NPAS2_MOUSE
ID NPAS2_MOUSE Reviewed; 816 AA.
AC P97460;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Neuronal PAS domain-containing protein 2;
DE Short=Neuronal PAS2;
GN Name=Npas2;
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 [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9012850; DOI=10.1073/pnas.94.2.713;
RA Zhou Y.-D., Barnard M., Tian H., Li X., Ring H.Z., Francke U., Shelton J.,
RA Richardson J., Russell D.W., McKnight S.L.;
RT "Molecular characterization of two mammalian bHLH-PAS domain proteins
RT selectively expressed in the central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:713-718(1997).
RN [2]
RP FUNCTION.
RX PubMed=12843397; DOI=10.1126/science.1082795;
RA Dudley C.A., Erbel-Sieler C., Estill S.J., Reick M., Franken P., Pitts S.,
RA McKnight S.L.;
RT "Altered patterns of sleep and behavioral adaptability in NPAS2-deficient
RT mice.";
RL Science 301:379-383(2003).
RN [3]
RP INTERACTION WITH EP300, AND INDUCTION.
RX PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA Chakravarti D., FitzGerald G.A., McNamara P.;
RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT clock.";
RL J. Biol. Chem. 279:7091-7097(2004).
RN [4]
RP HEME-BINDING, RESONANCE RAMAN SPECTROSCOPY, AND ACTIVITY REGULATION.
RX PubMed=15797872; DOI=10.1074/jbc.m412350200;
RA Uchida T., Sato E., Sato A., Sagami I., Shimizu T., Kitagawa T.;
RT "CO-dependent activity-controlling mechanism of heme-containing CO-sensor
RT protein, neuronal PAS domain protein 2.";
RL J. Biol. Chem. 280:21358-21368(2005).
RN [5]
RP INTERACTION WITH ARNTL/BMAL1, FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16628007; DOI=10.4161/cc.5.8.2684;
RA Kondratov R.V., Kondratova A.A., Lee C., Gorbacheva V.Y., Chernov M.V.,
RA Antoch M.P.;
RT "Post-translational regulation of circadian transcriptional
RT CLOCK(NPAS2)/BMAL1 complex by CRYPTOCHROMES.";
RL Cell Cycle 5:890-895(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16636276; DOI=10.1073/pnas.0602006103;
RA Franken P., Dudley C.A., Estill S.J., Barakat M., Thomason R., O'Hara B.F.,
RA McKnight S.L.;
RT "NPAS2 as a transcriptional regulator of non-rapid eye movement sleep:
RT genotype and sex interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7118-7123(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17417633; DOI=10.1038/nn1884;
RA DeBruyne J.P., Weaver D.R., Reppert S.M.;
RT "CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian
RT clock.";
RL Nat. Neurosci. 10:543-545(2007).
RN [8]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF HIS-119 AND HIS-171.
RX PubMed=18230344; DOI=10.1016/j.bbrc.2008.01.053;
RA Ishida M., Ueha T., Sagami I.;
RT "Effects of mutations in the heme domain on the transcriptional activity
RT and DNA-binding activity of NPAS2.";
RL Biochem. Biophys. Res. Commun. 368:292-297(2008).
RN [9]
RP FUNCTION.
RX PubMed=18439826; DOI=10.1016/j.cub.2008.04.012;
RA Hampp G., Ripperger J.A., Houben T., Schmutz I., Blex C., Perreau-Lenz S.,
RA Brunk I., Spanagel R., Ahnert-Hilger G., Meijer J.H., Albrecht U.;
RT "Regulation of monoamine oxidase A by circadian-clock components implies
RT clock influence on mood.";
RL Curr. Biol. 18:678-683(2008).
RN [10]
RP REVIEW.
RX PubMed=19147932; DOI=10.1007/s12041-008-0066-7;
RA Debruyne J.P.;
RT "Oscillating perceptions: the ups and downs of the CLOCK protein in the
RT mouse circadian system.";
RL J. Genet. 87:437-446(2008).
RN [11]
RP FUNCTION.
RX PubMed=18316400; DOI=10.1128/mcb.01931-07;
RA Bertolucci C., Cavallari N., Colognesi I., Aguzzi J., Chen Z., Caruso P.,
RA Foa A., Tosini G., Bernardi F., Pinotti M.;
RT "Evidence for an overlapping role of CLOCK and NPAS2 transcription factors
RT in liver circadian oscillators.";
RL Mol. Cell. Biol. 28:3070-3075(2008).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20026146; DOI=10.1016/j.physbeh.2009.12.010;
RA Wu X., Wiater M.F., Ritter S.;
RT "NPAS2 deletion impairs responses to restricted feeding but not to
RT metabolic challenges.";
RL Physiol. Behav. 99:466-471(2010).
