SMCA4_MOUSE
ID SMCA4_MOUSE Reviewed; 1613 AA.
AC Q3TKT4; Q3TUD7; Q6AXG8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcription activator BRG1;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase SMARCA4;
DE AltName: Full=BRG1-associated factor 190A;
DE Short=BAF190A;
DE AltName: Full=Protein brahma homolog 1;
DE AltName: Full=SNF2-beta;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP INTERACTION WITH PHF10.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [5]
RP INTERACTION WITH MYOG.
RX PubMed=16424906; DOI=10.1038/sj.emboj.7600943;
RA Ohkawa Y., Marfella C.G., Imbalzano A.N.;
RT "Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase
RT Brg1.";
RL EMBO J. 25:490-501(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; SER-613; SER-695;
RP SER-699; THR-1390; SER-1536; SER-1541 AND SER-1552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH KDM6A; KDM6B AND TBX21.
RX PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
RA Miller S.A., Mohn S.E., Weinmann A.S.;
RT "Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling
RT to regulate T-box family member-dependent gene expression.";
RL Mol. Cell 40:594-605(2010).
RN [10]
RP INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
RX PubMed=22162999; DOI=10.1371/journal.pone.0028049;
RA Vizlin-Hodzic D., Runnberg R., Ryme J., Simonsson S., Simonsson T.;
RT "SAF-A forms a complex with BRG1 and both components are required for RNA
RT polymerase II mediated transcription.";
RL PLoS ONE 6:E28049-E28049(2011).
RN [11]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=22952240; DOI=10.1074/jbc.r111.309302;
RA Euskirchen G., Auerbach R.K., Snyder M.;
RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
RT functions.";
RL J. Biol. Chem. 287:30897-30905(2012).
RN [12]
RP FUNCTION, INTERACTION WITH DLX1, SUBCELLULAR LOCATION, AND RNA-BINDING
RP REGION.
RX PubMed=26138476; DOI=10.1242/dev.126318;
RA Cajigas I., Leib D.E., Cochrane J., Luo H., Swyter K.R., Chen S.,
RA Clark B.S., Thompson J., Yates J.R. III, Kingston R.E., Kohtz J.D.;
RT "Evf2 lncRNA/BRG1/DLX1 interactions reveal RNA-dependent inhibition of
RT chromatin remodeling.";
RL Development 142:2641-2652(2015).
RN [13]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=26601204; DOI=10.1126/sciadv.1500447;
RA Kadoch C., Crabtree G.R.;
RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic
RT insights gained from human genomics.";
RL Sci. Adv. 1:E1500447-E1500447(2015).
RN [14]
RP IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
RN [15]
RP INTERACTION WITH HDGFL2.
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Component of SWI/SNF chromatin remodeling complexes that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. Component of the CREST-BRG1 complex, a multiprotein complex
CC that regulates promoter activation by orchestrating the calcium-
CC dependent release of a repressor complex and the recruitment of an
CC activator complex. In resting neurons, transcription of the c-FOS
CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho-
CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is
CC dephosphorylated by calcineurin, which leads to release of the
CC repressor complex. At the same time, there is increased recruitment of
CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to
CC transcriptional activation. The CREST-BRG1 complex also binds to the
CC NR2B promoter, and activity-dependent induction of NR2B expression
CC involves the release of HDAC1 and recruitment of CREBBP (By
CC similarity). Belongs to the neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) and the neuron-specific chromatin
CC remodeling complex (nBAF complex). During neural development, a switch
CC from a stem/progenitor to a postmitotic chromatin remodeling mechanism
CC occurs as neurons exit the cell cycle and become committed to their
CC adult state. The transition from proliferating neural stem/progenitor
CC cells to postmitotic neurons requires a switch in subunit composition
CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role in regulating the
CC activity of genes essential for dendrite growth. SMARCA4/BAF190A may
CC promote neural stem cell self-renewal/proliferation by enhancing Notch-
CC dependent proliferative signals, while concurrently making the neural
CC stem cell insensitive to SHH-dependent differentiating cues. Acts as a
CC corepressor of ZEB1 to regulate E-cadherin transcription and is
CC required for induction of epithelial-mesenchymal transition (EMT) by
CC ZEB1 (By similarity). Binds via DLX1 to enhancers located in the
CC intergenic region between DLX5 and DLX6 and this binding is stabilized
CC by the long non-coding RNA (lncRNA) Evf2 (PubMed:26138476). Binds to
CC RNA in a promiscuous manner (PubMed:26138476). Binding to RNAs
CC including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and
CC chromatin remodeling activities (PubMed:26138476).
