ATG9_SCLS1
ID ATG9_SCLS1 Reviewed; 944 AA.
AC A7ERK1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; ORFNames=SS1G_07955;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN92093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476630; EDN92093.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001591329.1; XM_001591279.1.
DR AlphaFoldDB; A7ERK1; -.
DR SMR; A7ERK1; -.
DR STRING; 665079.A7ERK1; -.
DR PRIDE; A7ERK1; -.
DR GeneID; 5487317; -.
DR KEGG; ssl:SS1G_07955; -.
DR VEuPathDB; FungiDB:sscle_11g082070; -.
DR InParanoid; A7ERK1; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
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:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..944
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317916"
FT TOPO_DOM 1..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..294
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 463..483
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 484..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..584
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 652..672
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 673..944
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 70..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 106967 MW; B35350BBA2D39ADF CRC64;
MASNLISRLL PSNTQGRSIY DSLRAHDEAS GSDMDVEERA AMAIDEENLR FKDDELGNPA
DVISGESVTE STAFLSDQQQ TPQKQGYNRK GKGKGRSHNL AESPRLLEED SDDDVPASLL
IEGNNRHADP ETPNHIRARQ TALPKRAPAV PGPSAQQIKE ERDRAHWEMT QEQQKLHEDG
GNRATGVPHT PQSIPQNTGF YLTGSPKDKA MYRWVNVTNL DNFIGDLYAY FEGAGIWCIV
LAKVIDILTL VFVAVFTTFL TQCVDYKKIY RGDARSLEYA LVPQCTKKIS GMSNVAIWLV
CLFVLYRVYQ LLTDLPRLMK MRDFFTYLLE IQDSNMQTVS FQDVIARLMA LRDANPMTVE
RISPDNRKFV LGTQSKQRLD AHDIANRLMR KENYLIALFN KEILDLTLPL PFLQGRQLFS
KTLQWNLEWC ILDFVFNDYG QVRQLVLKDS HRRELSDGLR NRFLFAGLMN VICAPVIVIY
VVIVYFFKYF NQYHKNPAAL GSRGYTPLAE WKFREFNELH HLFNKRLNMS YPFASRYLNQ
FPNVKTAHMA KFITFMAGAV VSVLVVATVW DSEVLAGFDI TSERPVLFYI GVFGSLWAIT
NGMIPEENEV FDPEYALRQV IEYTHYMPNH WQDRLHSDEV KREFSTLYQL KLMIFIEEVF
SIIITPFLLW FSLPKCADQI IDFFREFTVH VDGVGYVCSF AVFDFKKGDG RAPTQGKAKS
DMREDYYSTK HGKMAASYYN FLDNYLLNPK TGVPGHNPPG LRQQFYPPPA FPGLISSPTS
GADLQSSRMG RSDVRPMNRA PYVPQQAVRT PRFPSNTTAT GSPMASILLD PRHQPPSSEL
GARSVRRSSR SRYQARRGNN IIEDPMEDEN GPGRPVAQPG RSYAVDDTVA NLGESTWEVS
PAKADADGQD EEEDGDGTGG AGVLGLVYQF QKAQTNGRPG VSIW
