ID A0A3F3RV15_ASPNG Unreviewed; 941 AA. AC A0A3F3RV15; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 27-NOV-2024, entry version 31. DE RecName: Full=Autophagy-related protein 9 {ECO:0000256|ARBA:ARBA00018074, ECO:0000256|RuleBase:RU364027}; GN ORFNames=CAN33_0045060 {ECO:0000313|EMBL:TPR02589.1}; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061 {ECO:0000313|EMBL:TPR02589.1, ECO:0000313|Proteomes:UP000197666}; RN [1] {ECO:0000313|Proteomes:UP000197666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_311 {ECO:0000313|Proteomes:UP000197666}; RA Kerrigan L., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A., RA Nagaraj S., Vavikolanu K., Nadendla S., George J., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00025503}. CC -!- FUNCTION: Phospholipid scramblase involved in autophagy. Cycles between CC the 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. {ECO:0000256|RuleBase:RU364027}. 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:0000256|ARBA:ARBA00024621}; 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:0000256|ARBA:ARBA00024479}; 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:0000256|ARBA:ARBA00024631}; 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:0000256|ARBA:ARBA00024615}; CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms CC a path between the two membrane leaflets. CC {ECO:0000256|ARBA:ARBA00025904}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004439}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004653}. Preautophagosomal structure membrane CC {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004511, CC ECO:0000256|RuleBase:RU364027}. CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000256|ARBA:ARBA00006185, CC ECO:0000256|RuleBase:RU364027}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TPR02589.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NKJJ02000001; TPR02589.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3F3RV15; -. DR SMR; A0A3F3RV15; -. DR EnsemblFungi; CAK47994; CAK47994; An06g01500. DR VEuPathDB; FungiDB:An06g01500; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1114277; -. DR VEuPathDB; FungiDB:ATCC64974_97800; -. DR VEuPathDB; FungiDB:M747DRAFT_281926; -. DR OrthoDB; 5481548at2759; -. DR Proteomes; UP000197666; Unassembled WGS sequence. DR GO; GO:0005776; C:autophagosome; IEA:TreeGrafter. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:EnsemblFungi. 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:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0032258; P:cytoplasm to vacuole targeting by the Cvt pathway; IEA:EnsemblFungi. DR GO; GO:0000423; P:mitophagy; 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; APG9 AUTOPHAGY 9; 1. DR PANTHER; PTHR13038:SF10; AUTOPHAGY-RELATED PROTEIN 9; 1. DR Pfam; PF04109; ATG9; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:TPR02589.1}; KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU364027}; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055, KW ECO:0000256|RuleBase:RU364027}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364027}; KW Transferase {ECO:0000313|EMBL:TPR02589.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU364027}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU364027}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 289..307 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 456..480 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 539..559 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 579..597 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 645..666 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT REGION 1..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 795..889 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..64 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..157 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 869..889 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 941 AA; 106681 MW; B3B11FD93BEAA795 CRC64; MMTSNILSRF LPPNGSPSVY ETIRQHDNHS DASDVEERAG MAFEDEHGDR FSDRELEDAL ADAGRDDSPG PSEPFLPRSP PTKRDEGGFL KAGSRRRKFS RSGRIHAASP RHKFDDSDDD VPPSLLVEGD QDDDDVLRSK LPPPPRSIDP PNVEPPPRPS PRDDRVHWEA ARDRLPLHDT NRRAHHASLW SAGYPNLALV DPKEKALWMW ANVENLDNFL KEVYTYFLGN GIWSILLNRV LSLLTFAFVV GFSIFLTNCI DYHKVRGSRT LDDILIQKCT KQMSMSATFL LWLLSFFWIG KAFQYLLDIR RLKHMHDFYH YLLGISDAEI QSISWQEVVS RLMTLRDSNP ATAGAVSAKH RKFMGSQSKQ RMDAHDIANR LMRKENYLIA LINKDILDLT LPIPFLRNRQ LFSRTLEWNI NLCIMDYVFN EQGQVRTLFL KDTHRRALSE GLRRRFMFAG IMNIFVAPFI VVYFMMHYFF RYFNEYKKNP SQIGSRQYTP LAEWKFREFN ELWHLFERRV NMSYPFASRY VDQFPKDKMV QFAGFVAFVS GALASVLALA SVVDPELFLG FEITHDRTVL FYLGVFGSIW AVAQGLVPEE TNVFDPEYAL LEVINFTHYF PGHWKGRLHS DDVRKDFAVL YQMKIVIFLE EILSMIFTPF ILWFSLPKCS DRLIDFFREF TVHVDGMGYL CSFAVFDFKK GTNVISQGDT GRRDAARQDL RADYFSTKDG KMLASYYGFL DNYGANPRSG HPSTKRQFHP PPTFPTLGSP SAIEMGNFGD RPAAAGLMGQ QSTYGAAPRF GPAGMGDHLS PAPSMLLDPH HQPSASGFRS THRANPYPRY RASRPPPTIS DPIEDEDPPA GKGRSAVKSS PGVGSSGGGI GTSDSNLGES WRMNLVGDEV EEEDEGGENV DTLAGGGGVL GLIQQFQKVN QDNRGRTTVG I //