ATG9_KLULA
ID ATG9_KLULA Reviewed; 908 AA.
AC Q6CT08;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; OrderedLocusNames=KLLA0C16357g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382123; CAH01782.1; -; Genomic_DNA.
DR RefSeq; XP_452931.1; XM_452931.1.
DR AlphaFoldDB; Q6CT08; -.
DR SMR; Q6CT08; -.
DR STRING; 28985.XP_452931.1; -.
DR EnsemblFungi; CAH01782; CAH01782; KLLA0_C16357g.
DR GeneID; 2892175; -.
DR KEGG; kla:KLLA0_C16357g; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; Q6CT08; -.
DR OMA; LGYVCKY; -.
DR Proteomes; UP000000598; Chromosome C.
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:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
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..908
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119832"
FT TOPO_DOM 1..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..349
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 508..528
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 529..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..629
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 697..717
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 718..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 37..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 104039 MW; DB62798ECC7295FE CRC64;
MTDSQDKVNG GSKNTFLSRV FGVHSSAVEN SLDAAEMSHI TMPTEQDFSN YAEDEGNVRL
IESDQEPSSS NEDSNDEEPL IQQPQSIRFD TASDGMATIQ SESEPDEGGT EEDEVHLEEE
DFSDQDLASS VSKYGQPSSS EDEEPLSNRD SNRGSDETIP FIGRQRLNLG GKNPITGATK
STKNPSESRV FERLLGNSPA KMFRNNGRPN NLEESFLFRK PSVAEQSGPG KSTHFNLKPP
PIFNNISTLT STSKNSLSSL SPKERALWKW ANIENLDTFL QQVYEYYLGN GFYCIITEKV
IHLATILFVV FISTYMGHCI DYSRLSSSHT FEEIHIEQCY KTQISPTAKV FLWIFYAFIG
LKVLQLYFDV KALKDIRNFY NYLLSISDKD LQTIPWQSVI QQLVLLKDQN AITANATEVK
AKNRLSAHDV ANRIMRKENF VIALYDNNIL DLSLPVPLLR TCALTKTLEW NINLCILGFA
FNEKGYLKQA FLRESQREYL GEELKKRFVL AGFLNIILSP FLVTYFVLLN FFRYFNEYKT
SPGSIGSRQY TPIAEWKFRE YNELYHIFQK RMRLSMIIAD NYVNQFPNTL LSLTLSFIQF
VSGSFVAILG ILTIFDPDNF LNFEITPDRT VLFYMTVFGT LWAVCHSSIN DEYTVLKPEE
TLEELVSYTH YAPKEWKGKY HTEDIKNEFC RLYNLRITLL LRELVSIIIT PFILWFSLPK
NSERIIDFFR ECTVYEEGLG YVCKYAMFEA TKIDKGTKAK KQTKRMFSQA EQDDSETESD
EGVNKMLQSY MYFVDDYKNA GNAVGKNQLP ASPIEPSYHP YSSTKDYSWK TQFALGKNSN
RKRNLNRSRV KRFPDRSSDL ELGSLSGSLI NKSTLFKDDI ADNADELKAG NGVMGLLNQY
YKKSDRNR
