ATG9_YEAS7
ID ATG9_YEAS7 Reviewed; 997 AA.
AC A6ZXH8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000250|UniProtKB:Q12142};
DE AltName: Full=Cytoplasm to vacuole targeting protein 7 {ECO:0000250|UniProtKB:Q12142};
GN Name=ATG9 {ECO:0000250|UniProtKB:Q12142};
GN Synonyms=APG9 {ECO:0000250|UniProtKB:Q12142},
GN AUT9 {ECO:0000250|UniProtKB:Q12142}, CVT7 {ECO:0000250|UniProtKB:Q12142};
GN ORFNames=SCY_0766 {ECO:0000303|PubMed:17652520};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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. Recruits
CC vesicle-tethering proteins TRS85 and YPT1 to the autophagosome
CC formation site. Recruits also ATG23 and ATG8 to the PAS.
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. Interacts with ATG23 and
CC ATG27 to form a cycling complex for trafficking to the PAS. Interacts
CC (via N-terminus) with ATG11, required for recruitment of ATG9 to the
CC PAS for the Cvt pathway during nutrient-rich conditions. Interacts (via
CC N-terminus) with ATG17; required for recruitment to the PAS during
CC autophagy and starved conditions. Interacts with ATG2 and ATG18;
CC required for the retrieval of ATG9 from the PAS to the cytoplasmic
CC pool. Interacts with ATG41. Interacts with the conserved oligomeric
CC Golgi (COG) complex subunits COG3 and COG4. Interacts with TRS85.
CC {ECO:0000250|UniProtKB:Q12142}.
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}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Note=The vast majority of ATG9 exists
CC on cytoplasmic mobile vesicles (designated ATG9 vesicles) that were
CC derived from the Golgi apparatus in a process involving ATG23 and
CC ATG27. The peripheral pool of ATG9 partially colocalizes within
CC tubulovesicular clusters adjacent to mitochondria. It appears that
CC membrane that contains ATG9 is delivered to the autophagosome from the
CC Golgi-endosomal system rather than from the ER or mitochondria. Within
CC the PAS, localizes at the edge of the isolation membrane. ATG9 cycling
CC is regulated by at least the conserved oligomeric Golgi (COG) complex,
CC ARP2, HOG1, PIK1, SEC2, SEC9, SSO1 and SSO2.
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; phosphorylation is required for autophagy
CC and cytoplasm to vacuole transport (Cvt) vesicle formation.
CC Phosphorylation by ATG1 regulates ATG18 interaction and
CC preautophagosome elongation. Phosphorylation at Ser-122 is required for
CC selective autophagy by regulating anterograde trafficking and
CC interaction with ATG23 and ATG27. Phosphorylation at Ser-122 prevents
CC ubiquitination by the SCF(MET30) complex.
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- PTM: Ubiquitinated by the SCF(MET30) complex in normal conditions,
CC leading to its degradation by the proteasome, thereby preventing
CC inappropriate induction of autophagy. Ubiquitination by the SCF(MET30)
CC complex is prevented by phosphorylation at Ser-122.
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; AAFW02000145; EDN60208.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZXH8; -.
DR SMR; A6ZXH8; -.
DR PRIDE; A6ZXH8; -.
DR EnsemblFungi; EDN60208; EDN60208; SCY_0766.
DR HOGENOM; CLU_006200_1_0_1; -.
DR Proteomes; UP000007060; 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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 Isopeptide bond; Lipid transport; Membrane; Mitochondrion; Phosphoprotein;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..997
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317919"
FT TOPO_DOM 1..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..376
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 539..559
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 560..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..656
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 724..744
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 745..997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 29..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 794
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 804
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12142"
SQ SEQUENCE 997 AA; 115452 MW; 6275F15EAA206383 CRC64;
MERDEYQLPN SHGKNTFLSR IFGLQSDEVN PSLNSQEMSN FPLPDIERGS SLLHSTNDSR
EDVDENDLRV PESDQGTSTE EEDEVDEEQV QAYAPQISDG LNGDHQLNSV TSKENVLETE
KSNLERLVEG STDDSVPKVG QLSSEEEEDN EFINNDGFDD DTPLFQKSKI HEFSSKKSNT
IEDGKRPLFF RHIYQNNRPQ RDTQKLFTSS NAIHHDKDKS ANNGPRNING NQKHGTKYFG
SATQPRFTGS PLNNTNRFTK LFPLRKPNLL SNISVLNNTP EDRINTLSVK ERALWKWANV
ENLDIFLQDV YNYYLGNGFY CIILEKILNI CTLLFVVFVS TYMGHCVDYS KLPTSHRVSD
IIIDKCYSNS ITGFTKFFLW MFYFFVILKI VQLYFDVQKL SELQNFYKYL LNISDDELQT
LPWQNVIQQL MYLKDQNAMT ANVVEVKAKN RIDAHDVANR IMRRENYLIA LYNSDILNLS
LPIPLFRTNV LTKTLEWNIN LCVMGFVFNE SGFIKQSILK PSQREFTREE LQKRFMLAGF
LNIILAPFLV TYFVLLYFFR YFNEYKTSPG SIGARQYTPI AEWKFREYNE LYHIFKKRIS
LSTTLANKYV DQFPKEKTNL FLKFVSFICG SFVAILAFLT VFDPENFLNF EITSDRSVIF
YITILGAIWS VSRNTITQEY HVFDPEETLK ELYEYTHYLP KEWEGRYHKE EIKLEFCKLY
NLRIVILLRE LTSLMITPFV LWFSLPSSAG RIVDFFRENS EYVDGLGYVC KYAMFNMKNI
DGEDTHSMDE DSLTKKIAVN GSHTLNSKRR SKFTAEDHSD KDLANNKMLQ SYVYFMDDYS
NSENLTGKYQ LPAKKGYPNN EGDSFLNNKY SWRKQFQPGQ KPELFRIGKH ALGPGHNISP
AIYSTRNPGK NWDNNNNGDD IKNGTNNATA KNDDNNGNND HEYVLTESFL DSGAFPNHDV
IDHNKMLNSN YNGNGILNKG GVLGLVKEYY KKSDVGR