RN [13]
RP HEME-BINDING, AND RESONANCE RAMAN SPECTROSCOPY.
RX PubMed=22245004; DOI=10.1016/j.jinorgbio.2011.12.005;
RA Uchida T., Sagami I., Shimizu T., Ishimori K., Kitagawa T.;
RT "Effects of the bHLH domain on axial coordination of heme in the PAS-A
RT domain of neuronal PAS domain protein 2 (NPAS2): conversion from
RT His119/Cys170 coordination to His119/His171 coordination.";
RL J. Inorg. Biochem. 108:188-195(2012).
RN [14]
RP DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=23831463; DOI=10.1016/j.bbrc.2013.06.086;
RA Yoshii K., Ishijima S., Sagami I.;
RT "Effects of NAD(P)H and its derivatives on the DNA-binding activity of
RT NPAS2, a mammalian circadian transcription factor.";
RL Biochem. Biophys. Res. Commun. 437:386-391(2013).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24048828; DOI=10.1523/jneurosci.2039-13.2013;
RA Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R.,
RA Iuvone P.M.;
RT "Circadian rhythm of contrast sensitivity is regulated by a dopamine-
RT neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in
RT retinal ganglion cells.";
RL J. Neurosci. 33:14989-14997(2013).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24067359; DOI=10.1016/j.ymgme.2013.08.015;
RA O'Neil D., Mendez-Figueroa H., Mistretta T.A., Su C., Lane R.H.,
RA Aagaard K.M.;
RT "Dysregulation of Npas2 leads to altered metabolic pathways in a murine
RT knockout model.";
RL Mol. Genet. Metab. 110:378-387(2013).
RN [17]
RP FUNCTION.
RX PubMed=25212631; DOI=10.1002/hep.27437;
RA Lee S.M., Zhang Y., Tsuchiya H., Smalling R., Jetten A.M., Wang L.;
RT "Small heterodimer partner/neuronal PAS domain protein 2 axis regulates the
RT oscillation of liver lipid metabolism.";
RL Hepatology 61:497-505(2015).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=29163035; DOI=10.3389/fnmol.2017.00360;
RA Ozburn A.R., Kern J., Parekh P.K., Logan R.W., Liu Z., Falcon E.,
RA Becker-Krail D., Purohit K., Edgar N.M., Huang Y., McClung C.A.;
RT "NPAS2 regulation of anxiety-like behavior and GABAA receptors.";
RL Front. Mol. Neurosci. 10:360-360(2017).
CC -!- FUNCTION: Transcriptional activator which forms a core component of the
CC circadian clock. The circadian clock, an internal time-keeping system,
CC regulates various physiological processes through the generation of
CC approximately 24 hour circadian rhythms in gene expression, which are
CC translated into rhythms in metabolism and behavior. It is derived from
CC the Latin roots 'circa' (about) and 'diem' (day) and acts as an
CC important regulator of a wide array of physiological functions
CC including metabolism, sleep, body temperature, blood pressure,
CC endocrine, immune, cardiovascular, and renal function. Consists of two
CC major components: the central clock, residing in the suprachiasmatic
CC nucleus (SCN) of the brain, and the peripheral clocks that are present
CC in nearly every tissue and organ system. Both the central and
CC peripheral clocks can be reset by environmental cues, also known as
CC Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the
CC central clock is light, which is sensed by retina and signals directly
CC to the SCN. The central clock entrains the peripheral clocks through
CC neuronal and hormonal signals, body temperature and feeding-related
CC cues, aligning all clocks with the external light/dark cycle. Circadian
CC rhythms allow an organism to achieve temporal homeostasis with its
CC environment at the molecular level by regulating gene expression to
CC create a peak of protein expression once every 24 hours to control when
CC a particular physiological process is most active with respect to the
CC solar day. Transcription and translation of core clock components
CC (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and
CC CRY2) plays a critical role in rhythm generation, whereas delays
CC imposed by post-translational modifications (PTMs) are important for
CC determining the period (tau) of the rhythms (tau refers to the period
CC of a rhythm and is the length, in time, of one complete cycle). A
CC diurnal rhythm is synchronized with the day/night cycle, while the
CC ultradian and infradian rhythms have a period shorter and longer than
CC 24 hours, respectively. Disruptions in the circadian rhythms contribute
CC to the pathology of cardiovascular diseases, cancer, metabolic
CC syndromes and aging. A transcription/translation feedback loop (TTFL)
CC forms the core of the molecular circadian clock mechanism.
