ID NCOA3_MOUSE Reviewed; 1398 AA. AC O09000; Q9CRD5; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 16-SEP-2015, entry version 148. DE RecName: Full=Nuclear receptor coactivator 3; DE Short=NCoA-3; DE EC=2.3.1.48; DE AltName: Full=Amplified in breast cancer-1 protein homolog; DE Short=AIB-1; DE AltName: Full=CBP-interacting protein; DE Short=p/CIP; DE Short=pCIP; DE AltName: Full=Receptor-associated coactivator 3; DE Short=RAC-3; DE AltName: Full=Steroid receptor coactivator protein 3; DE Short=SRC-3; DE AltName: Full=Thyroid hormone receptor activator molecule 1; DE Short=ACTR; DE Short=TRAM-1; GN Name=Ncoa3; Synonyms=Aib1, Pcip, Rac3, Tram1; 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 [MRNA], AND INTERACTION WITH CREBBP; ESR AND RARA. RX PubMed=9192892; DOI=10.1038/42652; RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., RA Rosenfeld M.G.; RT "The transcriptional co-activator p/CIP binds CBP and mediates RT nuclear-receptor function."; RL Nature 387:677-684(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1360-1398. RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=10823921; DOI=10.1073/pnas.120166297; RA Xu J., Liao L., Ning G., Yoshida-Komiya H., Deng C., O'Malley B.W.; RT "The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) RT is required for normal growth, puberty, female reproductive function, RT and mammary gland development."; RL Proc. Natl. Acad. Sci. U.S.A. 97:6379-6384(2000). RN [4] RP INTERACTION WITH CARM1. RX PubMed=10381882; DOI=10.1126/science.284.5423.2174; RA Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., RA Aswad D.W., Stallcup M.R.; RT "Regulation of transcription by a protein methyltransferase."; RL Science 284:2174-2177(1999). RN [5] RP METHYLATION BY CARM1. RX PubMed=11701890; DOI=10.1126/science.1065961; RA Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., RA Evans R.M.; RT "A transcriptional switch mediated by cofactor methylation."; RL Science 294:2507-2511(2001). RN [6] RP INTERACTION WITH NR4A3. RX PubMed=12709428; DOI=10.1074/jbc.M300088200; RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.; RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans- RT activation, coactivator recruitment, and activation by the purine RT anti-metabolite 6-mercaptopurine."; RL J. Biol. Chem. 278:24776-24790(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-544; SER-720; RP SER-847 AND SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-544; SER-562; RP SER-847 AND SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609; LYS-612 AND LYS-613, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear CC receptors and stimulates the transcriptional activities in a CC hormone-dependent fashion. Plays a central role in creating a CC multisubunit coactivator complex, probably via remodeling of CC chromatin. Involved in the coactivation of different nuclear CC receptors, such as for steroids (GR and ER), retinoids (RARs and CC RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids CC (PPARs). Displays histone acetyltransferase activity. Also CC involved in the coactivation of the NF-kappa-B pathway via its CC interaction with the NFKB1 subunit (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- CC [histone]. CC -!- ENZYME REGULATION: Coactivator activity on nuclear receptors and CC NF-kappa-B pathways is enhanced by various hormones, and the TNF CC cytokine, respectively. TNF stimulation probably enhances CC phosphorylation, which in turn activates coactivator function. In CC contrast, acetylation by CREBBP apparently suppresses coactivation CC of target genes by disrupting its association with nuclear CC receptors (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with the histone acetyltransferase protein CC CREBBP. These two proteins are present in a complex containing CC NCOA2, IKKA, IKKB and IKBKG. Interacts with PCAF and NR3C1 (By CC similarity). Interacts with CARM1. Interacts with CASP8AP2. CC Interacts with ATAD2 and this interaction is enhanced by estradiol CC (By similarity). Interacts with PSMB9. Binds to CSNK1D (By CC similarity). Found in a complex