TNR6A_HUMAN
ID TNR6A_HUMAN Reviewed; 1962 AA.
AC Q8NDV7; C9JAR8; O15408; Q658L5; Q6NVB5; Q8NEZ0; Q8TBT8; Q8TCR0; Q9NV59;
AC Q9P268;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Trinucleotide repeat-containing gene 6A protein;
DE AltName: Full=CAG repeat protein 26;
DE AltName: Full=EMSY interactor protein;
DE AltName: Full=GW182 autoantigen;
DE Short=Protein GW1;
DE AltName: Full=Glycine-tryptophan protein of 182 kDa;
GN Name=TNRC6A; Synonyms=CAGH26, KIAA1460, TNRC6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), RNA-BINDING, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11950943; DOI=10.1091/mbc.01-11-0544;
RA Eystathioy T., Chan E.K.L., Tenenbaum S.A., Keene J.D., Griffith K.,
RA Fritzler M.J.;
RT "A phosphorylated cytoplasmic autoantigen, GW182, associates with a unique
RT population of human mRNAs within novel cytoplasmic speckles.";
RL Mol. Biol. Cell 13:1338-1351(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hughes-Davies L.;
RT "Candidate EMSY interactor protein.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 861-1962 (ISOFORM 6).
RC TISSUE=Kidney, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1515-1962.
RC TISSUE=Kidney, and PNS;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-157 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1962.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-1962.
RC TISSUE=Ovarian carcinoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [9]
RP AUTOANTIGENIC EPITOPE MAPPING.
RX PubMed=14598044; DOI=10.1007/s00109-003-0495-y;
RA Eystathioy T., Chan E.K.L., Takeuchi K., Mahler M., Luft L.M.,
RA Zochodne D.W., Fritzler M.J.;
RT "Clinical and serological associations of autoantibodies to GW bodies and a
RT novel cytoplasmic autoantigen GW182.";
RL J. Mol. Med. 81:811-818(2003).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=13130130; DOI=10.1261/rna.5810203;
RA Eystathioy T., Jakymiw A., Chan E.K.L., Seraphin B., Cougot N.,
RA Fritzler M.J.;
RT "The GW182 protein colocalizes with mRNA degradation associated proteins
RT hDcp1 and hLSm4 in cytoplasmic GW bodies.";
RL RNA 9:1171-1173(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15494374; DOI=10.1242/jcs.01477;
RA Yang Z., Jakymiw A., Wood M.R., Eystathioy T., Rubin R.L., Fritzler M.J.,
RA Chan E.K.L.;
RT "GW182 is critical for the stability of GW bodies expressed during the cell
RT cycle and cell proliferation.";
RL J. Cell Sci. 117:5567-5578(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=15908945; DOI=10.1038/ncb1265;
RA Sen G.L., Blau H.M.;
RT "Argonaute 2/RISC resides in sites of mammalian mRNA decay known as
RT cytoplasmic bodies.";
RL Nat. Cell Biol. 7:633-636(2005).
RN [13]
RP FUNCTION, INTERACTION WITH AGO2, AND SUBCELLULAR LOCATION.
RX PubMed=16284623; DOI=10.1038/ncb1333;
RA Liu J., Rivas F.V., Wohlschlegel J., Yates J.R. III, Parker R.,
RA Hannon G.J.;
RT "A role for the P-body component GW182 in microRNA function.";
RL Nat. Cell Biol. 7:1261-1266(2005).
RN [14]
RP FUNCTION, INTERACTION WITH AGO2, ASSOCIATION WITH SIRNA, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16284622; DOI=10.1038/ncb1334;
RA Jakymiw A., Lian S.L., Eystathioy T., Li S., Satoh M., Hamel J.C.,
RA Fritzler M.J., Chan E.K.L.;
RT "Disruption of GW bodies impairs mammalian RNA interference.";
RL Nat. Cell Biol. 7:1267-1274(2005).
RN [15]
RP ERRATUM OF PUBMED:16284622.
RA Jakymiw A., Lian S.L., Eystathioy T., Li S., Satoh M., Hamel J.C.,
RA Fritzler M.J., Chan E.K.L.;
RL Nat. Cell Biol. 8:100-100(2006).
RN [16]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICRORNA.
