ATG9_PICPA
ID ATG9_PICPA Reviewed; 885 AA.
AC Q876N4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Autophagy-related protein 9;
DE AltName: Full=Glucose-induced selective autophagy protein 14;
GN Name=ATG9; Synonyms=GSA14;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chang T., Thomson J.M., Dunn W.A. Jr.;
RT "Gsa14 is a membrane protein required for pexophagy and autophagy in Pichia
RT pastoris.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=11533052; DOI=10.1074/jbc.m104087200;
RA Stromhaug P.E., Bevan A., Dunn W.A. Jr.;
RT "GSA11 encodes a unique 208-kDa protein required for pexophagy and
RT autophagy in Pichia pastoris.";
RL J. Biol. Chem. 276:42422-42435(2001).
RN [3]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16874040; DOI=10.4161/auto.1.2.1840;
RA Reggiori F., Shintani T., Nair U., Klionsky D.J.;
RT "Atg9 cycles between mitochondria and the pre-autophagosomal structure in
RT yeasts.";
RL Autophagy 1:101-109(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=16079180; DOI=10.1091/mbc.e05-02-0143;
RA Chang T., Schroder L.A., Thomson J.M., Klocman A.S., Tomasini A.J.,
RA Stromhaug P.E., Dunn W.A. Jr.;
RT "PpATG9 encodes a novel membrane protein that traffics to vacuolar
RT membranes, which sequester peroxisomes during pexophagy in Pichia
RT pastoris.";
RL Mol. Biol. Cell 16:4941-4953(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 (By
CC similarity). Essential for the formation of the sequestering membranes
CC and assembly of the micropexophagy-specific membrane apparatus (MIPA)
CC which mediates the fusion of the sequestering membranes and
CC incorporation of the peroxisomes into the vacuole during micropexophagy
CC (PubMed:11533052, PubMed:16079180). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:11533052, ECO:0000269|PubMed:16079180}.
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:0000269|PubMed:16079180}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:16079180}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16079180}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:16079180}. Vacuole membrane
CC {ECO:0000269|PubMed:16079180}; Multi-pass membrane protein
CC {ECO:0000303|PubMed:16079180}. 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}. Note=The peripheral pool of ATG9
CC partially colocalizes with mitochondria and it has been speculated that
CC ATG9 resides either in the mitochondria or within vesicles in very
CC close to the mitochondria. During methanol growth, localizes to
CC multiple structures situated near the plasma membrane referred as the
CC peripheral compartment (Atg9-PC). During glucose-induced
CC micropexophagy, traffics from the Atg9-PC to unique perivacuolar
CC structures (PVS) that contain ATG11, but lack ATG2 and ATG8.
CC {ECO:0000269|PubMed:16079180}.
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; AY075105; AAL77196.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876N4; -.
DR SMR; Q876N4; -.
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:0005774; C:vacuolar 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; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..885
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119835"
FT TOPO_DOM 1..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..279
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 439..459
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 460..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..555
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 626..646
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 647..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 49..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 102597 MW; B7853F8E91F78187 CRC64;
MHKNNTTFLS RVFGINSRNI DVHNPLFADD SVIPLYDQNQ SAYYDNAYSD YSSDEEDSKP
RTSRQTDSNL HMTDHSGDGN DPFNQMDNSS RFSNSSSFHY NNTDQEDDNP ELLLLQDEDS
SLNRKNLDNS DFQSFAKKTF NQIPKIKFQL PKKEDYPTSH RQPPDIENQN GTLKSSVKKQ
IHFLDPMDKA LWMWSNVSNL DTFLHQVYDY YTGNGFNCIM MNKFTELFTV VFIVWLFSFM
GNCIDYDKLM NDRNVYQFSQ VKIDKCYSKI GFFPQKLIYW LFFIGLCLKL YQIFLDYLVL
KDMKLFFNLL LGLSDDELQT ISWGLVVKRI MILRDKNINA IVSQNTDLTS RKRMNAHDIA
NRILRKENYM IAMYNKSILD LDIELPLIGK VQLLTNTLQW NLNIAILDYF FDSETGQINL
PALKERNRHT ISTELKKRLI FCGIINIVLA PILSIYFIMY YFLKFFYDFK TNPADISSRE
YSPYARWKLR EFNELPHIFN RRLNISTESS NKYINQFPKE TTTALLKFIM FISGSIVGVL
VIVTILDPEF FLNFELTPGR TVLFYVSTLG AIFTICKNSI PDDTLVFDPE VSLRYLSQFT
HYLPQEWEGK YHTEEVKNDF CKLYTLKLYL VGKEILSWLF LPYILCYKLP ECADTISDFF
REFSVHVDGL GYVCTFAMFQ FNNQHNENGN ANVHQNGNGN GGVPSAKSKS KKVPNPNRFT
TKPSMRDMEN DDKMIKSYMY FLESYGNDEI VQHQQALNRS LIYSTEISPT SGDDLNDSNI
LGLRQRNVAT TGKRQNSIGN GLIYNGQNKR LSIGEAKTNV YSNPIASTVL DKDLQYKLAN
SYILNGMPGL NEANQPADRK NERKYSNDSP GVMKLVDKIS QQHKA
