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 06-JUL-2016, entry version 87. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT project: 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 RT 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 CC the preautophagosomal structure/phagophore assembly site (PAS), CC the nucleating site for formation of the sequestering vesicle. CC Cycles between a juxta-nuclear trans-Golgi network compartment and CC late endosomes. Nutrient starvation induces accumulation on CC autophagosomes. Starvation-dependent trafficking requires ULK1, CC ATG13 and SUPT20H (By similarity). Required for carbonyl cyanide CC m-chlorophenylhydrazone (CCCP)-induced ATG8 family proteins CC lipidation, a key autophagy step. {ECO:0000250, CC 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 CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Isoform displayed in this entry matches to human CC isoform 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 UniGene; Mm.238266; -. DR UniGene; Mm.491221; -. DR IntAct; Q68FE2; 1. DR STRING; 10090.ENSMUSP00000047449; -. DR iPTMnet; Q68FE2; -. DR EPD; Q68FE2; -. DR MaxQB; Q68FE2; -. DR PaxDb; Q68FE2; -. DR PeptideAtlas; Q68FE2; -. DR PRIDE; Q68FE2; -. DR GeneID; 245860; -. DR KEGG; mmu:245860; -. DR CTD; 79065; -. DR MGI; MGI:2138446; Atg9a. DR eggNOG; KOG2173; Eukaryota. DR eggNOG; ENOG410XQBE; LUCA. DR InParanoid; Q68FE2; -. DR KO; K17907; -. DR ChiTaRS; Atg9a; mouse. DR PRO; PR:Q68FE2; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_ATG9A; -. DR GO; GO:0005776; C:autophagosome; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005770; C:late endosome; ISO:MGI. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0000407; C:pre-autophagosomal structure; ISO:MGI. DR GO; GO:0055037; C:recycling endosome; 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:0045087; P:innate immune response; IMP:MGI. DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central. DR GO; GO:0000422; P:mitophagy; IBA:GO_Central. DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:MGI. DR GO; GO:0034727; P:piecemeal microautophagy of nucleus; IBA:GO_Central. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:MGI. DR GO; GO:0034497; P:protein localization to pre-autophagosomal structure; 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; Complete proteome; Cytoplasmic vesicle; KW Endosome; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q7Z3C6}. FT CHAIN 2 551 Autophagy-related protein 9A. FT /FTId=PRO_0000119821. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 290 310 Helical. {ECO:0000255}. FT TRANSMEM 372 392 Helical. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:Q7Z3C6}. FT MOD_RES 14 14 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7Z3C6}. FT MOD_RES 16 16 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 18 18 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 524 524 Phosphoserine. FT {ECO:0000250|UniProtKB:Q7Z3C6}. FT CARBOHYD 99 99 N-linked (GlcNAc...). {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 //