RX PubMed=16906129; DOI=10.1038/sj.embor.7400783;
RA Pauley K.M., Eystathioy T., Jakymiw A., Hamel J.C., Fritzler M.J.,
RA Chan E.K.L.;
RT "Formation of GW bodies is a consequence of microRNA genesis.";
RL EMBO Rep. 7:904-910(2006).
RN [17]
RP FUNCTION.
RX PubMed=17671087; DOI=10.1101/gad.1566707;
RA Wakiyama M., Takimoto K., Ohara O., Yokoyama S.;
RT "Let-7 microRNA-mediated mRNA deadenylation and translational repression in
RT a mammalian cell-free system.";
RL Genes Dev. 21:1857-1862(2007).
RN [18]
RP ERRATUM OF PUBMED:17671087.
RA Wakiyama M., Takimoto K., Ohara O., Yokoyama S.;
RL Genes Dev. 21:2509-2509(2007).
RN [19]
RP FUNCTION.
RX PubMed=17596515; DOI=10.1091/mbc.e07-01-0070;
RA Lian S.L., Fritzler M.J., Katz J., Hamazaki T., Terada N., Satoh M.,
RA Chan E.K.L.;
RT "Small interfering RNA-mediated silencing induces target-dependent assembly
RT of GW/P bodies.";
RL Mol. Biol. Cell 18:3375-3387(2007).
RN [20]
RP ERRATUM OF PUBMED:17596515.
RA Lian S.L., Fritzler M.J., Katz J., Hamazaki T., Terada N., Satoh M.,
RA Chan E.K.L.;
RL Mol. Biol. Cell 18:4200-4200(2007).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19056672; DOI=10.1242/jcs.036905;
RA Li S., Lian S.L., Moser J.J., Fritzler M.L., Fritzler M.J., Satoh M.,
RA Chan E.K.L.;
RT "Identification of GW182 and its novel isoform TNGW1 as translational
RT repressors in Ago2-mediated silencing.";
RL J. Cell Sci. 121:4134-4144(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH AGO2.
RX PubMed=18690212; DOI=10.1038/nature07186;
RA Qi H.H., Ongusaha P.P., Myllyharju J., Cheng D., Pakkanen O., Shi Y.,
RA Lee S.W., Peng J., Shi Y.;
RT "Prolyl 4-hydroxylation regulates Argonaute 2 stability.";
RL Nature 455:421-424(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18946079; DOI=10.1091/mbc.e08-08-0796;
RA Jagannath A., Wood M.J.A.;
RT "Localization of double-stranded small interfering RNA to cytoplasmic
RT processing bodies is Ago2 dependent and results in up-regulation of GW182
RT and Argonaute-2.";
RL Mol. Biol. Cell 20:521-529(2009).
RN [25]
RP FUNCTION, AND INTERACTION WITH AGO2.
RX PubMed=19304925; DOI=10.1261/rna.1448009;
RA Zipprich J.T., Bhattacharyya S., Mathys H., Filipowicz W.;
RT "Importance of the C-terminal domain of the human GW182 protein TNRC6C for
RT translational repression.";
RL RNA 15:781-793(2009).
RN [26]
RP INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TRP-313; TRP-345; TRP-370; TRP-420 AND TRP-483.
RX PubMed=19324964; DOI=10.1261/rna.1229409;
RA Lian S.L., Li S., Abadal G.X., Pauley B.A., Fritzler M.J., Chan E.K.L.;
RT "The C-terminal half of human Ago2 binds to multiple GW-rich regions of
RT GW182 and requires GW182 to mediate silencing.";
RL RNA 15:804-813(2009).
RN [27]
RP INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4.
RX PubMed=19383768; DOI=10.1261/rna.1606309;
RA Lazzaretti D., Tournier I., Izaurralde E.;
RT "The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence bound
RT transcripts independently of Argonaute proteins.";
RL RNA 15:1059-1066(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1869, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP INTERACTION WITH CNOT1.
RX PubMed=21981923; DOI=10.1016/j.molcel.2011.09.007;
RA Braun J.E., Huntzinger E., Fauser M., Izaurralde E.;
RT "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA
RT targets.";
RL Mol. Cell 44:120-133(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-878; SER-991;
RP SER-1212; SER-1270 AND SER-1890, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP INTERACTION WITH ZC3H12A.
RX PubMed=26134560; DOI=10.1074/jbc.m114.635870;
RA Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G., Fu M.;
RT "Monocyte chemotactic protein-induced protein 1 and 4 form a complex but
RT act independently in regulation of interleukin-6 mRNA degradation.";
RL J. Biol. Chem. 290:20782-20792(2015).
