ID   ATG9_CRYNB              Reviewed;         879 AA.
AC   P0CM41; Q55UN1; Q5KHR3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Autophagy-related protein 9;
GN   Name=ATG9; OrderedLocusNames=CNBD0770;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL21381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAEY01000019; EAL21381.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_776028.1; XM_770935.1.
DR   AlphaFoldDB; P0CM41; -.
DR   SMR; P0CM41; -.
DR   EnsemblFungi; EAL21381; EAL21381; CNBD0770.
DR   GeneID; 4935466; -.
DR   KEGG; cnb:CNBD0770; -.
DR   HOGENOM; CLU_006200_3_0_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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; Glycoprotein;
KW   Golgi apparatus; Lipid transport; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..879
FT                   /note="Autophagy-related protein 9"
FT                   /id="PRO_0000410022"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        385..405
FT                   /evidence="ECO:0000250|UniProtKB:O74312"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        555..575
FT                   /evidence="ECO:0000250|UniProtKB:O74312"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   879 AA;  99290 MW;  CE9AB3018C711165 CRC64;
     MGKGEGYLDP TILSVASGSR NSGKGKERTR RKGGHKYHSL HVQDEEEEEP PESDALRTRG
     KVGLNAYEKA LWKWVNVDDL DGFLQEVYDY YKGKGIYCIV LARVLNLLTT FFVIAFSTFL
     ISCIDYSKLF SSISTAEAVG RLEDVLVAQC ITKFVHFKLY ILNKTNSSAY DYRGSFAHTL
     FLIILSAFFI FQVASFAMSV PRLLDMYRFY THLLGVPDAD IQTLPWPEIV RLIGDIRKHN
     PVTSLSNGQA TALADMVGND AKAPAKKLDA HDIANRILRQ ENYLIALFNK DLLDLRVRIP
     VPHVLTAFIP SSILISSADA PLPSLQSEPE RKFLSFGANH LTKALEWNLR FCLLGYLFDR
     RGQVRKEFVR EKRRKDLVQG LRRRFIFMGI LNAIFAPFII LYLLIYSFFR YFEWKFREFN
     ELPHLFERRL DRSYEIAKEY VDQFPKERTA LVMRFVAFIA GSFAAVLLVA SLIDPDLFLH
     FEITPHRTVL FYLGVFGSIL AISRGMVPQE NMVFDPEASL NEVVRWTHYL PVEWRGQLHS
     QMVHQEFSKL FALKIMIFFS ELLSVILTPF ILFFSLPPCA AAIIDFFREF TVHVDGVGYV
     CSFAVFDFAR YGNVDANQPE TGLEGATGPD GGPAADGFAA GKPSRPTTRR TTSSSPSRLK
     HRDWRGNENK MEQSFLHFKA THPDWQPSDP SSSLFLDRLM GAGTRNRHGG GPVSAATGGI
     SGSIYGGGGG GVGGRGLGVD GSVMAEMEEE RLRAKRQSYE RAWAKSSHLH RPDSSHSHPL
     RHPHSAASEI IEEEEGGEGD KGDDSIDGWS KRVKTDGETD DEEERERLWK DEGVIIIFFL
     TNNHITVVVM NVCRCIFRVA ADEHKTAGRI NKSQTRRLT