PER3_MOUSE
ID PER3_MOUSE Reviewed; 1113 AA.
AC O70361; A2A894;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Period circadian protein homolog 3;
DE Short=mPER3;
DE AltName: Full=Circadian clock protein PERIOD 3;
GN Name=Per3;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9655499; DOI=10.1016/s0896-6273(00)80492-4;
RA Zylka M.J., Shearman L.P., Weaver D.R., Reppert S.M.;
RT "Three period homologs in mammals: differential light responses in the
RT suprachiasmatic circadian clock and oscillating transcripts outside of
RT brain.";
RL Neuron 20:1103-1110(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP HOMODIMERIZATION, INTERACTION WITH PER1; PER2; CRY1 AND CRY2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10428031; DOI=10.1016/s0092-8674(00)81014-4;
RA Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X.,
RA Maywood E.S., Hastings M.H., Reppert S.M.;
RT "mCRY1 and mCRY2 are essential components of the negative limb of the
RT circadian clock feedback loop.";
RL Cell 98:193-205(1999).
RN [4]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=11591712; DOI=10.1074/jbc.m107726200;
RA Vielhaber E.L., Duricka D., Ullman K.S., Virshup D.M.;
RT "Nuclear export of mammalian PERIOD proteins.";
RL J. Biol. Chem. 276:45921-45927(2001).
RN [5]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND DISRUPTION PHENOTYPE.
RX PubMed=11395012; DOI=10.1016/s0896-6273(01)00302-6;
RA Bae K., Jin X., Maywood E.S., Hastings M.H., Reppert S.M., Weaver D.R.;
RT "Differential functions of mPer1, mPer2, and mPer3 in the SCN circadian
RT clock.";
RL Neuron 30:525-536(2001).
RN [6]
RP INTERACTION WITH CSNK1D AND CSNK1E, PHOSPHORYLATION, UBIQUITINATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11865049; DOI=10.1128/mcb.22.6.1693-1703.2002;
RA Akashi M., Tsuchiya Y., Yoshino T., Nishida E.;
RT "Control of intracellular dynamics of mammalian period proteins by casein
RT kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells.";
RL Mol. Cell. Biol. 22:1693-1703(2002).
RN [7]
RP INTERACTION WITH TIMELESS, AND INDUCTION.
RX PubMed=14564007; DOI=10.1126/science.1086593;
RA Barnes J.W., Tischkau S.A., Barnes J.A., Mitchell J.W., Burgoon P.W.,
RA Hickok J.R., Gillette M.U.;
RT "Requirement of mammalian Timeless for circadian rhythmicity.";
RL Science 302:439-442(2003).
RN [8]
RP INTERACTION WITH PER1; PER2; CRY1 AND CRY2, PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=14701732; DOI=10.1128/mcb.24.2.584-594.2004;
RA Lee C., Weaver D.R., Reppert S.M.;
RT "Direct association between mouse PERIOD and CKIepsilon is critical for a
RT functioning circadian clock.";
RL Mol. Cell. Biol. 24:584-594(2004).
RN [9]
RP INTERACTION WITH FBXW11 AND BTRC, AND MUTAGENESIS OF 613-S--S-627.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [10]
RP FUNCTION IN SLEEP HOMEOSTASIS, AND DISRUPTION PHENOTYPE.
RX PubMed=21957163; DOI=10.1152/ajpregu.00260.2011;
RA Hasan S., van der Veen D.R., Winsky-Sommerer R., Dijk D.J., Archer S.N.;
RT "Altered sleep and behavioral activity phenotypes in PER3-deficient mice.";
RL Am. J. Physiol. 301:R1821-R1830(2011).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=26903630; DOI=10.1073/pnas.1600039113;
RA Zhang L., Hirano A., Hsu P.K., Jones C.R., Sakai N., Okuro M., McMahon T.,
RA Yamazaki M., Xu Y., Saigoh N., Saigoh K., Lin S.T., Kaasik K., Nishino S.,
RA Ptacek L.J., Fu Y.H.;
RT "A PERIOD3 variant causes a circadian phenotype and is associated with a
RT seasonal mood trait.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1536-E1544(2016).
RN [12]
RP REVIEW.
RX PubMed=23303907; DOI=10.1152/physrev.00016.2012;
RA Eckel-Mahan K., Sassone-Corsi P.;
RT "Metabolism and the circadian clock converge.";
RL Physiol. Rev. 93:107-135(2013).