CC Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2,
CC form the positive limb of the feedback loop, act in the form of a
CC heterodimer and activate the transcription of core clock genes and
CC clock-controlled genes (involved in key metabolic processes), harboring
CC E-box elements (5'-CACGTG-3') within their promoters. The core clock
CC genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form
CC the negative limb of the feedback loop and interact with the
CC CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its
CC activity and thereby negatively regulating their own expression. This
CC heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G,
CC which form a second feedback loop and which activate and repress
CC ARNTL/BMAL1 transcription, respectively. The NPAS2-ARNTL/BMAL1
CC heterodimer positively regulates the expression of MAOA, F7 and LDHA
CC and modulates the circadian rhythm of daytime contrast sensitivity by
CC regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1)
CC in the retina. NPAS2 plays an important role in sleep homeostasis and
CC in maintaining circadian behaviors in normal light/dark and feeding
CC conditions and in the effective synchronization of feeding behavior
CC with scheduled food availability. Regulates the gene transcription of
CC key metabolic pathways in the liver and is involved in DNA damage
CC response by regulating several cell cycle and DNA repair genes.
CC Controls the circadian rhythm of NR0B2 expression by binding
CC rhythmically to its promoter (PubMed:25212631). Mediates the diurnal
CC variation in the expression of GABARA1 receptor in the brain and
CC contributes to the regulation of anxiety-like behaviors and GABAergic
CC neurotransmission in the ventral striatum (PubMed:29163035).
CC {ECO:0000269|PubMed:12843397, ECO:0000269|PubMed:16628007,
CC ECO:0000269|PubMed:16636276, ECO:0000269|PubMed:17417633,
CC ECO:0000269|PubMed:18230344, ECO:0000269|PubMed:18316400,
CC ECO:0000269|PubMed:18439826, ECO:0000269|PubMed:20026146,
CC ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:24067359,
CC ECO:0000269|PubMed:25212631, ECO:0000269|PubMed:29163035}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:15797872, ECO:0000269|PubMed:22245004};
CC -!- ACTIVITY REGULATION: Carbon monoxide (CO) and the redox state of the
CC cell can modulate the transcriptional activity of the NPAS2-ARNTL/BMAL1
CC heterodimer. NADH and NADPH enhance the DNA-binding activity of the
CC heterodimer whereas CO binds the heme group in NPAS2 and inhibits the
CC DNA-binding activity of the heterodimer. {ECO:0000269|PubMed:15797872,
CC ECO:0000269|PubMed:23831463}.
CC -!- SUBUNIT: Component of the circadian clock oscillator which includes the
CC CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D
CC and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding
CC requires dimerization with another bHLH protein. Interacts with NCOA3,
CC KAT2B and CREBBP (By similarity). Forms a heterodimer with ARNTL/BMAL1
CC and this heterodimerization is required for E-box-dependent
CC transactivation. Interacts with EP300. {ECO:0000250|UniProtKB:Q99743,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:16628007}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:16628007}.
CC -!- TISSUE SPECIFICITY: Expressed in the retinal ganglion cells (at protein
CC level). Expressed in the hypothalamic suprachiasmatic nuclei (SCN) of
CC the brain. Also found in spinal cord, and to a lesser extent in colon,
CC small intestine and uterus. Exhibits a diurnal variation in its
CC expression in the brain (PubMed:29163035).
CC {ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:24048828,
CC ECO:0000269|PubMed:29163035, ECO:0000269|PubMed:9012850}.
CC -!- DEVELOPMENTAL STAGE: First detected 3 days after birth.
CC {ECO:0000269|PubMed:9012850}.
CC -!- INDUCTION: Expression in the retinal ganglion cells and heart
CC oscillates in a circadian manner. {ECO:0000269|PubMed:14645221,
CC ECO:0000269|PubMed:24048828}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit altered sleep and locomotor
CC activity. Show alterations in sleep homeostasis, altering the
CC electrophysiological properties of neurons after sleep deprivation.
CC Display normal patterns of sleep throughout the light period, however
CC during the active, nocturnal period, they remain awake nearly
CC continuously for the first 8 to 9 hours of darkness and tend to fast
CC rather than readapt to eating in daylight. Exhibit a dysregulation in
CC the lipid and fatty acid metabolism pathways and a significant
CC reduction in daytime contrast sensitivity. Null mutant mice and the
CC mice with a conditional knockdown in the ventral striatum show a
CC reduced anxiety-like behavior and a reduced sensitivity to diazepam
CC (PubMed:29163035). {ECO:0000269|PubMed:16636276,
CC ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:20026146,
CC ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:24067359,
CC ECO:0000269|PubMed:29163035}.