RN [33]
RP INTERACTION WITH SND1.
RX PubMed=28546213; DOI=10.1126/science.aai9372;
RA Elbarbary R.A., Miyoshi K., Myers J.R., Du P., Ashton J.M., Tian B.,
RA Maquat L.E.;
RT "Tudor-SN-mediated endonucleolytic decay of human cell microRNAs promotes
RT G1/S phase transition.";
RL Science 356:859-862(2017).
RN [34]
RP INVOLVEMENT IN FAME6, AND TISSUE SPECIFICITY.
RX PubMed=29507423; DOI=10.1038/s41588-018-0067-2;
RA Ishiura H., Doi K., Mitsui J., Yoshimura J., Matsukawa M.K., Fujiyama A.,
RA Toyoshima Y., Kakita A., Takahashi H., Suzuki Y., Sugano S., Qu W.,
RA Ichikawa K., Yurino H., Higasa K., Shibata S., Mitsue A., Tanaka M.,
RA Ichikawa Y., Takahashi Y., Date H., Matsukawa T., Kanda J., Nakamoto F.K.,
RA Higashihara M., Abe K., Koike R., Sasagawa M., Kuroha Y., Hasegawa N.,
RA Kanesawa N., Kondo T., Hitomi T., Tada M., Takano H., Saito Y., Sanpei K.,
RA Onodera O., Nishizawa M., Nakamura M., Yasuda T., Sakiyama Y., Otsuka M.,
RA Ueki A., Kaida K.I., Shimizu J., Hanajima R., Hayashi T., Terao Y.,
RA Inomata-Terada S., Hamada M., Shirota Y., Kubota A., Ugawa Y., Koh K.,
RA Takiyama Y., Ohsawa-Yoshida N., Ishiura S., Yamasaki R., Tamaoka A.,
RA Akiyama H., Otsuki T., Sano A., Ikeda A., Goto J., Morishita S., Tsuji S.;
RT "Expansions of intronic TTTCA and TTTTA repeats in benign adult familial
RT myoclonic epilepsy.";
RL Nat. Genet. 50:581-590(2018).
RN [35]
RP INTERACTION WITH GARRE1.
RX PubMed=29395067; DOI=10.1016/j.molcel.2017.12.020;
RA Youn J.Y., Dunham W.H., Hong S.J., Knight J.D.R., Bashkurov M., Chen G.I.,
RA Bagci H., Rathod B., MacLeod G., Eng S.W.M., Angers S., Morris Q.,
RA Fabian M., Cote J.F., Gingras A.C.;
RT "High-Density Proximity Mapping Reveals the Subcellular Organization of
RT mRNA-Associated Granules and Bodies.";
RL Mol. Cell 69:517.e11-532.e11(2018).
CC -!- FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-
CC RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-
CC dependent repression of translation and for siRNA-dependent
CC endonucleolytic cleavage of complementary mRNAs by argonaute family
CC proteins. As a scaffolding protein, associates with argonaute proteins
CC bound to partially complementary mRNAs, and can simultaneously recruit
CC CCR4-NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:16284622,
CC ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:17596515,
CC ECO:0000269|PubMed:17671087, ECO:0000269|PubMed:19056672,
CC ECO:0000269|PubMed:19304925}.
CC -!- SUBUNIT: Interacts with AGO2 (PubMed:16284623, PubMed:16284622,
CC PubMed:18690212, PubMed:19304925, PubMed:19324964, PubMed:19383768).
CC Interacts with AGO1, AGO3 and AGO4 (PubMed:19324964, PubMed:19383768).
CC Interacts with CNOT1; the interaction is direct and mediates the
CC association with the CCR4-NOT complex (PubMed:21981923). Interacts with
CC ZC3H12A (PubMed:26134560). Interacts with SND1 (PubMed:28546213).
CC Interacts with GARRE1 (PubMed:29395067). {ECO:0000269|PubMed:16284622,
CC ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:18690212,
CC ECO:0000269|PubMed:19304925, ECO:0000269|PubMed:19324964,
CC ECO:0000269|PubMed:19383768, ECO:0000269|PubMed:21981923,
CC ECO:0000269|PubMed:26134560, ECO:0000269|PubMed:28546213,
CC ECO:0000269|PubMed:29395067}.
