ID   ATG9_CRYGA              Reviewed;         751 AA.
AC   Q6TGJ4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Autophagy-related protein 9;
GN   Name=ATG9; Synonyms=APG9;
OS   Cryptococcus gattii (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=552467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32609 / CBS 6956 / NIH 444 / Serotype B;
RX   PubMed=15567176; DOI=10.1016/j.bbrc.2004.11.017;
RA   Ren P., Roncaglia P., Springer D.J., Fan J., Chaturvedi V.;
RT   "Genomic organization and expression of 23 new genes from MATalpha locus of
RT   Cryptococcus neoformans var. gattii.";
RL   Biochem. Biophys. Res. Commun. 326:233-241(2005).
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; AY421966; AAS92527.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6TGJ4; -.
DR   SMR; Q6TGJ4; -.
DR   VEuPathDB; FungiDB:CGB_I1270C; -.
DR   VEuPathDB; FungiDB:CNBG_5852; -.
DR   VEuPathDB; FungiDB:I306_06625; -.
DR   VEuPathDB; FungiDB:I308_03655; -.
DR   VEuPathDB; FungiDB:I311_03678; -.
DR   VEuPathDB; FungiDB:I314_03643; -.
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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..751
FT                   /note="Autophagy-related protein 9"
FT                   /id="PRO_0000119828"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..71
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        277..297
FT                   /evidence="ECO:0000250|UniProtKB:O74312"
FT   TOPO_DOM        298..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..398
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..465
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        466..486
FT                   /evidence="ECO:0000250|UniProtKB:O74312"
FT   TOPO_DOM        487..751
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          528..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  84191 MW;  4842F0C6433B886D CRC64;
     MRKLCGNGST SMISTDSYKN TTFFVIAFST FLISCIDYTK LFSSLSTPEA VGRLEDVLIG
     QCITKGSFAH TLFLIILSAF FIFQVANFAM SVPRLLDMYR FYTHLLGVPD ADIQTLPWPE
     IVRLIGDIRK HNPVTSLSNG QATALADMVG NDAKAPVKKL DAHDIANRIL RQENYLIALF
     NKDLLDLRVR IPVPHIFTAF IPSSMLILSA DPPLPSLQSE PERKFLSFGA NHLTKALEWN
     LRFCLLGYLF DRRGQVRKEF VREKRRKDLV QGLRRRFVFM GILNAIFAPF IILYLLIYSF
     FRYFEEYHKN PSSIGSRQYT PYAQWKFREF NELPHLFERR LDRSYETAKE YVDQFPKERT
     ALVMRFVAFV AGSFAAVLLV ASLIDPDLFL HFEITPHRTV LFYLGVFGSV LAISRGMVPQ
     ENMVFDPEAS LNEVVRWTHY LPVEWRGQLH SQMVHQEFSK LFALKIMIFF SELLSVILTP
     FILFFSLPPC AAAIIDFFRE FTVHVDGVGY VCSFAVFDFA RHGNIDSNRP ETGVQGATGP
     DAGDSGGGGG GGGGGFAAGK SGRQTTRRAA SASPSRFKQK DWRSNENKME QSFLHFKATH
     PDWQPSDPSS SLFLDRLMGA GARNRPAGGI SGSIYGGGGG GGGGGGRGLG IDGSVMAEME
     EERLRAKSQS YERAWAKSSH LHRPDISNPL RHPHSAASEI IEEEEGGEGD KGDDSIDGWS
     KRMKTDGESD DEQEEHGRLW KDDGVQIDIK Q