1; XM_746020.1.
DR AlphaFoldDB; Q4WLT9; -.
DR SMR; Q4WLT9; -.
DR STRING; 746128.CADAFUBP00007637; -.
DR EnsemblFungi; EAL89075; EAL89075; AFUA_6G12350.
DR GeneID; 3508419; -.
DR KEGG; afm:AFUA_6G12350; -.
DR VEuPathDB; FungiDB:Afu6g12350; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR InParanoid; Q4WLT9; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
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:0017128; F:phospholipid scramblase activity; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
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..951
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119825"
FT TOPO_DOM 1..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..289
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 457..477
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 478..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..578
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 646..666
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 667..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 107356 MW; 3612A5EDF029F851 CRC64;
MMTSNILSRF LPPNGSPSVY ETIRNHDATS DSSDVEERAG LTLEDGPGEH YSDRELEDAM
ADAGRSRLLD RDDAFISRRS PRKASVAGPS KSNSRRRHFS RPRWAHDASP SHDFEDGDDD
VPASLLVEGH HDDDELKSRL PPPPTSHITP DDRQPSRPGP STRGVRGRGR AAKEQQPLHH
ADRRRAPAVR WSLGQPNLNT VDPKEKAMWM WANVENLDNF LKEVYTYFLG NGIWSILLNR
VLSLLTFAFV VGFSTFLTNC IDYHKVRGSK SLNDILIKQC TTKMSLSSTF LLWLLTLFWI
GKAFQCLLDI RRLKHMHDFY YYLLGVSDTD IQTISWQEIV SRLMTLRDAN PATAGAVSAR
HRKFMGSQSK QRMDAHDIAN RLMRKENYLI ALINKDILDL TLPIPFLRNK QLFSRTLEWN
INLCIMDYVF NEQGQVRTLF LKDTHRKALS EGLRRRFIFA GIMNIFVAPF IVVYFMMHYF
FRYFNEYKKN PSQIGSRQYT PLAEWKFREF NELWHLFERR INMSYPFASR YVDQFPKDKT
VQVAGFVAFV SGALASVLAL ASIVDPELFL GFEITHDRTV LFYLGVFGSV WAVARGLVPE
ETTVFDPEYA LLEVINYTHY APSHWKGRLH SDEVRREFTE LYQMKIVIFL EEILSMIFTP
FILWFNLPKC SDRLIDFFRE FTVHVDGMGY LCSFAVFDFK KGTNVINQGD RRDPARQDLR
ADYFSTKDGK MLASYYGFLD NYGANHRGSH PATRRQFYPP PAFPTLGSPP AGEMGTIGDR
LDQTQTRHGL AGPFMGQQSV FGPSRYGLTG LGDHASPAPS ILLDPHHQPS TSGFRGTSRA
AGVQRYRSSR AHPPISGTIA DGDESPVATG RSDPSRPAAN AAGASSAGGV GTSDSNLGDS
WRMNLVEDGD DDNTEGGENV DAIAGGAGVL GLIQQFQRVN KDSRGRTAVG L