RN [13]
RP REVIEW.
RX PubMed=23916625; DOI=10.1016/j.tcb.2013.07.002;
RA Partch C.L., Green C.B., Takahashi J.S.;
RT "Molecular architecture of the mammalian circadian clock.";
RL Trends Cell Biol. 24:90-99(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 108-411, FUNCTION IN HEME BINDING,
RP SUBUNIT, AND MUTAGENESIS OF TRP-359 AND ILE-367.
RX PubMed=22331899; DOI=10.1073/pnas.1113280109;
RA Kucera N., Schmalen I., Hennig S., Ollinger R., Strauss H.M.,
RA Grudziecki A., Wieczorek C., Kramer A., Wolf E.;
RT "Unwinding the differences of the mammalian PERIOD clock proteins from
RT crystal structure to cellular function.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3311-3316(2012).
CC -!- FUNCTION: Originally described as a core component of the circadian
CC clock. The circadian clock, an internal time-keeping system, regulates
CC various physiological processes through the generation of approximately
CC 24 hour circadian rhythms in gene expression, which are translated into
CC rhythms in metabolism and behavior. It is derived from the Latin roots
CC 'circa' (about) and 'diem' (day) and acts as an important regulator of
CC a wide array of physiological functions including metabolism, sleep,
CC body temperature, blood pressure, endocrine, immune, cardiovascular,
CC and renal function. Consists of two major components: the central
CC clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and
CC the peripheral clocks that are present in nearly every tissue and organ
CC system. Both the central and peripheral clocks can be reset by
CC environmental cues, also known as Zeitgebers (German for 'timegivers').
CC The predominant Zeitgeber for the central clock is light, which is
CC sensed by retina and signals directly to the SCN. The central clock
CC entrains the peripheral clocks through neuronal and hormonal signals,
CC body temperature and feeding-related cues, aligning all clocks with the
CC external light/dark cycle. Circadian rhythms allow an organism to
CC achieve temporal homeostasis with its environment at the molecular
CC level by regulating gene expression to create a peak of protein
CC expression once every 24 hours to control when a particular
CC physiological process is most active with respect to the solar day.
CC Transcription and translation of core clock components (CLOCK, NPAS2,
CC ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a
CC critical role in rhythm generation, whereas delays imposed by post-
CC translational modifications (PTMs) are important for determining the
CC period (tau) of the rhythms (tau refers to the period of a rhythm and
CC is the length, in time, of one complete cycle). A diurnal rhythm is
CC synchronized with the day/night cycle, while the ultradian and
CC infradian rhythms have a period shorter and longer than 24 hours,
CC respectively. Disruptions in the circadian rhythms contribute to the
CC pathology of cardiovascular diseases, cancer, metabolic syndromes and
CC aging. A transcription/translation feedback loop (TTFL) forms the core
CC of the molecular circadian clock mechanism. Transcription factors,
CC CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb
CC of the feedback loop, act in the form of a heterodimer and activate the
CC transcription of core clock genes and clock-controlled genes (involved
CC in key metabolic processes), harboring E-box elements (5'-CACGTG-3')
CC within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which
CC are transcriptional repressors form the negative limb of the feedback
CC loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2
CC heterodimer inhibiting its activity and thereby negatively regulating
CC their own expression. This heterodimer also activates nuclear receptors
CC NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop
CC and which activate and repress ARNTL/BMAL1 transcription, respectively.
CC Has a redundant role with the other PER proteins PER1 and PER2 and is
CC not essential for the circadian rhythms maintenance. In contrast, plays
CC an important role in sleep-wake timing and sleep homeostasis probably
CC through the transcriptional regulation of sleep homeostasis-related
CC genes, without influencing circadian parameters. Can bind heme.
CC {ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:21957163,
CC ECO:0000269|PubMed:22331899}.
CC -!- SUBUNIT: Homodimer. Component of the circadian core oscillator, which
CC includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2,
CC CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly
CC with PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and
CC CRY2 is weak and not rhythmic. Interacts with FBXW11 and BTRC.
CC {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11865049,
CC ECO:0000269|PubMed:14564007, ECO:0000269|PubMed:14701732,
CC ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:22331899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428031,
CC ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049,
CC ECO:0000269|PubMed:14701732}. Nucleus {ECO:0000269|PubMed:10428031,
CC ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049,
CC ECO:0000269|PubMed:14701732}. Note=Mainly cytoplasmic. Translocates to
CC the nucleus through binding PER1, PER2, CRY1 or CRY2, but not TIMELESS.