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DR EMBL; U77969; AAB47249.1; -; mRNA.
DR CCDS; CCDS48244.1; -.
DR RefSeq; NP_032745.2; NM_008719.2.
DR AlphaFoldDB; P97460; -.
DR BMRB; P97460; -.
DR SMR; P97460; -.
DR IntAct; P97460; 1.
DR MINT; P97460; -.
DR STRING; 10090.ENSMUSP00000054719; -.
DR PhosphoSitePlus; P97460; -.
DR MaxQB; P97460; -.
DR PaxDb; P97460; -.
DR PRIDE; P97460; -.
DR ProteomicsDB; 293877; -.
DR DNASU; 18143; -.
DR GeneID; 18143; -.
DR KEGG; mmu:18143; -.
DR CTD; 4862; -.
DR MGI; MGI:109232; Npas2.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; P97460; -.
DR OrthoDB; 205871at2759; -.
DR PhylomeDB; P97460; -.
DR BioGRID-ORCS; 18143; 2 hits in 112 CRISPR screens.
DR ChiTaRS; Npas2; mouse.
DR PRO; PR:P97460; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97460; protein.
DR GO; GO:1990513; C:CLOCK-BMAL transcription complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0042745; P:circadian sleep/wake cycle; IMP:MGI.
DR GO; GO:0045475; P:locomotor rhythm; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051775; P:response to redox state; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; DNA damage; DNA-binding; Heme; Iron;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..816
FT /note="Neuronal PAS domain-containing protein 2"
FT /id="PRO_0000127407"
FT DOMAIN 9..59
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 82..152
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 237..307
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 311..354
FT /note="PAC"
FT REGION 1..61
FT /note="Sufficient for heterodimer formation with
FT ARNTL/BMAL1, E-box binding and for the effect of NADPH"
FT /evidence="ECO:0000269|PubMed:23831463"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:15797872,
FT ECO:0000269|PubMed:22245004"
FT BINDING 171
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:15797872,
FT ECO:0000269|PubMed:22245004"
FT MUTAGEN 119
FT /note="H->A: Significant decrease in DNA binding affinity
FT resulting in a loss of the transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18230344"
FT MUTAGEN 171
FT /note="H->A: Significant decrease in DNA binding affinity
FT resulting in a loss of the transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18230344"
SQ SEQUENCE 816 AA; 90916 MW; 7E5CF0641CFDC1DD CRC64;
MDEDEKDRAK RASRNKSEKK RRDQFNVLIK ELSSMLPGNT RKMDKTTVLE KVIGFLQKHN
EVSAQTEICD IQQDWKPSFL SNEEFTQLML EALDGFVIVV TTDGSIIYVS DSITPLLGHL
PADVMDQNLL NFLPEQEHSE VYKILSSHML VTDSPSPEFL KSDNDLEFYC HLLRGSLNPK
EFPTYEYIKF VGNFRSYNNV PSPSCNGFDN TLSRPCHVPL GKDVCFIATV RLATPQFLKE
MCVADEPLEE FTSRHSLEWK FLFLDHRAPP IIGYLPFEVL GTSGYNYYHI DDLELLARCH
QHLMQFGKGK SCCYRFLTKG QQWIWLQTHY YITYHQWNSK PEFIVCTHSV VSYADVRVER
RQELALEDPP TEAMHPSAVK EKDSSLEPPQ PFNALDMGAS GLPSSPSPSA SSRSSHKSSH
TAMSEPTSTP TKLMAENSTT ALPRPATLPQ ELPVQGLSQA ATMPTALHSS ASCDLTKQLL
LQSLPQTGLQ SPPAPVTQFS AQFSMFQTIK DQLEQRTRIL QANIRWQQEE LHKIQEQLCL
VQDSNVQMFL QQPAVSLSFS STQRPAAQQQ LQQRPAAPSQ PQLVVNTPLQ GQITSTQVTN
QHLLRESNVI SAQGPKPMRS SQLLPASGRS LSSLPSQFSS TASVLPPGLS LTTIAPTPQD
DSQCQPSPDF GHDRQLRLLL SQPIQPMMPG SCDARQPSEV SRTGRQVKYA QSQVMFPSPD
SHPTNSSAST PVLLMGQAVL HPSFPASRPS PLQPAQAQQQ PPPYLQAPTS LHSEQPDSLL
LSTFSQQPGT LGYAATQSTP PQPPRPSRRV SRLSES
