ID A0A087WP33_MOUSE Unreviewed; 847 AA. AC A0A087WP33; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 14-DEC-2022, entry version 42. DE RecName: Full=Autophagy-related protein 9 {ECO:0000256|RuleBase:RU364027}; DE Flags: Fragment; GN Name=Atg9a {ECO:0000313|Ensembl:ENSMUSP00000139608.2, GN ECO:0000313|MGI:MGI:2138446}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000139608.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0007829|PubMed:19144319} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000139608.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139608.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000139608.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000139608.2}; RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004511, CC ECO:0000256|RuleBase:RU364027}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}. CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000256|ARBA:ARBA00006185, CC ECO:0000256|RuleBase:RU364027}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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 jPOST; A0A087WP33; -. DR ProteomicsDB; 310337; -. DR Ensembl; ENSMUST00000189820.7; ENSMUSP00000139608.2; ENSMUSG00000033124.17. DR UCSC; uc007bnz.1; mouse. DR AGR; MGI:2138446; -. DR MGI; MGI:2138446; Atg9a. DR VEuPathDB; HostDB:ENSMUSG00000033124; -. DR GeneTree; ENSGT00390000014839; -. DR PhylomeDB; A0A087WP33; -. DR ChiTaRS; Atg9a; mouse. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000033124; Expressed in hindlimb stylopod muscle and 59 other tissues. DR ExpressionAtlas; A0A087WP33; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. DR GO; GO:0005770; C:late endosome; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl. DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl. DR GO; GO:0017128; F:phospholipid scramblase activity; IEA:Ensembl. DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl. DR InterPro; IPR007241; Autophagy-rel_prot_9. DR PANTHER; PTHR13038; APG9 AUTOPHAGY 9; 1. DR Pfam; PF04109; ATG9; 1. PE 1: Evidence at protein level; KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU364027}; KW Lipid transport {ECO:0000256|RuleBase:RU364027}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364027}; KW Proteomics identification {ECO:0007829|EPD:A0A087WP33, KW ECO:0007829|MaxQB:A0A087WP33}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; 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 63..85 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 283..307 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 373..390 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT TRANSMEM 397..418 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364027" FT REGION 650..676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 710..847 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..676 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 713..733 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 811..831 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000139608.2" SQ SEQUENCE 847 AA; 95222 MW; BF065225E5A63227 CRC64; XQRLEASYSD SPPGEEDLLV HVAEGSKSPW HHIENLDLFF SRVYNLHQKN GFTCMLIGEM FELMQFLFVV AFTTFLVSCV DYDILFANKM VNHSLHPTEP VKVTLPDAFL PAQVCSARIQ ENGSLITILV IAGVFWIHRL IKFIYNICCY WEIHSFYLHA LRIPMSALPY CTWQEVQARI VQTQKEHQIC IHKRELTELD IYHRILRFQN YMVALVNKSL LPLRFRLPGL GEVVFFTRGL KYNFELILFW GPGSLFLNEW SLKAEYKRGG QRLELAQRLS NRILWIGIAN FLLCPLILIW QILYAFFSYA EVLKREPGAL GARCWSLYGR CYLRHFNELE HELQSRLNRG YKPASKYMNC FLSPLLTLLA KNGAFFAGSI LAVLIALTIY DEDVLAVEHV LTTVTLLGVT VTVCRSFIPD QHMVFCPEQL LRVILAHIHY MPDHWQGNAH RSQTRDEFAQ LFQYKAVFIL EELLSPIVTP LILIFCLRPR ALEIIDFFRN FTVEVVGVGD TCSFAQMDVR QHGHPQWLSG GQTEASVYQQ AEDGKTELSL MHFAITNPGW QPPRESTAFL GFLKEQVQRD GAAAGLAQGG LLPENALFTS IQSLQSESEP LSLIANVVAG SSCRGPSLSR DLQGSRHRAD VASALRSFSP LQPGAAPQGR VPSTMTGSGV DARTASSGSS VWEGQLQSLV LSEYASTEMS LHALYMHQLH KQQTQAEPER HVWHRRESDE SGESAPEEGG EGARAPQPIP RSASYPCATP RPGAPETTAL HGGFQRRYGG ITDPGTVPRG PSHFSRLPLG GWAEDGQPAS RHPEPVPEEG SEDELPPQVH KVKAVRPRTT ARSGDFQ //