CC {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712,
CC ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, lung,
CC liver, skeletal muscle, testis, and at low level in the spleen and
CC kidney. In brain, mainly found in the SCN, hippocampus, piriform
CC cortex, and cerebellum. Lower level of expression in the neocortex.
CC Expression exhibits synchronous oscillations in liver, skeletal muscle
CC and testis. {ECO:0000269|PubMed:14701732, ECO:0000269|PubMed:9655499}.
CC -!- INDUCTION: Exhibits circadian oscillation expression in SCN, liver,
CC skeletal muscle, testis and eyes. In the SCN, highest levels during
CC subjective day at CT6 and CT9, lowest levels at night, CT15, CT18 and
CC CT 21. In the liver, skeletal muscle, testis and eyes highest levels at
CC CT15, CT15-CT18, CT9 and CT15, and CT9-CT15, respectively. During
CC subjective night, unresponsive to light exposure.
CC {ECO:0000269|PubMed:14564007, ECO:0000269|PubMed:14701732,
CC ECO:0000269|PubMed:9655499}.
CC -!- PTM: Phosphorylation by CSNK1E is weak and appears to require
CC association with PER1 and translocation to the nucleus.
CC {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:11865049}.
CC -!- DISRUPTION PHENOTYPE: Animals show altered sleep and behavioral
CC activity whitout changes in total activity or vigilance states. They
CC have increased wheel-running activity and reduced REM (rapid eye
CC movement) sleep and NREM (non-REM) sleep in the middle of the dark
CC phase. At the beginning of the baseline light period, they have less
CC wakefulness and more REM and NREM sleep. Mice spend less time in
CC wakefulness and more time in NREM sleep on the light period immediately
CC after sleep deprivation and REM sleep accumulates more slowly during
CC the recovery dark phase. They also display a depression-like phenotype.
CC Double knocknouts for PER2 and PER3 show the same phenotype as PER2
CC knockouts with severely disrupted circadian behavior.
CC {ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:21957163,
CC ECO:0000269|PubMed:26903630}.
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DR EMBL; AF050182; AAC40147.1; -; mRNA.
DR EMBL; AL607143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18978.1; -.
DR PIR; T14260; T14260.
DR RefSeq; NP_035197.2; NM_011067.3.
DR PDB; 4DJ3; X-ray; 2.50 A; A/B=108-411.
DR PDBsum; 4DJ3; -.
DR AlphaFoldDB; O70361; -.
DR SMR; O70361; -.
DR BioGRID; 202113; 9.
DR ComplexPortal; CPX-3217; Cry1-Per3 complex.
DR ComplexPortal; CPX-3218; Cry2-Per3 complex.
DR DIP; DIP-60820N; -.
DR IntAct; O70361; 4.
DR STRING; 10090.ENSMUSP00000099493; -.
DR iPTMnet; O70361; -.
DR PhosphoSitePlus; O70361; -.
DR PaxDb; O70361; -.
DR PRIDE; O70361; -.
DR ProteomicsDB; 289348; -.
DR Antibodypedia; 13182; 212 antibodies from 32 providers.
DR DNASU; 18628; -.
DR Ensembl; ENSMUST00000103204; ENSMUSP00000099493; ENSMUSG00000028957.
DR GeneID; 18628; -.
DR KEGG; mmu:18628; -.
DR UCSC; uc008vye.2; mouse.
DR CTD; 8863; -.
DR MGI; MGI:1277134; Per3.
DR VEuPathDB; HostDB:ENSMUSG00000028957; -.
DR eggNOG; KOG3753; Eukaryota.
DR GeneTree; ENSGT00940000160817; -.
DR HOGENOM; CLU_006667_0_1_1; -.
DR InParanoid; O70361; -.
DR OMA; EQVLMTY; -.
DR OrthoDB; 331262at2759; -.
DR PhylomeDB; O70361; -.
DR TreeFam; TF318445; -.
DR BioGRID-ORCS; 18628; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Per3; mouse.
DR PRO; PR:O70361; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O70361; protein.
DR Bgee; ENSMUSG00000028957; Expressed in ciliary body and 212 other tissues.
DR ExpressionAtlas; O70361; baseline and differential.
