ATG9_VANPO
ID ATG9_VANPO Reviewed; 961 AA.
AC A7TR50;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=Kpol_461p14;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480470; EDO15260.1; -; Genomic_DNA.
DR RefSeq; XP_001643118.1; XM_001643068.1.
DR AlphaFoldDB; A7TR50; -.
DR SMR; A7TR50; -.
DR STRING; 436907.A7TR50; -.
DR EnsemblFungi; EDO15260; EDO15260; Kpol_461p14.
DR GeneID; 5543328; -.
DR KEGG; vpo:Kpol_461p14; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; A7TR50; -.
DR OMA; LGYVCKY; -.
DR OrthoDB; 712239at2759; -.
DR PhylomeDB; A7TR50; -.
DR Proteomes; UP000000267; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..961
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317918"
FT TOPO_DOM 1..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..374
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 537..557
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 558..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..654
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 722..742
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 743..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 110107 MW; 3D3650D011A0B279 CRC64;
MGDSESVNQD HGRNTFLSRV FGLQPDDITT SIRTGDMSRY PLNAYSGGSE MFSGSPTSSR
IDDDDDDDEG RVPESDQQSS SGDNSDDIKA NDDVIEDVEL TDGNGDNYTN SKMINTNYSI
FGSLRKVGQQ SSDEEDDGSL SNEEEDIDEE DEIDEIDADE PLFVNSTSQR KQKRKSSVNF
KNGSEMSSLL FQRILNKKDS KSNGEASNKM FTSSNQGNHN YKYRNGHDLE GGVHFNKKEG
RRNSLFGSHE AGGHKSHNSA PSKGPNLLKN ISILNNTPSN KVYTLSPKER ALWKWANVEN
LDVFLQEVYK YYLGSGFSCI VLRKLLNLTT LIFVVYISTY LGYCIDYSKL PTSSRLSDII
IDQCYTTRIT GITKGLLWVF YVFVGLKVVQ FYFDLQNLTD MHNFYNYLLG ISDNELQTIP
WQNIIQQLMY LKDQNALTAN VVEVKAKNKI DPLVVANRIM RKDNYLIALY NENILDLSLP
IPFYKESILT KTLEWNINLC IIGFAFNESG FIKQSFLKKS QHQFITEELR KRFMLAGFLN
IILSPFLVTY FVLLYFLRYF NEFKTSPGTI GARQYTPMAE WTFREFNELY HIFQKRLGLS
TVIADKYINQ FPKESTDLIL KFISFISGSF VAVLMSLTLL DSENFLNFEV TKDRSVLFYI
TVFGAIWSVC RNSISDEYKV YDPDETIKEL SEFTHYLPKE WEGKHHTEDV KQEFCKLYNI
RLIILLRELA SLVLTPFILW FSLPACSDRI VDFFSDSSTY IDGLGYVCKY ATFGINQANA
QKVKGGKRHQ DMKMNTNNFS NEVINESDED VLDSDSDSEI DSNDKMMRSY MYFMEDYENS
ENAIGKNQLP RKKYKDPSLT NPSLNTDYSW RKQFQPGQRP ELFRIGKHAL QVPTNVRNLG
KKSTLNSENP YDNSSNLGES FINPTIMPDR DLGRNGVNGG KKEAGMLRMV KDYYKTSDIG
R
