ATG9_NEOFI
ID ATG9_NEOFI Reviewed; 953 AA.
AC A1DNW0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=NFIA_058310;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16481.1; -; Genomic_DNA.
DR RefSeq; XP_001258378.1; XM_001258377.1.
DR AlphaFoldDB; A1DNW0; -.
DR SMR; A1DNW0; -.
DR STRING; 36630.CADNFIAP00004557; -.
DR EnsemblFungi; EAW16481; EAW16481; NFIA_058310.
DR GeneID; 4584894; -.
DR KEGG; nfi:NFIA_058310; -.
DR VEuPathDB; FungiDB:NFIA_058310; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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: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; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
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..953
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317910"
FT TOPO_DOM 1..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..291
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 459..479
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 480..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..580
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 648..668
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 669..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 107554 MW; 206D17E8E4FCC0A5 CRC64;
MMTSNILSRF LPPNGSPSVY ETIRHHDATS DSSDVEERAG LTLEDGSGEH YSDRELEDAM
TDAERSRLLD PDDAFIRRKS PRKASVAGPS KSNSRHRHSG RPRWAHDASP GHDFEDGDDD
VPASLLVEGH HDDDDDDLKS RLPPPPTSHF TPDNRQTSLP GPSTRGDRAR WRAAREQQPL
HHADRRRAPA VRWSLGQPNL NTVDPKEKAM WMWANVENLD NFLKDVYTYF LGNGIWSILL
NRVLSLLTFA FVIGFTTFLT NCIDYHKVRG SKTLNDILIE QCTTKMSLSS TFLLWLLTLF
WIGKAFQCLL DIRRLKHMHD FYYYLLGVSD TDIQTISWQE VVSRLMTLRD ANPATAGAVS
ARHRKFMGSQ SKQRMDAHDI ANRLMRKENY LIALINKDIL DLTLPIPFLR NKQLFSQTLE
WNINLCIMDY VFNEQGQVRT LFLKDTHRKA LSEGLRRRFI FAGIMNIFVA PFIVVYFMMH
YFFRYFNEYK KNPSQIGSRQ YTPLAEWKFR EFNELWHLFE RRINMSYPFA SRYVDQFPKD
KTVQVAGFVA FVSGALASVL ALASIVDPEL FLGFEITHDR TVLFYLGVFG SVWAVARGLV
PEETTVFDPE YALLEVINYT HYAPSHWKGR LHSDEVRREF AELYQMKIVI FLEEILSMIF
TPFILWFNLP KCSDRLIDFF REFTVHVDGM GYLCSFAVFD FKKGTNVINQ GDRREPARQD
LRADYFSTKD GKMLASYYGF LDNYGANHRG SHPATRRQFH PPPAFPTLGS PPAGEMGTIG
DRLDQTQTRH GLAGPFMGQQ SVFGPSRYGP TGLGDHASPA PSILLDPHHQ PSTSGFRGTS
RAAAFPRYRS SRAHPPTSGT IADGDESPVA TGGSDPSRPA ANAAGASSAG GVGTSDSNLG
DSWRMNLAED VDDDNTEGGE NVDAIAGGAG VLGLIQQLQR VNKDTRGRTA VGL
