ATG9_ASPCL
ID ATG9_ASPCL Reviewed; 949 AA.
AC A1CU77;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=ACLA_085600;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06864.1; -; Genomic_DNA.
DR RefSeq; XP_001268290.1; XM_001268289.1.
DR AlphaFoldDB; A1CU77; -.
DR SMR; A1CU77; -.
DR STRING; 5057.CADACLAP00007661; -.
DR PRIDE; A1CU77; -.
DR EnsemblFungi; EAW06864; EAW06864; ACLA_085600.
DR GeneID; 4700445; -.
DR KEGG; act:ACLA_085600; -.
DR VEuPathDB; FungiDB:ACLA_085600; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_1_1; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000006701; 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..949
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317906"
FT TOPO_DOM 1..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..289
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 432..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..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Basic and acidic 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 949 AA; 106768 MW; 25A9E0EE4E5D0A41 CRC64;
MMTSNILSRF LPPNNSPSVY EAIRQNDADS DSSDVEERAG LTLEDGHGGH YTDHELQDAM
VDADQSELPS PDDAFLARES HHRVPSEGPS KSTSRRRKNS RPRWMQAASP GQDFEYGDDD
DVPASLLVEG HHDDEDLKSR LPPPPRPLSP HEIQPSLPGP SSQGDQARWR AARDQQPLHN
ASRRRPPGVK WSLGQPNLNT VDPKEKAMWM WANVDNLDNF LKEVYSYFLG NGIWSILLTR
VLSLLTFAFV VGFSTFLTNC VNYHKVRGSK TLDDILVDRC TTKMSLSSTF LLWLLTFFWI
GKAFQCLLGI RRLKHMHDFY HYLLGVSDTD IQTISWQEVV SRLMTLRDAN PATAGAVSAR
HRKFMGSQSK QRMDAHDIAN RLMRKENYLI ALVNKDILDL TLPIPFLRNR PLFSQTLEWN
LNLCIMDYVF NEQGQVRTLF LKDTHRKALS EGLRRRFIFA GFMNIFVAPF IVVYFMMHYF
FRYFNEYKKN PSQIGSRQYT PLAEWKFREF NELWHLFERR INMSYPFASR YVDQFPKDKT
VQVAGFVAFV SGALASVLAL ASVVDPELFL GFEITHDRTV LFYLGVFGSV WAVARGMVPE
ETNVFDPEYA LLEVINYTHY FPSQWKGRLH SDEVRREFAE LYQMKIVIFL EEILSMIFTP
FILWFSLPRC SDRLIDFFRE FTVHVDGMGY LCSFAVFDFK KGTNVITQGD RREPARQDLR
ADYFATKDGK MLASYYGFLD NYGANPRGAH PSTKRQFHPP PAFPTLGSPS AMDLGHLGDR
ADPPQARPFA GQQSTFGPSR FGPTGLADHG SPAPSMLLDP HHQPSASGFR TAHRTAFSRY
RSSRAAPPIS GAILDDDESP SAPNRNGSAR SAAGAPAPPG GSSGGGVGAS DSNLEDSWRM
NLTGDTDDED AGAGGENADA IAGGAGVLGL IQQFQRVNQD GRGRTAVGL
