ID ATG9B_HUMAN Reviewed; 924 AA. AC Q674R7; A1A5D3; Q6JRW5; Q8N8I8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 16-OCT-2013, entry version 71. DE RecName: Full=Autophagy-related protein 9B; DE AltName: Full=APG9-like 2; DE AltName: Full=Nitric oxide synthase 3-overlapping antisense gene protein; DE Short=Protein sONE; GN Name=ATG9B; Synonyms=APG9L2, NOS3AS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=15234981; DOI=10.1074/jbc.M400271200; RA Robb G.B., Carson A.R., Tai S.C., Fish J.E., Singh S., Yamada T., RA Scherer S.W., Nakabayashi K., Marsden P.A.; RT "Post-transcriptional regulation of endothelial nitric-oxide synthase RT by an overlapping antisense mRNA transcript."; RL J. Biol. Chem. 279:37982-37996(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP IDENTIFICATION. RX PubMed=15755735; DOI=10.1074/jbc.M413957200; RA Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T., RA Nakabayashi K., Scherer S.W.; RT "Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an RT autophagy-related protein (APG9-like2) highly expressed in RT trophoblast."; RL J. Biol. Chem. 280:18283-18290(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [6] RP INDUCTION. RX PubMed=17403686; DOI=10.1074/jbc.M608318200; RA Fish J.E., Matouk C.C., Yeboah E., Bevan S.C., Khan M., Patil K., RA Ohh M., Marsden P.A.; RT "Hypoxia-inducible expression of a natural cis-antisense transcript RT inhibits endothelial nitric-oxide synthase."; RL J. Biol. Chem. 282:15652-15666(2007). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=18936157; DOI=10.1128/MCB.01082-08; RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.; RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved RT C-terminal domains using an Atg13-independent mechanism."; RL Mol. Cell. Biol. 29:157-171(2009). 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 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; CC Multi-pass membrane protein. Note=Under amino acid starvation or CC rapamycin treatment, redistributes from a juxtanuclear clustered CC pool to a dispersed peripheral cytosolic pool. The starvation- CC induced redistribution depends on ULK1 and ATG13. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q674R7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q674R7-2; Sequence=VSP_030410, VSP_030413; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q674R7-3; Sequence=VSP_030411, VSP_030412; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in placenta (trophoblast CC cells) and pituitary gland. Not expressed in vascular endothelial. CC -!- INDUCTION: By hypoxia, leading to inhibit NOS3 expression. CC -!- MISCELLANEOUS: ATG9B gene is located on the opposite DNA strand of CC the NOS3 gene at chromosome 7q36. The genes are oriented in a CC tail-to-tail configuration and the mRNAs encoding ATG9B and NOS3 CC are complementary for 662 nucleotides. ATG9B transcription may a CC role in NOS3 transcription regulation. CC -!- SIMILARITY: Belongs to the ATG9 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ86941.1; Type=Erroneous initiation; CC Sequence=AC010973; Type=Frameshift; Positions=766; 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; AY515311; AAS87212.1; -; mRNA. DR EMBL; AY316116; AAQ86941.1; ALT_INIT; mRNA. DR EMBL; AK096734; BAC04853.1; -; mRNA. DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC128587; AAI28588.1; -; mRNA. DR EMBL; BK004019; DAA05200.1; -; mRNA. DR IPI; IPI00465328; -. DR IPI; IPI00747506; -. DR IPI; IPI00827670; -. DR RefSeq; NP_775952.4; NM_173681.5. DR UniGene; Hs.707300; -. DR