ATG9_PICGU
ID ATG9_PICGU Reviewed; 808 AA.
AC A5DEX5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=PGUG_01826;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408156; EDK37728.2; -; Genomic_DNA.
DR RefSeq; XP_001486155.1; XM_001486105.1.
DR AlphaFoldDB; A5DEX5; -.
DR SMR; A5DEX5; -.
DR STRING; 4929.XP_001486155.1; -.
DR EnsemblFungi; EDK37728; EDK37728; PGUG_01826.
DR GeneID; 5127568; -.
DR KEGG; pgu:PGUG_01826; -.
DR VEuPathDB; FungiDB:PGUG_01826; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; A5DEX5; -.
DR OMA; ELMTISW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000001997; 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: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 Lipid transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..808
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317914"
FT TOPO_DOM 1..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..258
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 434..454
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 455..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..557
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 634..654
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 655..808
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 51..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 93175 MW; 4BE3A00843BBCE32 CRC64;
MPDVHLSSSF AEGNTSEQNE NDTFLSRIFG FHSIYNQLDN YQYYDPESQV GDSMIRRDGG
SNHLLDSESD SDLSSIESSS SSQDQPPSIH ANDIQMQPYE PPTQPYGEID PQPQNAPIMT
ESAPSHGILN NGAVSTDEAQ VQFRKTKTLP SFHTMYQRQA RGRVFIPSRE RALYLWANIV
NMDEFLSDLY YYYRGRGVMN IVLGRIVDLA TLVFVIGFAS FLAWGVDYDK FLSRGQKSLT
LSDLIIPHYI SKAPAMAKLL LFGFAIYITL RIVQLYFDFR YKLSEIRNFY RQLLDIPHDD
ELMTISWATI VERLMELKDF NTLTSSSHYV NDLKSKVRLN AHDIANRIMR KENYIIALIN
KDTLNLGFEI PLLSVLNPIL NTRAVLTRTL EWNLKLCIYN FVFNNQGQVN PNVLKDYNRN
MLAKELSSRF KMAAIINLLL CPFIVVYFVL LYFFRYFNEY KTNPSSLIGL RQYTPWAEWK
LREFNELPHF FVKRLQLSIG PANTYINQFP RGFLVVNIMT LVNFVAGAIT AVLVVMGLWF
EDEEHSFWAF ELTENKSALF YISIFGTIWA VTAGSLATDT SSTESANSSS PFYYDPEASL
RYVTQFTHYM PSTWSKKLHT AEVKGEFCEL FSLKIVVIIN ELLSLVLTPF ILWFKLSSQS
GAIIDFVREY SVYVDGLGYV CYFAMFNFEK KDKNMMHDLN KKKKKSPSHR TKRDDIEEEE
ESDNGVPNGD DKMIKSYMYF LESYDDRERA ARPTPKSRQL PRTRLPPGSI SESTYNVDHI
LEEEELPQGK SAGVFGMINQ FYKQDLGR