CC -!- INTERACTION:
CC Q8NDV7; Q9UL18: AGO1; NbExp=5; IntAct=EBI-2269715, EBI-527363;
CC Q8NDV7; Q9UKV8: AGO2; NbExp=22; IntAct=EBI-2269715, EBI-528269;
CC Q8NDV7; Q9H9G7: AGO3; NbExp=5; IntAct=EBI-2269715, EBI-2267883;
CC Q8NDV7; Q9HCK5: AGO4; NbExp=4; IntAct=EBI-2269715, EBI-2269696;
CC Q8NDV7; A5YKK6: CNOT1; NbExp=2; IntAct=EBI-2269715, EBI-1222758;
CC Q8NDV7; P11940: PABPC1; NbExp=3; IntAct=EBI-2269715, EBI-81531;
CC Q8NDV7; Q58A45: PAN3; NbExp=2; IntAct=EBI-2269715, EBI-2513054;
CC Q8NDV7; Q15645: TRIP13; NbExp=3; IntAct=EBI-2269715, EBI-358993;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:11950943,
CC ECO:0000269|PubMed:13130130, ECO:0000269|PubMed:15494374,
CC ECO:0000269|PubMed:15908945, ECO:0000269|PubMed:16284622,
CC ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:16906129,
CC ECO:0000269|PubMed:18946079, ECO:0000269|PubMed:19056672,
CC ECO:0000269|PubMed:19324964}. Note=Mammalian P-bodies are also known as
CC GW bodies (GWBs). {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=TNGW1;
CC IsoId=Q8NDV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDV7-2; Sequence=VSP_013294;
CC Name=3;
CC IsoId=Q8NDV7-3; Sequence=VSP_037287, VSP_037288, VSP_037289;
CC Name=4;
CC IsoId=Q8NDV7-4; Sequence=VSP_013292;
CC Name=5;
CC IsoId=Q8NDV7-5; Sequence=VSP_013295;
CC Name=6;
CC IsoId=Q8NDV7-6; Sequence=VSP_037288;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11950943,
CC ECO:0000269|PubMed:29507423}.
CC -!- INDUCTION: By exogenous short interfering RNA (siRNA).
CC {ECO:0000269|PubMed:18946079}.
CC -!- DISEASE: Epilepsy, familial adult myoclonic, 6 (FAME6) [MIM:618074]: A
CC form of familial myoclonic epilepsy, a neurologic disorder
CC characterized by cortical hand tremors, myoclonic jerks and occasional
CC generalized or focal seizures with a non-progressive or very slowly
CC progressive disease course. Usually, myoclonic tremor is the presenting
CC symptom, characterized by tremulous finger movements and myoclonic
CC jerks of the limbs increased by action and posture. In a minority of
CC patients, seizures are the presenting symptom. Some patients exhibit
CC mild cognitive impairment. FAME6 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:29507423}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Antibodies against TNRC6A are found in sera from
CC patients with Sjoegren syndrome (SS), ataxia and sensor neuropathy
CC diseases that developed autoantibodies against protein of the GWB
CC structure. Autoantibodies were mapped to the GW-rich mid-part, the non-
CC GW-rich region and the C-terminus of the protein.
CC -!- SIMILARITY: Belongs to the GW182 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91899.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD28525.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY035864; AAK62026.1; -; mRNA.
DR EMBL; AJ492221; CAD37348.1; -; mRNA.
DR EMBL; AL713750; CAD28525.2; ALT_INIT; mRNA.
DR EMBL; AL833757; CAH56236.1; -; mRNA.
DR EMBL; AC002565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024324; AAH24324.2; -; mRNA.
DR EMBL; BC068209; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U80739; AAB91438.1; -; mRNA.
DR EMBL; AB040893; BAA95984.1; -; mRNA.
DR EMBL; AK001773; BAA91899.1; ALT_INIT; mRNA.
DR CCDS; CCDS10624.2; -. [Q8NDV7-1]
DR CCDS; CCDS81959.1; -. [Q8NDV7-6]
DR RefSeq; NP_001317449.1; NM_001330520.1. [Q8NDV7-6]
DR RefSeq; NP_055309.2; NM_014494.2. [Q8NDV7-1]
DR RefSeq; XP_005255314.1; XM_005255257.4. [Q8NDV7-2]
DR RefSeq; XP_016878642.1; XM_017023153.1. [Q8NDV7-2]
DR PDB; 5W6V; X-ray; 2.83 A; B=1073-1094.