DR Genevisible; O70361; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IDA:MGI.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR015524; Per_circ_prot_3.
DR InterPro; IPR022728; Period_circadian-like_C.
DR PANTHER; PTHR11269:SF13; PTHR11269:SF13; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12114; Period_C; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1113
FT /note="Period circadian protein homolog 3"
FT /id="PRO_0000162634"
FT DOMAIN 120..187
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 258..324
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 333..376
FT /note="PAC"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..750
FT /note="CSNK1E binding domain"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1113
FT /note="CRY binding domain"
FT /evidence="ECO:0000250"
FT MOTIF 54..63
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 399..408
FT /note="Nuclear export signal 3"
FT /evidence="ECO:0000250"
FT MOTIF 719..735
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 913..920
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 418..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56645"
FT MUTAGEN 359
FT /note="W->E: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:22331899"
FT MUTAGEN 367
FT /note="I->E: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:22331899"
FT MUTAGEN 613..627
FT /note="SVASGISQCSCSSTS->AVAAGIAQCACAATA: No effect on
FT interaction with BTRC and FBXW11."
FT /evidence="ECO:0000269|PubMed:15917222"
FT CONFLICT 967
FT /note="Q -> H (in Ref. 1; AAC40147)"
FT /evidence="ECO:0000305"
FT CONFLICT 1107
FT /note="H -> R (in Ref. 1; AAC40147)"
FT /evidence="ECO:0000305"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4DJ3"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:4DJ3"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4DJ3"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:4DJ3"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 345..356
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:4DJ3"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4DJ3"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:4DJ3"
SQ SEQUENCE 1113 AA; 120911 MW; 99B06113BAB743C7 CRC64;
MDPCGDPAVP GGDCPQTRGP GLQGASGQEG PLQGTCVDSS HSEHEDRNRM SEELIMVVQE
MKKYFPAERH TKPSTLDALN YALRCVHSVQ ANSDFFQSLG PRGAHQADVT VYSLEDLTAL
ASEHTSKNTD TFAAVFSFLS GRLVHISEQA ALILNSKRGF LKSVHFVDLL APQDVRAFYA
HTAPTQLPFW NNWTQRASQY ECAPAKPFFC RICGGGDREK RHYSPFRILP YLVHVHSSAQ
PEPEPCCLTL VEKIHSGYEA PRIPVDKRIF TTTHTPGCVF LEVDERAVPL LGYLPQDLIG
TSILTYLHPE DRPLMVAIHQ KVLKYAGHPP FEHSPVRFCT QNGEYVILDS SWSSFVNPWS
RKVSFIIGRH KVRTSPLNED VFATRIKKAA SNDKDIAELQ EQIHKLLLQP VHASASSGYG
SLGSSGSQEQ HVSITSSSES SGHCPEEGQH EQMTLQQVYA SVNKIKNVGQ QLYIESMARS
SVKPVAETCV EPQGGDEQKD FSSSQTLKNK STTDTGSGGN LQQEQPSSSY QQMNCIDSVI
RYLTSYSLPA LKRKCISCTN TSSSSEEAKP IPEVDSSQRD TEQLLDIRKQ ETTGPSTDIE
GGAARTLSTA ALSVASGISQ CSCSSTSGHA PPLQSESVAV ACKPWALRTK ASHLAAGGFK
HVGLTAAVLS AHTQKEEQNY VDRFREKILT SPYGCYLQQE SRNRAQYSCV QAGSTAKHSR
CAGSERQKHK RKKLPAPVDT SSPGAHLCPH VTGLLPDEQH WGPSASPSPL GAGLAFPSAL
VVPSQTPYLL PSFPLQDMAS QGVGVSAAWG AAAGCPPLSA GPQAVAAFPS AYVDTLMTIF
LHNAPLFPLW PPSFSPYPSL GAAGSSELAP LVPAMAPNPE PTTSGHSQRR VEENWEAHSE
ELPFISSRSS SPLQLNLLQE EMPAPSESAD AVRRGAGPDA KHHCVTGPSG SRSRHCTSGE
LATATAQQES AAASGSSASS IYFSSTDYAS EVSENRQRPQ DRQRDEALPG AAEESIWRMI
ERTPECVLMT YQVPERGREE VLKQDLEKLQ SMEQQQPLFS PAQREELAKV RSWIHSHTAP
QEGHLQSCVA CEDRGSVGDT AEVLEQHPAE DTS
