ATG9_ASPOR
ID ATG9_ASPOR Reviewed; 951 AA.
AC Q2UUT6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=AO090009000183;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007150; BAE54679.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UUT6; -.
DR SMR; Q2UUT6; -.
DR STRING; 510516.Q2UUT6; -.
DR EnsemblFungi; BAE54679; BAE54679; AO090009000183.
DR HOGENOM; CLU_006200_1_1_1; -.
DR OMA; FSRTLEW; -.
DR Proteomes; UP000006564; Chromosome 1.
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..951
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317908"
FT TOPO_DOM 1..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..288
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 456..476
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 477..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..577
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 645..665
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 666..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 108226 MW; 5083844480C37337 CRC64;
MMTSNILSRF LPPNGSPSVY ETLRQQDAES NPSDVEERAG LEFEDDRRTQ FSDRELEEAM
VDAARDGIRS PSPSPSEPFL TQRSPQRTSG TATAKTGGRR RKHSRPRWMH QDPDDGDDDV
PPSLLVEGHQ DDDEMRSRLP PPPPSHRHPQ RELSPAPGPS SRADRARWNT TREQLPLHND
GRGQRPGVIW SLGHPNLASV DPKEKAMWLW ANVENLDNFL KDVYTYFLGN GIWSILLNRG
LSLLTFAFVV GFSTFLTNCI DYRNFRGSRK MDDILIQQCT KKMSMSSTFL LWLLTVFWIG
KAFQYLMDIR RLKHMHDFYY YLLGISDSEI QTISWQEVVS RLMTLRDANP ATAGAVSARH
RKFMGSQSKQ RMDAHDIANR LMRKENYLIA LVNKDILDLT LPIPFLRNRQ LFSQTLEWNI
NLCIMDYVFN DQGQVRTLFL KDTHRKALSE GLRRRFIFAG IMNIFVAPFI VVYFLMHYFF
RYFNEYKKNP AQIGSRQYTP LAEWKFREFN ELWHLFERRV NMSYPFASRY VDQFPKDKTV
QVAGFVAFVS GALASVLALV SIIDPELFLG FEITHDRTVL FYLGVFGSVW AFARGLVPEE
TNVFDPEFAL LEVIDFTHYF PNHWKGRLHS DEVRKEFAVL YQMKIVIFLE EILSMIFTPF
ILWFSLPKCS DRLIDFFREF TVHVDGMGYL CSFAVFDFKK GTNVISQGGT GRRESGRQDL
RADYFSTKDG KMLASYYGFL DNYGGNRPAN PSSRRQFHPP PAFPTLGSPS AIEMGNIGER
LERTQTRHGP AATFMGQQSG LGPGFGAAGF GDHASPAPSI LLDPHHQPTA SDFRTANRSA
LYPRFRSSRP VRPITDPIED DNESPSAEIR RGAVKKSPHT TTGSSGGAIG TSDSNLGESW
RMNLIGDELD KDTGEDGENV DEIAGNAGVL GLIQQFQKVS KDNRGRTTVG I