containing NCOA3, AR and MAK. CC Interacts with DDX5. Interacts with NPAS2 (By similarity). CC Interacts with NR4A3 (via AF-1 domain) (PubMed:12709428). CC {ECO:0000250, ECO:0000269|PubMed:12709428}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic CC and weakly nuclear. Upon TNF activation and subsequent CC phosphorylation, it translocates from the cytoplasm to the nucleus CC (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Not expressed in all steroid sensitive CC tissues. Highly expressed in the female reproductive system, in CC both oocyte and smooth muscle cells of the oviduct, but not CC expressed in the uterine endometrium. Highly expressed in mammary CC glands. Expressed moderately in smooth muscle cells of both blood CC vessels and intestines, and weakly expressed in hepatocytes. In CC brain, highly expressed in neurons of the hyppocampus, and in CC mitral cell and granule layers of the olfactory bulb. Expressed CC moderately in the internal layer of cerebellum. Not expressed in CC the spinal chord, cardiac muscle, skeletal muscle, thymus and CC pancreas. {ECO:0000269|PubMed:10823921}. CC -!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs CC 1 and 2 are essential for the association with nuclear receptors, CC and constitute the RID domain (Receptor-interacting domain) (By CC similarity). {ECO:0000250}. CC -!- PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, CC and disrupts the interaction with nuclear receptors and regulates CC its function (By similarity). {ECO:0000250}. CC -!- PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}. CC -!- PTM: Phosphorylated by IKK complex. Regulated its function (By CC similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Defects result in diverse phenotype of CC postnatal growth retardation, such as dwarfism, delayed puberty, CC abnormal reproductive function and mammary gland growth CC retardation. {ECO:0000269|PubMed:10823921}. CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00981}. CC -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00140}. 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; AF000581; AAC05020.1; -; mRNA. DR EMBL; AK021229; -; NOT_ANNOTATED_CDS; mRNA. DR UniGene; Mm.469663; -. DR ProteinModelPortal; O09000; -. DR SMR; O09000; 35-365, 1052-1098. DR DIP; DIP-44921N; -. DR IntAct; O09000; 12. DR MINT; MINT-1531012; -. DR STRING; 10090.ENSMUSP00000085416; -. DR PhosphoSite; O09000; -. DR PaxDb; O09000; -. DR PRIDE; O09000; -. DR MGI; MGI:1276535; Ncoa3. DR eggNOG; NOG315556; -. DR HOGENOM; HOG000230947; -. DR HOVERGEN; HBG052583; -. DR InParanoid; O09000; -. DR Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation. DR Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes. DR ChiTaRS; Ncoa3; mouse. DR PRO; PR:O09000; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_NCOA3; -. DR CleanEx; MM_RAC3; -. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0000790; C:nuclear chromatin; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI. DR GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI. DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IBA:GO_Central. DR GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI. DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI. DR GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:MGI. DR GO; GO:0001135; F:RNA polymerase II transcription factor recruiting transcription factor activity; IDA:MGI. DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI. DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI. DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central. DR GO; GO:0048589; P:developmental growth; IMP:MGI. DR GO; GO:0016573; P:histone acetylation; ISO:MGI. DR GO; GO:0060713; P:labyrinthine layer morphogenesis; IGI:MGI. DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI. DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISO:MGI. DR GO; GO:2000035; P:regulation of stem cell division; IMP:MGI. DR GO; GO:2000036; P:regulation of stem cell maintenance; IMP:MGI. DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:MGI. