ATG9_PICST
ID ATG9_PICST Reviewed; 916 AA.
AC A3LZS3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=PICST_64286;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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.
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; CP000502; ABN68594.2; -; Genomic_DNA.
DR RefSeq; XP_001386623.2; XM_001386586.1.
DR AlphaFoldDB; A3LZS3; -.
DR SMR; A3LZS3; -.
DR STRING; 4924.XP_001386623.2; -.
DR EnsemblFungi; ABN68594; ABN68594; PICST_64286.
DR GeneID; 4841042; -.
DR KEGG; pic:PICST_64286; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; A3LZS3; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
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..916
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317915"
FT TOPO_DOM 1..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..293
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 482..502
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 503..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..605
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 682..702
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 703..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 105558 MW; F451C82B589B3FFA CRC64;
MSRNSPLQSG QRGPPNGSPY PDSSQNNDTF LSRIFGLNSV YNHLQENYQY YDPEFDSTYN
QQVLANSQRQ DYDLFGNGLD KTNLLDSESD SDLSSSSSAS PSVVVKPRFK RTEASDNEDD
EVDDLLTSLS KPRSSPPRRK PTFNIPNARD IFSANGNTQA TSVLPLYNQK YRKPVERDTG
ASAGDSRGYA NSGIRRTNGT RFVIPPKERA LYLWANITNM DEFLTDLYYY YRGKGMLNIV
LSSIIDLLIL VFILGFTVFL KWGINYRYFF DNYKDSTYIT LADLIIPNFL VDEVPLLAKF
FLFGFVCYIV LRLIQLYFNY NYKLKEIKNF YKYLINISND DELMTITWKT IVERLMLLKD
YNSLTSTTSH FDGATDHYIN DLNSKVRLNA HDIANRIMRK ENYMIALINK DVLDLSLSPF
QNSSFQLINN KSVLTKTLEW NLKLCINNFA FNNEGQINPS ILKDFNRNQL AKELNSRFKM
AAIINLILCP FIVIYFVLLY FFRYFNEYKS NPASIMGLRQ YTPYAEWKLR EFNELPHFFI
RRLQLSVGPA NTYINMFPRG FLVINLMNLV NFISGAIMAI LVIMGLWFED ENHSFWSFEL
TEGKSTLFYI SIFGTLWAIT STSTSTSDTA DNLNPNSHSF VYDPEASLRY VSQFTHYLPS
SWNRRLHTVE VKNEFCELYS LKIIIILNEI FSLILTPFIL WFRASSSSGA IIDFFREYSI
HVDGLGYVCY FAMFNFEEKD KNMMFDLNKR KGKSKRSRRS KTSKTSSKKT VNEIELNNIK
SKRREKAKIS DSEDASSLPN TSDDESGNDL NADTYQDEKM IKSYMYFLES YGAGKADVRA
INSNNKLLAK NSVISNIDPS PSLIIQGPSD NHSLLDSAYN INYKFDDAEQ EESTRPGKKS
GVLGMINQFY KQDLGR