DR PDBsum; 5W6V; -.
DR AlphaFoldDB; Q8NDV7; -.
DR SMR; Q8NDV7; -.
DR BioGRID; 118141; 249.
DR DIP; DIP-54489N; -.
DR ELM; Q8NDV7; -.
DR IntAct; Q8NDV7; 87.
DR MINT; Q8NDV7; -.
DR STRING; 9606.ENSP00000379144; -.
DR GlyGen; Q8NDV7; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; Q8NDV7; -.
DR PhosphoSitePlus; Q8NDV7; -.
DR BioMuta; TNRC6A; -.
DR DMDM; 296452846; -.
DR EPD; Q8NDV7; -.
DR jPOST; Q8NDV7; -.
DR MassIVE; Q8NDV7; -.
DR MaxQB; Q8NDV7; -.
DR PaxDb; Q8NDV7; -.
DR PeptideAtlas; Q8NDV7; -.
DR PRIDE; Q8NDV7; -.
DR ProteomicsDB; 73061; -. [Q8NDV7-1]
DR ProteomicsDB; 73062; -. [Q8NDV7-2]
DR ProteomicsDB; 73063; -. [Q8NDV7-3]
DR ProteomicsDB; 73064; -. [Q8NDV7-4]
DR ProteomicsDB; 73065; -. [Q8NDV7-5]
DR ProteomicsDB; 73066; -. [Q8NDV7-6]
DR Antibodypedia; 12719; 122 antibodies from 23 providers.
DR DNASU; 27327; -.
DR Ensembl; ENST00000315183.11; ENSP00000326900.7; ENSG00000090905.19. [Q8NDV7-6]
DR Ensembl; ENST00000395799.8; ENSP00000379144.3; ENSG00000090905.19. [Q8NDV7-1]
DR Ensembl; ENST00000672933.1; ENSP00000500125.1; ENSG00000288130.1. [Q8NDV7-6]
DR Ensembl; ENST00000673084.1; ENSP00000500873.1; ENSG00000288130.1. [Q8NDV7-1]
DR GeneID; 27327; -.
DR KEGG; hsa:27327; -.
DR MANE-Select; ENST00000395799.8; ENSP00000379144.3; NM_014494.4; NP_055309.2.
DR UCSC; uc002dmm.4; human. [Q8NDV7-1]
DR CTD; 27327; -.
DR DisGeNET; 27327; -.
DR GeneCards; TNRC6A; -.
DR HGNC; HGNC:11969; TNRC6A.
DR HPA; ENSG00000090905; Low tissue specificity.
DR MalaCards; TNRC6A; -.
DR MIM; 610739; gene.
DR MIM; 618074; phenotype.
DR neXtProt; NX_Q8NDV7; -.
DR OpenTargets; ENSG00000090905; -.
DR PharmGKB; PA36656; -.
DR VEuPathDB; HostDB:ENSG00000090905; -.
DR eggNOG; ENOG502QPQQ; Eukaryota.
DR GeneTree; ENSGT00940000158180; -.
DR HOGENOM; CLU_001298_3_1_1; -.
DR InParanoid; Q8NDV7; -.
DR OMA; VMNGTSI; -.
DR OrthoDB; 50428at2759; -.
DR PhylomeDB; Q8NDV7; -.
DR TreeFam; TF329702; -.
DR PathwayCommons; Q8NDV7; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8943723; Regulation of PTEN mRNA translation.
DR Reactome; R-HSA-8948700; Competing endogenous RNAs (ceRNAs) regulate PTEN translation.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q8NDV7; -.
DR BioGRID-ORCS; 27327; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; TNRC6A; human.
DR GeneWiki; TNRC6A; -.
DR GenomeRNAi; 27327; -.
DR Pharos; Q8NDV7; Tbio.
DR PRO; PR:Q8NDV7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NDV7; protein.
DR Bgee; ENSG00000090905; Expressed in corpus callosum and 106 other tissues.
DR ExpressionAtlas; Q8NDV7; baseline and differential.
DR Genevisible; Q8NDV7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:BHF-UCL.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR CDD; cd12711; RRM_TNRC6A; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019486; Argonaute_hook_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR032226; TNRC6_PABC-bd.
DR InterPro; IPR033501; TNRC6A.
DR InterPro; IPR034924; TNRC6A_RRM.
DR PANTHER; PTHR13020:SF28; PTHR13020:SF28; 1.