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:GOC. DR GO; GO:0060068; P:vagina development; IMP:MGI. DR Gene3D; 4.10.630.10; -; 2. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR010011; DUF1518. DR InterPro; IPR028818; NCOA3. DR InterPro; IPR009110; Nuc_rcpt_coact. DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ. DR InterPro; IPR017426; Nuclear_rcpt_coactivator. DR InterPro; IPR000014; PAS. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR014935; SRC-1. DR InterPro; IPR008955; Src1_rcpt_coact. DR PANTHER; PTHR10684; PTHR10684; 1. DR PANTHER; PTHR10684:SF3; PTHR10684:SF3; 1. DR Pfam; PF07469; DUF1518; 1. DR Pfam; PF08815; Nuc_rec_co-act; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF08832; SRC-1; 1. DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF47459; SSF47459; 1. DR SUPFAM; SSF55785; SSF55785; 2. DR SUPFAM; SSF69125; SSF69125; 1. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50112; PAS; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Acyltransferase; Complete proteome; Cytoplasm; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9Y6Q9}. FT CHAIN 2 1398 Nuclear receptor coactivator 3. FT /FTId=PRO_0000094407. FT DOMAIN 26 83 bHLH. {ECO:0000255|PROSITE- FT ProRule:PRU00981}. FT DOMAIN 111 181 PAS. {ECO:0000255|PROSITE- FT ProRule:PRU00140}. FT REGION 949 1113 Interaction with CREBBP. {ECO:0000250}. FT REGION 1104 1278 Acetyltransferase. FT MOTIF 678 682 LXXLL motif 1. FT MOTIF 730 734 LXXLL motif 2. FT MOTIF 1041 1045 LXXLL motif 3. FT COMPBIAS 429 664 Ser-rich. FT COMPBIAS 965 987 Poly-Gln. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:Q9Y6Q9}. FT MOD_RES 215 215 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 544 544 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 562 562 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 594 594 Phosphoserine; by CK1. {ECO:0000250}. FT MOD_RES 609 609 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 609 609 N6-acetyllysine; by CREBBP; alternate. FT {ECO:0000250}. FT MOD_RES 612 612 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 612 612 N6-acetyllysine; by CREBBP; alternate. FT {ECO:0000250}. FT MOD_RES 613 613 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 613 613 N6-acetyllysine; by CREBBP; alternate. FT {ECO:0000250}. FT MOD_RES 680 680 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9Y6Q9}. FT MOD_RES 720 720 Phosphoserine. FT {ECO:0000244|PubMed:19144319}. FT MOD_RES 847 847 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 850 850 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. SQ SEQUENCE 1398 AA; 151574 MW; EF44E92735816C24 CRC64; MSGLGESSLD PLAAESRKRK LPCDAPGQGL VYSGEKWRRE QESKYIEELA ELISANLSDI DNFNVKPDKC AILKETVRQI RQIKEQGKTI SSDDDVQKAD VSSTGQGVID KDSLGPLLLQ ALDGFLFVVN RDGNIVFVSE NVTQYLQYKQ EDLVNTSVYS ILHEPRRKDF LNTYQNPQLM EFLGLMRTRD KKAPYILIVR MLMKTHDILE DVNASPETRQ RYETMQCFAL SQPRAMLEEG EDLQCCMICV ARRVTAPFPS SPESFITRHD LSGKVVNIDT NSLRSSMRPG FEDIIRRCIQ RFFSLNDGQS WSQKRHYQEA YVHGHAETPV YRFSLADGTI VSAQTKSKLF RNPVTNDRHG FISTHFLQRE QNGYRPNPIP QDKGIRPPAA GCGVSMSPNQ NVQMMGSRTY GVPDPSNTGQ MGGARYGASS SVASLTPGQS LQSPSSYQNS SYGLSMSSPP HGSPGLGPNQ QNIMISPRNR GSPKMASHQF SPAAGAHSPM GPSGNTGSHS FSSSSLSALQ AISEGVGTSL LSTLSSPGPK LDNSPNMNIS QPSKVSGQDS KSPLGLYCEQ NPVESSVCQS NSRDPQVKKE SKESSGEVSE TPRGPLESKG HKKLLQLLTC SSDDRGHSSL TNSPLDPNCK DSSVSVTSPS GVSSSTSGTV SSTSNVHGSL LQEKHRILHK LLQNGNSPAE VAKITAEATG KDTSSTASCG EGTTRQEQLS PKKKENNALL RYLLDRDDPS DVLAKELQPQ ADSGDSKLSQ CSCSTNPSSG QEKDPKIKTE TNDEVSGDLD NLDAILGDLT SSDFYNNPTN GGHPGAKQQM FAGPSSLGLR SPQPVQSVRP PYNRAVSLDS PVSVGSGPPV KNVSAFPGLP KQPILAGNPR MMDSQENYGA NMGPNRNVPV NPTSSPGDWG LANSRASRME PLASSPLGRT GADYSATLPR PAMGGSVPTL PLRSNRLPGA RPSLQQQQQQ QQQQQQQQQQ QQQQQQQMLQ MRTGEIPMGM GVNPYSPAVQ SNQPGSWPEG MLSMEQGPHG SQNRPLLRNS LDDLLGPPSN AEGQSDERAL LDQLHTFLSN TDATGLEEID RALGIPELVN QGQALESKQD VFQGQEAAVM MDQKAALYGQ TYPAQGPPLQ GGFNLQGQSP SFNSMMGQIS QQGSFPLQGM HPRAGLVRPR TNTPKQLRMQ LQQRLQGQQF LNQSRQALEM KMENPAGTAV MRPMMPQAFF NAQMAAQQKR ELMSHHLQQQ RMAMMMSQPQ PQAFSPPPNV TASPSMDGVL AGSAMPQAPP QQFPYPANYG MGQPPEPAFG RGSSPPSAMM SSRMGPSQNA MVQHPQPTPM YQPSDMKGWP SGNLARNGSF PQQQFAPQGN PAAYNMVHMN SSGGHLGQMA MTPMPMSGMP MGPDQKYC //