ATG9_DICDI
ID ATG9_DICDI Reviewed; 699 AA.
AC Q54NA3; Q86CR7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Autophagy-related protein 9;
GN Name=atg9; Synonyms=apg9; ORFNames=DDB_G0285323;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AX3 / DH1;
RX PubMed=12626495; DOI=10.1074/jbc.m212467200;
RA Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., Kessin R.H.;
RT "Macroautophagy is required for multicellular development of the social
RT amoeba Dictyostelium discoideum.";
RL J. Biol. Chem. 278:17636-17645(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP INDUCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20070309; DOI=10.1111/j.1462-5822.2010.01432.x;
RA Tung S.M., Unal C., Ley A., Pena C., Tunggal B., Noegel A.A., Krut O.,
RA Steinert M., Eichinger L.;
RT "Loss of Dictyostelium ATG9 results in a pleiotropic phenotype affecting
RT growth, development, phagocytosis and clearance and replication of
RT Legionella pneumophila.";
RL Cell. Microbiol. 12:765-780(2010).
RN [4]
RP FUNCTION.
RX PubMed=22575510; DOI=10.1016/j.bbrc.2012.05.006;
RA Pflaum K., Gerdes K., Yovo K., Callahan J., Snyder M.L.;
RT "Lipopolysaccharide induction of autophagy is associated with enhanced
RT bactericidal activity in Dictyostelium discoideum.";
RL Biochem. Biophys. Res. Commun. 422:417-422(2012).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy by mediating
CC autophagosomal membrane expansion. Cycles between the preautophagosomal
CC structure/phagophore assembly site (PAS) and the cytoplasmic vesicle
CC pool and supplies membrane for the growing autophagosome. Lipid
CC scramblase activity plays a key role in preautophagosomal
CC structure/phagophore assembly by distributing the phospholipids that
CC arrive through ATG2 from the cytoplasmic to the luminal leaflet of the
CC bilayer, thereby driving autophagosomal membrane expansion (By
CC similarity). Required for lipopolysaccharide (LPS)-enhanced bacterial
CC clearance through the autophagic pathway (PubMed:12626495,
CC PubMed:22575510). {ECO:0000250|UniProtKB:Q7Z3C6,
CC ECO:0000269|PubMed:12626495, ECO:0000269|PubMed:22575510}.
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:Q7Z3C6};
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:Q7Z3C6};
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:Q7Z3C6};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:20070309}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20070309}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:20070309}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20070309}.
CC -!- INDUCTION: Expression is up-regulated during development and Legionella
CC infection. {ECO:0000269|PubMed:20070309}.
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:Q7Z3C6}.
CC -!- DISRUPTION PHENOTYPE: Displays severe developmental defects as well as
CC a strong phagocytosis defect. {ECO:0000269|PubMed:20070309}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39079.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY191016; AAO39079.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAFI02000079; EAL64736.1; -; Genomic_DNA.
DR RefSeq; XP_638277.1; XM_633185.1.
DR AlphaFoldDB; Q54NA3; -.
DR SMR; Q54NA3; -.
DR STRING; 44689.DDB0191423; -.
DR PaxDb; Q54NA3; -.
DR EnsemblProtists; EAL64736; EAL64736; DDB_G0285323.
DR GeneID; 8625085; -.
DR KEGG; ddi:DDB_G0285323; -.
DR dictyBase; DDB_G0285323; atg9.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_3_1_1; -.
DR InParanoid; Q54NA3; -.
DR OMA; TVQNTHY; -.
DR PhylomeDB; Q54NA3; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR PRO; PR:Q54NA3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:dictyBase.
DR GO; GO:0005815; C:microtubule organizing center; IDA:dictyBase.
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:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0090382; P:phagosome maturation; IMP:dictyBase.
DR GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IGI:dictyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:dictyBase.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0048837; P:sorocarp sorus development; IMP:dictyBase.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasmic vesicle; Glycoprotein; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..699
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000327585"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..139
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 300..320
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 321..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..420
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 488..508
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 509..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 699 AA; 81314 MW; 1D24435E8097EE2A CRC64;
MSHEDRGGDY YPMMDDPEDR NFIQAKYPNS TGHMSSGGGS NHMSFDDNHG IEMLRDDEHS
LLHESPVSIP AIHNLDSFLT DVYNYFRGKG FMCIFFNDLF ELVSSLFVVL FFTFLVCFVD
YSKLFSEQMP PPALRESVNF SAPIPIWLMV FLVIFSLYWL SKLFSFFSSI KTNWEISSFY
KNTLKINEDD IQTIEWREVV SKIVLVPRLC IVKENMNALD IANRIMRKEN YIIGLINQRI
LNLSIPFPFL RNLTFITKTL EWSLMYSLFN YIFDENGIIK SEFQDPTQRK RLSRGLSRRF
MTIGILGLFT TPFIFFFLLI NFFFEYAEEL KNRPGSLFSR EWSPLARWEF RELNELPHYF
QNRLNLSYSH ANQYVESFPS QMLSTIAKFI SFLFGSVLAV FIVLGIVSDH FIMNYQIFDR
TPIWYIGILG TIVAITRSLI VDENQVFQPA KHMARTVQNT HYLPMSWVGK THTHKVRDEF
LVLFEYRIVD FVRDIFSVLF TPFILIFSLP KSSQAIIDFF GNNTVVLEGV GPICQLGDFS
NIRKLGDNSF GSLNHSQNKI SLTNNAKLEK SIINFKCLNP EWNTDNNELL QNLNEFSKIK
NNNNNNNNNG SNNHIGNHSQ LPTTSVDDFQ FIHDSHYIPH EIIDAVLGTH HHSQQSNNNA
PRFKTGRVDQ NILNAVNDLH QSFYESQYKH KNDNFVNSI