DR Pfam; PF10427; Ago_hook; 1.
DR Pfam; PF16608; TNRC6-PABC_bdg; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Epilepsy;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..1962
FT /note="Trinucleotide repeat-containing gene 6A protein"
FT /id="PRO_0000081980"
FT DOMAIN 1781..1853
FT /note="RRM"
FT REGION 1..932
FT /note="Interaction with argonaute family proteins"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..503
FT /note="Sufficient for interaction with AGO1, AGO3 and AGO4"
FT REGION 270..346
FT /note="Sufficient for interaction with AGO2"
FT REGION 318..399
FT /note="Sufficient for interaction with AGO2"
FT REGION 340..439
FT /note="Sufficient for interaction with AGO2"
FT REGION 409..495
FT /note="Sufficient for interaction with AGO2"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..751
FT /note="Sufficient for interaction with AGO2"
FT REGION 560..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..1343
FT /note="Sufficient for interaction with AGO1 and AGO4"
FT REGION 718..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1144
FT /note="Sufficient for interaction with AGO2"
FT REGION 1158..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1622
FT /note="PABPC1-interacting motif-2 (PAM2)"
FT REGION 1670..1962
FT /note="Sufficient for interaction with AGO2"
FT REGION 1724..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..54
FT /evidence="ECO:0000255"
FT COMPBIAS 1..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1801
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013292"
FT VAR_SEQ 1..1232
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037287"
FT VAR_SEQ 1..253
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11950943"
FT /id="VSP_013294"
FT VAR_SEQ 1..54
FT /note="MRELEAKATKDVERNLSRDLVQEEEQLMEEKKKKKDDKKKKEAAQKKATEQK
FT IK -> MAYFGGTLYWLIFSTPFLLLGL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9225980"
FT /id="VSP_013295"
FT VAR_SEQ 1280..1328
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037288"
FT VAR_SEQ 1611..1962
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037289"
FT VARIANT 185
FT /note="N -> K (in dbSNP:rs11639856)"
FT /id="VAR_057251"
FT VARIANT 592
FT /note="A -> T (in dbSNP:rs6497759)"
FT /id="VAR_057252"
FT VARIANT 788
FT /note="P -> S (in dbSNP:rs3803716)"
FT /id="VAR_057253"
FT VARIANT 1268
FT /note="E -> K (in dbSNP:rs2112782)"
FT /id="VAR_057254"
FT MUTAGEN 313
FT /note="W->A: Does not impair interaction with AGO2; when
FT associated with A-345; A-370; A-420 and A-483."
FT /evidence="ECO:0000269|PubMed:19324964"
FT MUTAGEN 345
FT /note="W->A: Does not impair interaction with AGO2; when
FT associated with A-313; A-370; A-420 and A-483."
FT /evidence="ECO:0000269|PubMed:19324964"
FT MUTAGEN 370
FT /note="W->A: Does not impair interaction with AGO2; when
FT associated with A-313; A-345; A-420 and A-483."
FT /evidence="ECO:0000269|PubMed:19324964"
FT MUTAGEN 420
FT /note="W->A: Does not impair interaction with AGO2; when
FT associated with A-313; A-345; A-370 and A-483."
FT /evidence="ECO:0000269|PubMed:19324964"
FT MUTAGEN 483
FT /note="W->A: Does not impair interaction with AGO2; when
FT associated with A-313; A-345; A-370 and A-420."