UniGene; Hs.716846; -. DR ProteinModelPortal; Q674R7; -. DR STRING; 9606.ENSP00000380436; -. DR PhosphoSite; Q674R7; -. DR DMDM; 74708555; -. DR PaxDb; Q674R7; -. DR PRIDE; Q674R7; -. DR GeneID; 285973; -. DR KEGG; hsa:285973; -. DR UCSC; uc011kvc.2; human. DR CTD; 285973; -. DR GeneCards; GC07M150710; -. DR H-InvDB; HIX0007219; -. DR HGNC; HGNC:21899; ATG9B. DR MIM; 612205; gene. DR neXtProt; NX_Q674R7; -. DR PharmGKB; PA134883165; -. DR eggNOG; NOG298729; -. DR HOVERGEN; HBG050539; -. DR InParanoid; Q674R7; -. DR GenomeRNAi; 285973; -. DR NextBio; 95902; -. DR PRO; PR:Q674R7; -. DR CleanEx; HS_ATG9B; -. DR Genevestigator; Q674R7; -. DR GO; GO:0000421; C:autophagic vacuole membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0000045; P:autophagic vacuole assembly; IDA:MGI. DR InterPro; IPR007241; Autophagy-rel_prot_9. DR PANTHER; PTHR13038; PTHR13038; 1. DR Pfam; PF04109; APG9; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Autophagy; Complete proteome; KW Cytoplasmic vesicle; Membrane; Polymorphism; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 924 Autophagy-related protein 9B. FT /FTId=PRO_0000314867. FT TOPO_DOM 1 207 Cytoplasmic (By similarity). FT TRANSMEM 208 228 Helical; (Potential). FT TOPO_DOM 229 276 Lumenal (By similarity). FT TRANSMEM 277 297 Helical; (Potential). FT TOPO_DOM 298 438 Cytoplasmic (By similarity). FT TRANSMEM 439 459 Helical; (Potential). FT TOPO_DOM 460 526 Lumenal (By similarity). FT TRANSMEM 527 547 Helical; (Potential). FT TOPO_DOM 548 551 Cytoplasmic (By similarity). FT TRANSMEM 552 572 Helical; (Potential). FT TOPO_DOM 573 624 Lumenal (By similarity). FT TRANSMEM 625 645 Helical; (Potential). FT TOPO_DOM 646 924 Cytoplasmic (By similarity). FT COMPBIAS 22 147 Pro-rich. FT VAR_SEQ 1 514 Missing (in isoform 2). FT /FTId=VSP_030410. FT VAR_SEQ 322 340 EELSSVPWAEVQSRLLALQ -> GKGREDTGMYWRGQPGGL FT D (in isoform 3). FT /FTId=VSP_030411. FT VAR_SEQ 341 924 Missing (in isoform 3). FT /FTId=VSP_030412. FT VAR_SEQ 515 572 RTAAPPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVLAV FT EHVLTAMTALGVTATVA -> MPSYPQPSVLRGSAPARCWS FT SSWSWLPASGWSNCFAQSATSSATGTSRCFTGRPCTSP FT (in isoform 2). FT /FTId=VSP_030413. FT VARIANT 166 166 P -> L (in dbSNP:rs61078191). FT /FTId=VAR_061030. FT CONFLICT 12 12 R -> K (in Ref. 2; BAC04853). FT CONFLICT 751 751 S -> P (in Ref. 1; AAQ86941). FT CONFLICT 752 752 T -> P (in Ref. 1; AAQ86941). FT CONFLICT 760 760 T -> A (in Ref. 1; AAQ86941). SQ SEQUENCE 924 AA; 101019 MW; 80C242069DF3D91E CRC64; MVSRMGWGGR RRRLGRWGDL GPGSVPLLPM PLPPPPPPSC RGPGGGRISI FSLSPAPHTR SSPSSFSPPT AGPPCSVLQG TGASQSCHSA LPIPATPPTQ AQPAMTPASA SPSWGSHSTP PLAPATPTPS QQCPQDSPGL RVGPLIPEQD YERLEDCDPE GSQDSPIHGE EQQPLLHVPE GLRGSWHHIQ NLDSFFTKIY SYHQRNGFAC ILLEDVFQLG QFIFIVTFTT FLLRCVDYNV LFANQPSNHT RPGPFHSKVT LSDAILPSAQ CAERIRSSPL LVLLLVLAAG FWLVQLLRSV CNLFSYWDIQ VFYREALHIP PEELSSVPWA EVQSRLLALQ RSGGLCVQPR PLTELDIHHR ILRYTNYQVA LANKGLLPAR CPLPWGGSAA FLSRGLALNV DLLLFRGPFS LFRGGWELPH AYKRSDQRGA LAARWGRTVL LLAALNLALS PLVLAWQVLH VFYSHVELLR REPGALGARG WSRLARLQLR HFNELPHELR ARLARAYRPA AAFLRTAAPP APLRTLLARQ LVFFAGALFA ALLVLTVYDE DVLAVEHVLT AMTALGVTAT VARSFIPEEQ CQGRAPQLLL QTALAHMHYL PEEPGPGGRD RAYRQMAQLL QYRAVSLLEE LLSPLLTPLF LLFWFRPRAL EIIDFFHHFT VDVAGVGDIC SFALMDVKRH GHPQWLSAGQ TEASLSQRAE DGKTELSLMR FSLAHPLWRP PGHSSKFLGH LWGRVQQDAA AWGATSARGP STPGVLSNCT SPLPEAFLAN LFVHPLLPPR DLSPTAPCPA AATASLLASI SRIAQDPSSV SPGGTGGQKL AQLPELASAE MSLHVIYLHQ LHQQQQQQEP WGEAAASILS RPCSSPSQPP SPDEEKPSWS SDGSSPASSP RQQWGTQKAR NLFPGGFQVT TDTQKEPDRA SCTD //