ATG9_DEBHA
ID ATG9_DEBHA Reviewed; 905 AA.
AC Q6BW58;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; OrderedLocusNames=DEHA2B14168g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382134; CAG85572.2; -; Genomic_DNA.
DR RefSeq; XP_457561.2; XM_457561.1.
DR AlphaFoldDB; Q6BW58; -.
DR SMR; Q6BW58; -.
DR STRING; 4959.XP_457561.2; -.
DR PRIDE; Q6BW58; -.
DR EnsemblFungi; CAG85572; CAG85572; DEHA2B14168g.
DR GeneID; 2913524; -.
DR KEGG; dha:DEHA2B14168g; -.
DR VEuPathDB; FungiDB:DEHA2B14168g; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; Q6BW58; -.
DR OMA; ELMTISW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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..905
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119830"
FT TOPO_DOM 1..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..272
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 464..484
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 485..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..588
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 666..686
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 687..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 55..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 104615 MW; 3ECDE012B18F77AF CRC64;
MSEYNQNSNN DTFLSRVFGL HSVYNQLQDE YQYYDPDVDY QQSFMNGGVL SSHVREEGNE
NTNNDNTNLL DSESDSDSSS SLSSPPSPIV SFTGKEHNQN EDSTKVHWDT TRPHYGQDND
ITTSIPKDPP KKNMVNTAKN FINKLHPATD SLPMYNQPQQ FRKPPPEGPS VQTVYQKKQH
KSKRKYVIPP KERALYLWAN ITNMDEFLTD VYYYYRGNGM LNIVLTRLVD LLILAFILSF
TVFLKWGINY DFFMSSSSDR ASVTLKDLVI PNFISEMVPV SVKLLLLGFS GYIVLRLVQL
YFDYNYKLKE IKNFYHYLIG IPNDDELMTI SWIVIVERLM ALKDYNSLTS TNTNLPAQFL
SDLNSKVRLN AHDIANRIMR KENYIIALIN KEVLDLSLSI PFLSNVNSFL SNKSVLTKTL
DWNIKLCINN FIFNQHGQIN SHVLKDFNRN QLSKELSARF KMAAIINLLL CPFIVIYFVL
LYFFRYFNEY KSNPSSILGL RQYTPWAEWK LREFNELPHF FIKRLHLSIG PANIYINQFP
RGFWVINLMN FVNFVSGAIT AILVLMGLWF DNEEHNFWSF EITENKSSLF YISLFGTVWA
ITSSSLTSTN SNTSENLNSQ TSSFFYDPEA SLRYVSQFTH YLPSSWNGRL HTVQVKNEFC
ELFSMKIIII INEILSLILT PFILWFKVSN SSGAIIDFFR EYSIHVDGLG YVCYFAMFNF
EQKDKNMMMS LNKSKKRKPR KSRANAKKKA SSKSKSRSDE IELDNVNSNK ADKSKLSDSE
TSSNSDDNDD TDINNDYYQD DKMIKSYMYF LETCGNDKAK QASKLTSNEQ LSTKPSRIAK
PDNSQSVVGD PTPSFLYQPL TSNSIDDSSY NINYNIDEQE EESSKGKRSG VLGMINQFYK
HDRNR
