ID A0A3F3RV15_ASPNG Unreviewed; 941 AA. AC A0A3F3RV15; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 31-JUL-2019, entry version 6. DE RecName: Full=Autophagy-related protein 9 {ECO:0000256|RuleBase:RU364027}; GN ORFNames=ATCC64974_97800 {ECO:0000313|EMBL:SPB52174.1}; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=5061 {ECO:0000313|EMBL:SPB52174.1, ECO:0000313|Proteomes:UP000236662}; RN [1] {ECO:0000313|Proteomes:UP000236662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 64974 / FGSC A733 / N402 RC {ECO:0000313|Proteomes:UP000236662}; RX PubMed=30319579; DOI=10.3389/fmicb.2018.02269; RA Laothanachareon T., Tamayo-Ramos J.A., Nijsse B., Schaap P.J.; RT "Forward genetics by genome sequencing uncovers the central role of RT the Aspergillus niger goxB locus in hydrogen peroxide induced glucose RT oxidase expression."; RL Front. Microbiol. 9:2269-2269(2018). CC -!- FUNCTION: Involved in autophagy and cytoplasm to vacuole transport CC (Cvt) vesicle formation. Plays a key role in the organization of CC the preautophagosomal structure/phagophore assembly site (PAS), CC the nucleating site for formation of the sequestering vesicle. CC {ECO:0000256|RuleBase:RU364027}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane CC {ECO:0000256|RuleBase:RU364027}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU364027}. CC -!- SIMILARITY: Belongs to the ATG9 family. CC {ECO:0000256|RuleBase:RU364027}. 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; OGUI01000017; SPB52174.1; -; Genomic_DNA. DR SMR; A0A3F3RV15; -. DR Proteomes; UP000236662; Unassembled WGS sequence. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR007241; Autophagy-rel_prot_9. DR PANTHER; PTHR13038; PTHR13038; 1. DR Pfam; PF04109; APG9; 1. PE 3: Inferred from homology; KW Autophagy {ECO:0000256|RuleBase:RU364027}; KW Complete proteome {ECO:0000313|Proteomes:UP000236662}; KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU364027}; KW Golgi apparatus {ECO:0000256|RuleBase:RU364027}; KW Membrane {ECO:0000256|RuleBase:RU364027}; KW Protein transport {ECO:0000256|RuleBase:RU364027}; KW Transmembrane {ECO:0000256|RuleBase:RU364027}; KW Transmembrane helix {ECO:0000256|RuleBase:RU364027}; KW Transport {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 236 256 Helical. {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 289 307 Helical. {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 456 480 Helical. {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 539 559 Helical. {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 579 597 Helical. {ECO:0000256|RuleBase:RU364027}. FT TRANSMEM 645 666 Helical. {ECO:0000256|RuleBase:RU364027}. FT REGION 1 164 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 795 889 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 24 64 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 143 157 Pro-rich. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 869 889 Polar. {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 //