CC {ECO:0000250|UniProtKB:P51532, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:26138476}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible developmental- and tissue-specific
CC combinations (Probable). Component of the BAF complex, which includes
CC at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of
CC the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin.
CC Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA
CC or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A
CC (PubMed:29374058). Component of the BAF53 complex, at least composed of
CC BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially
CC acetylates histone H4 (and H2A) within nucleosomes (By similarity).
CC Component of the CREST-BRG1 complex, at least composed of
CC SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity).
CC Interacts with PHF10/BAF45A (PubMed:17640523). Interacts with MYOG
CC (PubMed:16424906). Interacts directly with IKFZ1; the interaction
CC associates IKFZ1 with the BAF complex. Interacts with ZEB1 (via N-
CC terminus). Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7.
CC Interacts with (via the bromodomain) with TERT; the interaction
CC regulates Wnt-mediated signaling (By similarity). Interacts with KDM6A
CC and KDM6B (PubMed:21095589). Interacts with TBX21 in a KDM6B-dependent
CC manner (PubMed:21095589). Interacts with HNRNPU; this interaction
CC occurs in embryonic stem cells and stimulates global Pol II-mediated
CC transcription (PubMed:22162999). Interacts with ACTL6A (By similarity).
CC Interacts with DLX1 (PubMed:26138476). Interacts with DPF2 (By
CC similarity). Interacts with DPF3a (isoform 2 of DPF3/BAF45C) (By
CC similarity). Interacts with HDGFL2 in a DPF3a-dependent manner
CC (PubMed:32459350). {ECO:0000250|UniProtKB:P51532,
CC ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:22162999,
CC ECO:0000269|PubMed:26138476, ECO:0000269|PubMed:29374058,
CC ECO:0000269|PubMed:32459350, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q3TKT4; A2BH40: Arid1a; NbExp=7; IntAct=EBI-1210244, EBI-371499;
CC Q3TKT4; E9Q4N7: Arid1b; NbExp=5; IntAct=EBI-1210244, EBI-6900614;
CC Q3TKT4; O09106: Hdac1; NbExp=2; IntAct=EBI-1210244, EBI-301912;
CC Q3TKT4; P70288: Hdac2; NbExp=4; IntAct=EBI-1210244, EBI-302251;
CC Q3TKT4; O88895: Hdac3; NbExp=2; IntAct=EBI-1210244, EBI-302263;
CC Q3TKT4; Q99N13: Hdac9; NbExp=3; IntAct=EBI-1210244, EBI-645361;
CC Q3TKT4; Q8VEK3: Hnrnpu; NbExp=3; IntAct=EBI-1210244, EBI-529674;
CC Q3TKT4; Q9Z2D6: Mecp2; NbExp=2; IntAct=EBI-1210244, EBI-1188816;
CC Q3TKT4; Q01705: Notch1; NbExp=2; IntAct=EBI-1210244, EBI-1392707;
CC Q3TKT4; P11103: Parp1; NbExp=2; IntAct=EBI-1210244, EBI-642213;
CC Q3TKT4; P13405: Rb1; NbExp=3; IntAct=EBI-1210244, EBI-971782;
CC Q3TKT4; P97496: Smarcc1; NbExp=7; IntAct=EBI-1210244, EBI-648047;
CC Q3TKT4; Q6P9Z1: Smarcd3; NbExp=3; IntAct=EBI-1210244, EBI-7525857;
CC Q3TKT4; O70372: Tert; NbExp=2; IntAct=EBI-1210244, EBI-9662790;
CC Q3TKT4; Q01320: Top2a; NbExp=3; IntAct=EBI-1210244, EBI-642809;
CC Q3TKT4; Q6P1E1: Zmiz1; NbExp=2; IntAct=EBI-1210244, EBI-647033;
CC Q3TKT4; Q62908: Csrp2; Xeno; NbExp=3; IntAct=EBI-1210244, EBI-918425;
CC Q3TKT4; P06400: RB1; Xeno; NbExp=4; IntAct=EBI-1210244, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:26138476}. Note=Colocalizes with long non-coding RNA
CC Evf2 in nuclear RNA clouds. {ECO:0000269|PubMed:26138476}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TKT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TKT4-2; Sequence=VSP_038696;
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AK147285; BAE27821.1; -; mRNA.
DR EMBL; AK160825; BAE36034.1; -; mRNA.
DR EMBL; AK166837; BAE39059.1; -; mRNA.
DR EMBL; BC079560; AAH79560.1; -; mRNA.
DR EMBL; CH466522; EDL25209.1; -; Genomic_DNA.
