ATG9_NEUCR
ID ATG9_NEUCR Reviewed; 908 AA.
AC Q7S4D7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Autophagy-related protein 9;
GN Name=apg-7; Synonyms=atg9; ORFNames=NCU02422;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 atg-2 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 apg-7/atg9-containing vesicles,
CC thereby enabling growth into autophagosomes.
CC {ECO:0000250|UniProtKB:O74312}.
CC -!- PTM: Phosphorylated by apg-1. Apg-1 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; CM002242; EAA30368.1; -; Genomic_DNA.
DR RefSeq; XP_959604.1; XM_954511.2.
DR AlphaFoldDB; Q7S4D7; -.
DR SMR; Q7S4D7; -.
DR STRING; 5141.EFNCRP00000003157; -.
DR PRIDE; Q7S4D7; -.
DR EnsemblFungi; EAA30368; EAA30368; NCU02422.
DR GeneID; 3875751; -.
DR KEGG; ncr:NCU02422; -.
DR VEuPathDB; FungiDB:NCU02422; -.
DR HOGENOM; CLU_006200_1_1_1; -.
DR InParanoid; Q7S4D7; -.
DR OMA; FSRTLEW; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; IEA:UniProtKB-KW.
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: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: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; Glycoprotein;
KW Golgi apparatus; Lipid transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..908
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119834"
FT TOPO_DOM 1..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..259
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 434..454
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 455..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..555
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 623..643
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 644..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 64..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 908 AA; 102641 MW; 72998EB6613009AF CRC64;
MADGVIARLM SGGRGARSFY EELRGRDNVS DVDDRAGLLD EENLNQHFND YDLENAEGLR
LEDSRATVDG RIPRGRAQLS GRPPRPAATT HWGTSHDDDG DNDVPASLLV ERYDRGAAPL
GSPGKPRSQH AGSRAHPAPG LSKGRTHQQR PHIDQELQPP LHSDAAPSSL LAGAITGNAK
KMAEWRWANI TNLDSFMQDV YSYYRGSGMW CIVVERVLHL IKVAFVAFLL TFLSQCVDFK
KIPSNQKLSQ VLVPQCTRNM SGLWNIGLWL FAFYFMWKSI QYILDLRRLT HVRDFYIHLL
NIPDEDMQTI TWQEVVARIM VLRDQNVRTT RTITPQNQRW VLGSQSKERL DASDIANRLM
RRENYMIAMI NKDILDLTIP LPILRNRQLL SQTLEWTLMF SILDFVFDPK GQVHQEFLRS
DRRGILSAKL RSRFIFAGVM ILILSPFVAG YLIIVYFLEY YNEIQKNPSI LSARSYTPLA
EWKFREFNEL PHLFKRRLDM SHPFASHYID QFPKAKTSMV AKTVSFIAGS IATVLALISV
FDPEMFLGFE ITHDRTVLFY TAVFGAIWSV ARGSVSEDNA VFDPEYALGN VVEYTHYQPE
HWKDRWHSAD VKAEFEELYK LKLVIFIEEI LSILTTPFVL FFSLPKSADQ IIDFFREFTI
HVDGLGYVCY FAEFDFKKGS KSQAPAATAG EGDVRDDYYS TKHGKMEASM YGFINNYARN
PKHLPPAMRQ QFHLPPVFPG ITSPTLAGDL AASRMGRSQR GRSKGPLPSR TPRPGAVMAE
PSPMASILLD PRHQPIFPNN MSFVNTGHQF RGGNQGDGHM MGGGSMEEDV KGAARHGQQT
HDDESEDSRA GLDESAWQVS PTKDLSRENS GRGLDSVVGE EAGNGAGVVH MLYQFNQAHL
NRRLGGVR