FT /evidence="ECO:0000269|PubMed:19324964"
FT CONFLICT 31..34
FT /note="KKKK -> TEKE (in Ref. 2; CAD37348)"
FT /evidence="ECO:0000305"
FT CONFLICT 1375
FT /note="V -> VV (in Ref. 3; CAD28525)"
FT /evidence="ECO:0000305"
FT CONFLICT 1704
FT /note="S -> F (in Ref. 8; BAA91899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1962 AA; 210297 MW; 963C054628E18592 CRC64;
MRELEAKATK DVERNLSRDL VQEEEQLMEE KKKKKDDKKK KEAAQKKATE QKIKVPEQIK
PSVSQPQPAN SNNGTSTATS TNNNAKRATA NNQQPQQQQQ QQQPQQQQPQ QQPQPQPQQQ
QPQQQPQALP RYPREVPPRF RHQEHKQLLK RGQHFPVIAA NLGSAVKVLN SQSESSALTN
QQPQNNGEVQ NSKNQSDINH STSGSHYENS QRGPVSSTSD SSTNCKNAVV SDLSEKEAWP
SAPGSDPELA SECMDADSAS SSESERNITI MASGNTGGEK DGLRNSTGLG SQNKFVVGSS
SNNVGHGSST GPWGFSHGAI ISTCQVSVDA PESKSESSNN RMNAWGTVSS SSNGGLNPST
LNSASNHGAW PVLENNGLAL KGPVGSGSSG INIQCSTIGQ MPNNQSINSK VSGGSTHGTW
GSLQETCESE VSGTQKVSFS GQPQNITTEM TGPNNTTNFM TSSLPNSGSV QNNELPSSNT
GAWRVSTMNH PQMQAPSGMN GTSLSHLSNG ESKSGGSYGT TWGAYGSNYS GDKCSGPNGQ
ANGDTVNATL MQPGVNGPMG TNFQVNTNKG GGVWESGAAN SQSTSWGSGN GANSGGSRRG
WGTPAQNTGT NLPSVEWNKL PSNQHSNDSA NGNGKTFTNG WKSTEEEDQG SATSQTNEQS
SVWAKTGGTV ESDGSTESTG RLEEKGTGES QSRDRRKIDQ HTLLQSIVNR TDLDPRVLSN
SGWGQTPIKQ NTAWDTETSP RGERKTDNGT EAWGSSATQT FNSGACIDKT SPNGNDTSSV
SGWGDPKPAL RWGDSKGSNC QGGWEDDSAA TGMVKSNQWG NCKEEKAAWN DSQKNKQGWG
DGQKSSQGWS VSASDNWGET SRNNHWGEAN KKSSSGGSDS DRSVSGWNEL GKTSSFTWGN
NINPNNSSGW DESSKPTPSQ GWGDPPKSNQ SLGWGDSSKP VSSPDWNKQQ DIVGSWGIPP
ATGKPPGTGW LGGPIPAPAK EEEPTGWEEP SPESIRRKME IDDGTSAWGD PSKYNYKNVN
MWNKNVPNGN SRSDQQAQVH QLLTPASAIS NKEASSGSGW GEPWGEPSTP ATTVDNGTSA
WGKPIDSGPS WGEPIAAASS TSTWGSSSVG PQALSKSGPK SMQDGWCGDD MPLPGNRPTG
WEEEEDVEIG MWNSNSSQEL NSSLNWPPYT KKMSSKGLSG KKRRRERGMM KGGNKQEEAW
INPFVKQFSN ISFSRDSPEE NVQSNKMDLS GGMLQDKRME IDKHSLNIGD YNRTVGKGPG
SRPQISKESS MERNPYFDKD GIVADESQNM QFMSSQSMKL PPSNSALPNQ ALGSIAGLGM
QNLNSVRQNG NPSMFGVGNT AAQPRGMQQP PAQPLSSSQP NLRAQVPPPL LSPQVPVSLL
KYAPNNGGLN PLFGPQQVAM LNQLSQLNQL SQISQLQRLL AQQQRAQSQR SVPSGNRPQQ
DQQGRPLSVQ QQMMQQSRQL DPNLLVKQQT PPSQQQPLHQ PAMKSFLDNV MPHTTPELQK
GPSPINAFSN FPIGLNSNLN VNMDMNSIKE PQSRLRKWTT VDSISVNTSL DQNSSKHGAI
SSGFRLEESP FVPYDFMNSS TSPASPPGSI GDGWPRAKSP NGSSSVNWPP EFRPGEPWKG
YPNIDPETDP YVTPGSVINN LSINTVREVD HLRDRNSGSS SSLNTTLPST SAWSSIRASN
YNVPLSSTAQ STSARNSDSK LTWSPGSVTN TSLAHELWKV PLPPKNITAP SRPPPGLTGQ
KPPLSTWDNS PLRIGGGWGN SDARYTPGSS WGESSSGRIT NWLVLKNLTP QIDGSTLRTL
CMQHGPLITF HLNLPHGNAL VRYSSKEEVV KAQKSLHMCV LGNTTILAEF ASEEEISRFF
AQSQSLTPSP GWQSLGSSQS RLGSLDCSHS FSSRTDLNHW NGAGLSGTNC GDLHGTSLWG
TPHYSTSLWG PPSSSDPRGI SSPSPINAFL SVDHLGGGGE SM