DR CCDS; CCDS22909.1; -. [Q3TKT4-2]
DR CCDS; CCDS57662.1; -. [Q3TKT4-1]
DR RefSeq; NP_001167549.1; NM_001174078.1.
DR RefSeq; NP_001167550.1; NM_001174079.1. [Q3TKT4-1]
DR RefSeq; NP_035547.2; NM_011417.3. [Q3TKT4-2]
DR RefSeq; XP_006510180.2; XM_006510117.2.
DR RefSeq; XP_006510182.2; XM_006510119.2. [Q3TKT4-2]
DR RefSeq; XP_006510183.2; XM_006510120.2. [Q3TKT4-1]
DR AlphaFoldDB; Q3TKT4; -.
DR SMR; Q3TKT4; -.
DR BioGRID; 203336; 91.
DR ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; Q3TKT4; -.
DR DIP; DIP-40650N; -.
DR DIP; DIP-59249N; -.
DR IntAct; Q3TKT4; 49.
DR MINT; Q3TKT4; -.
DR STRING; 10090.ENSMUSP00000034707; -.
DR iPTMnet; Q3TKT4; -.
DR PhosphoSitePlus; Q3TKT4; -.
DR SwissPalm; Q3TKT4; -.
DR EPD; Q3TKT4; -.
DR jPOST; Q3TKT4; -.
DR MaxQB; Q3TKT4; -.
DR PaxDb; Q3TKT4; -.
DR PeptideAtlas; Q3TKT4; -.
DR PRIDE; Q3TKT4; -.
DR ProteomicsDB; 261524; -. [Q3TKT4-1]
DR ProteomicsDB; 261525; -. [Q3TKT4-2]
DR Antibodypedia; 3778; 546 antibodies from 45 providers.
DR DNASU; 20586; -.
DR Ensembl; ENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187. [Q3TKT4-2]
DR Ensembl; ENSMUST00000174008; ENSMUSP00000133922; ENSMUSG00000032187. [Q3TKT4-1]
DR GeneID; 20586; -.
DR KEGG; mmu:20586; -.
DR UCSC; uc009omd.2; mouse. [Q3TKT4-2]
DR UCSC; uc009ome.2; mouse. [Q3TKT4-1]
DR CTD; 6597; -.
DR MGI; MGI:88192; Smarca4.
DR VEuPathDB; HostDB:ENSMUSG00000032187; -.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000156887; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR InParanoid; Q3TKT4; -.
DR OMA; THNKLAV; -.
DR OrthoDB; 685477at2759; -.
DR PhylomeDB; Q3TKT4; -.
DR TreeFam; TF300785; -.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 20586; 20 hits in 82 CRISPR screens.
DR ChiTaRS; Smarca4; mouse.
DR PRO; PR:Q3TKT4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TKT4; protein.
DR Bgee; ENSMUSG00000032187; Expressed in rostral migratory stream and 312 other tissues.
DR ExpressionAtlas; Q3TKT4; baseline and differential.
DR Genevisible; Q3TKT4; MM.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:MGI.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0106222; F:lncRNA binding; IPI:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0035887; P:aortic smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IDA:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0007403; P:glial cell fate determination; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0060347; P:heart trabecula formation; IGI:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR GO; GO:0006334; P:nucleosome assembly; TAS:MGI.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030100; BRG1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF76; PTHR10799:SF76; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; ATP-binding; Bromodomain;
KW Chromatin regulator; Helicase; Hydrolase; Isopeptide bond; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1613
FT /note="Transcription activator BRG1"
FT /id="PRO_0000391343"
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 460..532
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 766..931
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1084..1246
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1443..1513
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..282
FT /note="Necessary for interaction with SS18L1/CREST"
FT /evidence="ECO:0000250"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..728
FT /note="RNA-binding region which is sufficient for binding
FT to lncRNA Evf2"
FT /evidence="ECO:0000269|PubMed:26138476"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..916
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000269|PubMed:26138476"
FT REGION 1247..1413
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000269|PubMed:26138476"
FT REGION 1366..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 881..884
FT /note="DEGH box"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 779..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 1505..1506
FT /note="Required for binding to 'Lys-15'-acetylated histone
FT 3"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT CROSSLNK 1332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT VAR_SEQ 1441
FT /note="D -> DS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_038696"
FT CONFLICT 1355
FT /note="W -> WLKT (in Ref. 1; BAE36034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1613 AA; 181427 MW; C23804ED858F98FE CRC64;
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG
PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV
SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE
MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA
RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE
TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD
GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG
KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK
TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE
DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE
VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR
KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK
DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ
NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK
VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSEEE QEEDRSGSGS EED
