ID ATG9A_MOUSE Reviewed; 551 AA. AC Q68FE2; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-DEC-2019, entry version 106. DE RecName: Full=Autophagy-related protein 9A; DE AltName: Full=APG9-like 1; GN Name=Atg9a; Synonyms=Apg9l1; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-18, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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] RP FUNCTION. RX PubMed=23402761; DOI=10.1016/j.bbrc.2013.02.010; RA Chen D., Chen X., Li M., Zhang H., Ding W.X., Yin X.M.; RT "CCCP-Induced LC3 lipidation depends on Atg9 whereas FIP200/Atg13 and RT Beclin 1/Atg14 are dispensable."; RL Biochem. Biophys. Res. Commun. 432:226-230(2013). CC -!- FUNCTION: Involved in autophagy and cytoplasm to vacuole transport CC (Cvt) vesicle formation. Plays a key role in the organization of the CC preautophagosomal structure/phagophore assembly site (PAS), the CC nucleating site for formation of the sequestering vesicle. Cycles CC between a juxta-nuclear trans-Golgi network compartment and late CC endosomes. Nutrient starvation induces accumulation on autophagosomes. CC Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H (By CC similarity). Required for carbonyl cyanide m-chlorophenylhydrazone CC (CCCP)-induced ATG8 family proteins lipidation, a key autophagy step. CC {ECO:0000250, ECO:0000269|PubMed:23402761}. CC -!- SUBUNIT: Interacts with SUPT20H. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi CC apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Isoform displayed in this entry matches to human isoform CC 3. CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}. 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; BC079884; AAH79884.1; -; mRNA. DR RefSeq; NP_001003917.2; NM_001003917.4. DR RefSeq; NP_001275541.1; NM_001288612.1. DR BioGrid; 232841; 2. DR IntAct; Q68FE2; 1. DR MINT; Q68FE2; -. DR STRING; 10090.ENSMUSP00000139608; -. DR iPTMnet; Q68FE2; -. DR PhosphoSitePlus; Q68FE2; -. DR SwissPalm; Q68FE2; -. DR MaxQB; Q68FE2; -. DR PaxDb; Q68FE2; -. DR PeptideAtlas; Q68FE2; -. DR PRIDE; Q68FE2; -. DR Ensembl; ENSMUST00000239085; ENSMUSP00000159170; ENSMUSG00000033124. DR GeneID; 245860; -. DR KEGG; mmu:245860; -. DR CTD; 79065; -. DR MGI; MGI:2138446; Atg9a. DR eggNOG; KOG2173; Eukaryota. DR eggNOG; ENOG410XQBE; LUCA. DR GeneTree; ENSGT00390000014839; -. DR InParanoid; Q68FE2; -. DR KO; K17907; -. DR OrthoDB; 712239at2759; -. DR Reactome; R-MMU-1632852; Macroautophagy. DR ChiTaRS; Atg9a; mouse. DR PRO; PR:Q68FE2; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q68FE2; protein. DR GO; GO:0005776; C:autophagosome; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005770; C:late endosome; ISO:MGI. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000407; C:phagophore assembly site; ISO:MGI. DR GO; GO:0055037; C:recycling endosome; ISO:MGI. DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI. DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI. DR GO; GO:0000045; P:autophagosome assembly; IMP:MGI. DR GO; GO:0006914; P:autophagy; IMP:MGI. DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IMP:MGI. DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central. DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:MGI. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:MGI. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central. 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 1: Evidence at protein level; KW Acetylation; Autophagy; Cytoplasmic vesicle; Endosome; Glycoprotein; KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6" FT CHAIN 2..551 FT /note="Autophagy-related protein 9A" FT /id="PRO_0000119821" FT TRANSMEM 73..93 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 372..392 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 401..421 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21183079" FT MOD_RES 524 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 551 AA; 63138 MW; BDCDBA33E0D10C26 CRC64; MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT CMLIGEMFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEV VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGVHLGGV AESHRHTPHS HLLPPPSGPG DHRLLPQLYG RGRGCGRHLL LCSDGRSPAW PSSVAVWRAD RGLSVPASRG REDRVVAHAL CHHQSRLAAP S //