ATG9_CANAL
ID ATG9_CANAL Reviewed; 952 AA.
AC Q5ANC9; A0A1D8PK44;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; OrderedLocusNames=CAALFM_C305040CA;
GN ORFNames=CaO19.13395, CaO19.5974;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=17185534; DOI=10.1099/mic.0.2006/001610-0;
RA Palmer G.E., Kelly M.N., Sturtevant J.E.;
RT "Autophagy in the pathogen Candida albicans.";
RL Microbiology 153:51-58(2007).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation (PubMed:17185534). Cycles
CC between the preautophagosomal structure/phagophore assembly site (PAS)
CC and the 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:17185534}.
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; CP017625; AOW28519.1; -; Genomic_DNA.
DR RefSeq; XP_723185.1; XM_718092.1.
DR AlphaFoldDB; Q5ANC9; -.
DR SMR; Q5ANC9; -.
DR BioGRID; 1218333; 1.
DR STRING; 237561.Q5ANC9; -.
DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PRIDE; Q5ANC9; -.
DR GeneID; 3635239; -.
DR KEGG; cal:CAALFM_C305040CA; -.
DR CGD; CAL0000185873; ATG9.
DR VEuPathDB; FungiDB:C3_05040C_A; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; Q5ANC9; -.
DR OMA; ELMTISW; -.
DR OrthoDB; 712239at2759; -.
DR PRO; PR:Q5ANC9; -.
DR Proteomes; UP000000559; Chromosome 3.
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; ISS:CGD.
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:0006914; P:autophagy; IMP:CGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:CGD.
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..952
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119826"
FT TOPO_DOM 1..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..308
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 491..511
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 512..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..614
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 703..723
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 724..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 110751 MW; C37B451E8DE96250 CRC64;
MSSSSYNPYK NNVNDRLINN STDSFQDNDQ GIPNNNDTFL SRIFGLNSIY NQLQDNYQYY
DPEFDSSLNQ QLQQSIQEND EAEDESLLPQ HQQQQQQAAP MDLSIQDKSA KQKSKSSSLL
NSDSDSDLSS SEDSYVRPNI PQIPSTPIET ENQGSSSKIK FSIPQRAKNF VGKLHPHHEP
TLPVYQTPQE FRRNLPQQQR ASATVNTNYQ RTRNNNRRFI IPPKERALYL WANITNMDEF
LSDVYYYYRG RGLLNIVLSR GFDLIILIFI LIFTVFLKWG IDYSIFFDNL HQEESKHITL
NDMIIPNYFA TIPLSIKFIL FGFSVYILLR SVQLYLDYNY KLKELKNFYH YLLDVTDDEL
MTISWKTIVE KLMLLKDYNS LTSTTKSNNF SENHYVNDLS SKVRLNAHDI ANRIMRRENY
MIALINKDIL DLSVLFMNEK SLLTKTLEWN LKLCIDNFIY NQQGQINGKI LKEYNRNQLA
RELTSRFKLA AIINLILSPF IVIYFVLLYF FRYFNEYKSN PASILGLRQY TPYAEWKLRE
YNELSHLFNK RLIMSMGPAN TYIDQFPKGF LVVNLMRLIN FISGSILAVL VIMGILLEDE
NHSFWSFEIT DGRSALFYIS IFGTIWAITA SSATGTSHES TISTTSQSSN SNSNSNAAST
FVYDPEASLR YVAQFTHYLP SSWNKKLHTI QVKNEFCQLY CLKIIIIINE ILSSVLTPFI
LWFKISHNSG NIIDFYREYS IHVDGLGYVC YFAMFNFEEK DKNMMSDLNK SKKRRKRMKN
KMNKYGKTKM VNPISGKTVN SEIEMTKISK SESERSSDDE SGNEQDYDND EELDYLSYKK
DDKMIKSYMY FLESYGGSKQ PQPQPPQQQQ HPQNQNQTVG GLRNRNPIQS IDPAIMTGNY
YDQQSLNSSI YNINYKFDDS GLLQDETMNS SSRKKGGVLG MLNQFYKQDI NR
