ATG9_YARLI
ID ATG9_YARLI Reviewed; 788 AA.
AC Q6C2F5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000250|UniProtKB:Q12142};
GN Name=ATG9 {ECO:0000250|UniProtKB:Q12142};
GN OrderedLocusNames=YALI0F08349g {ECO:0000303|PubMed:15229592};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382132; CAG77964.1; -; Genomic_DNA.
DR RefSeq; XP_505157.1; XM_505157.1.
DR AlphaFoldDB; Q6C2F5; -.
DR SMR; Q6C2F5; -.
DR STRING; 4952.CAG77964; -.
DR EnsemblFungi; CAG77964; CAG77964; YALI0_F08349g.
DR GeneID; 2908497; -.
DR KEGG; yli:YALI0F08349g; -.
DR VEuPathDB; FungiDB:YALI0_F08349g; -.
DR HOGENOM; CLU_006200_1_1_1; -.
DR InParanoid; Q6C2F5; -.
DR OMA; ELMTISW; -.
DR Proteomes; UP000001300; Chromosome F.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
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 InterPro; IPR018247; EF_Hand_1_Ca_BS.
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..788
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119838"
FT TOPO_DOM 1..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..222
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 391
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 392..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..512
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 580..600
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 601..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 32..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 89850 MW; DFBB77C1D7EE2547 CRC64;
MTDKSTFLSV LFGGGSVYQD LDGDGEVEDA EILRRVEEEH AQTSDNSNSD NDSGNDSDVP
TSLMVEGVQD PKPGSKRRQP HRMATLSNLQ SSAGPGARSV SFAQGTKTQT PIRLTKPTGV
ANGGLPRHKQ DLGASIRTMV DPKELALWKW ANVQNLDNFF AEAYMYYTGK GLVSIILSRV
LNMSTIMFVV VFSTYLGSCI DYSKIKGSRT LDEVHVKQCY AKLGSFHVFV LWTFFVLWFM
KLFQYVKDIR RLVDMKSFYQ ELLEIDENEL QTISWPQVAK RMATLSEANA ATQVGNSTKQ
RIEPHDIANR VMRKENYLVA MFHKRVLNMT VPLPQPLQRI FGRPQLLSRA LEWNLSLCIL
DYVFNPAGQV RPMFLKSTHK QILSTGLRRR FVFAAIMNVV FAPFIILYLA LLYFFRYFNE
YHKNPASIGT RRYNPLAEWK LREYNELPHQ FERRLTLSYI PASKYLDQFP KEKTALVSKF
VSFIAGSFAA VLGIASLIDP ELFLMFEISA NRTVLFYIGV FGSILAVSRS LIPEETLVFD
PEISLRYVAE FTHYLPPEWE GKLHTEQVKN EFSLMYEMRL IILLKELASI FLAPFILYYS
LTQSCDDIVD FIRDHSVHVD GLGYVCTFAM FDFKQKSPDH QPDEDQKMLK SYLYFMDHYG
DKPTNVSQTQ QNVPMYSSVR LKNDGLDLNN SIMQKFQKHN GHHALSGLTQ RDVGLSPAAP
TATTATSGTA TGAAPRRDLI NFDVDESFID QTTSNRDMDN DEQPKDKERV VDMLNQFYKK
TDNMNLGA
