ATG9_COCIM
ID ATG9_COCIM Reviewed; 931 AA.
AC Q1E6Q3; J3KK85;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=CIMG_01760;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS36406.3; -; Genomic_DNA.
DR RefSeq; XP_001247989.1; XM_001247988.2.
DR AlphaFoldDB; Q1E6Q3; -.
DR SMR; Q1E6Q3; -.
DR STRING; 246410.Q1E6Q3; -.
DR EnsemblFungi; EAS36406; EAS36406; CIMG_01760.
DR GeneID; 4566782; -.
DR KEGG; cim:CIMG_01760; -.
DR VEuPathDB; FungiDB:CIMG_01760; -.
DR InParanoid; Q1E6Q3; -.
DR OMA; FSRTLEW; -.
DR OrthoDB; 712239at2759; -.
DR Proteomes; UP000001261; 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; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..931
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317909"
FT TOPO_DOM 1..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..271
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 439..459
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 460..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..560
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 628..648
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 649..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 62..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 105882 MW; 839CF2449E543541 CRC64;
MTSQLITRLL PINSTTSPSI YETIRQYDDD SGHSDTEERA AMAVDEENLD GAYQDYELEG
ALAQASDTQS THSSFQSPAA GDSHLPRHPK WTQESVNEAE HDDEVPASLL VEGDGEEDPL
PPPPRPPSNR NRILDDAPAA EFCSPRLRGQ WEAAEEHQTP HLAPQPSPPL NLHSNRRAGL
AFANPKEKAM WRWANVENLD NFLKDVYIYF IGNGIWCIVL SRMLNILTLA FVVGFTTFLT
NCVDYRKVPH SKTLNQIIVP KCTNKMSASS TFFLWLFTVF WFGKVFQYII DFRRLRHMHD
FYLYLLDVPD SDIQTISWQE VVGRLMALRD ANPATAGTVS TKHRKYIGSQ SKQRMDAHDI
ANRLMRKENY LIALFNKEIL DLTLPIPFLR NRQLFSRTLE WNLNLCILDY VFNEQGQLRP
LFLKATHRRA LSEGLRRRFI FAGVMNIFIA PFIVAYFLMH YFFRYFNEYQ KNPSKIGSRQ
YTPLAEWKFR EFNELWHLFE RRIHMSYESA NMYINQFPKD KTVQLSRFVA FIAGALLSVL
ALASVIDPEL FLGFEITHDR TVLFYIGLFG TVYAVARGVV PDDAQVFDPE HALLDVTAYT
HYKPAHWQGK LHSDDVRKEF ATLYQLKVVI FLEEILSMIF TPFVLWFSLP KCSDRLIDFF
REFTVHVDGL GYVCSFAVFD FKKGTNLMPP EPQHHRPRGL KHGLHDLRGD YFSAKDGKML
ASYYGFLDHY APPARPSGPH ASQRQNYPQQ PVPGPTHRAQ PGANHLHSSR IDRWDNGQHS
TMRQSALRTS RFGAITGVGG HASPMASMLL DPHHQPSMSG FRSKAHPTAA SRYRPSRQAH
PMADTIQDVD EDQLPGINIQ PSNVTTTSSG GPATDDSQIE ESWRINLAED ANSGEDDEAE
DVEKVAGGGG VLGLIHQFQK VTNEGRGAVG M
