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 24-JAN-2024, entry version 169. 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 BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in CC rhythm generation, whereas delays imposed by post-translational CC modifications (PTMs) are important for determining the period (tau) of CC the rhythms (tau refers to the period of a rhythm and is the length, in CC time, of one complete cycle). A diurnal rhythm is synchronized with the CC day/night cycle, while the ultradian and infradian rhythms have a CC period shorter and longer than 24 hours, respectively. Disruptions in CC the circadian rhythms contribute to the pathology of cardiovascular CC diseases, cancer, metabolic syndromes and aging. A CC transcription/translation feedback loop (TTFL) forms the core of the CC molecular circadian clock mechanism. Transcription factors, CLOCK or CC NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, CC act in the form of a heterodimer and activate the transcription of core CC clock genes and clock-controlled genes (involved in key metabolic CC processes), harboring E-box elements (5'-CACGTG-3') within their CC promoters. The core clock genes: PER1/2/3 and CRY1/2 which are CC transcriptional repressors form the negative limb of the feedback loop CC and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting CC its activity and thereby negatively regulating their own expression. CC This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, CC RORB and RORG, which form a second feedback loop and which activate and CC repress BMAL1 transcription, respectively. Has a redundant role with CC the other PER proteins PER1 and PER2 and is not essential for the CC circadian rhythms maintenance. In contrast, plays an important role in CC sleep-wake timing and sleep homeostasis probably through the CC transcriptional regulation of sleep homeostasis-related genes, without CC 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, BMAL1 or BMAL2, CSNK1D CC and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with CC PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and CRY2 is CC 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}. 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; 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; 10090-ENSMUSP00000099493; -. DR ProteomicsDB; 289348; -. DR Antibodypedia; 13182; 243 antibodies from 32 providers. DR DNASU; 18628; -. DR Ensembl; ENSMUST00000103204.11; ENSMUSP00000099493.5; ENSMUSG00000028957.13. DR GeneID; 18628; -. DR KEGG; mmu:18628; -. DR UCSC; uc008vye.2; mouse. DR AGR; MGI:1277134; -. 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; EYQCVAG; -. DR PhylomeDB; O70361; -. DR TreeFam; TF318445; -. DR BioGRID-ORCS; 18628; 1 hit in 77 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 214 other cell types or tissues. DR ExpressionAtlas; O70361; baseline and differential. 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 Gene3D; 3.30.450.20; PAS domain; 2. DR InterPro; IPR000014; PAS. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013655; PAS_fold_3. DR InterPro; IPR048814; Per1-3_PAS-A. DR InterPro; IPR022728; Period_circadian-like_C. DR PANTHER; PTHR11269; PERIOD CIRCADIAN PROTEIN; 1. DR PANTHER; PTHR11269:SF13; PERIOD CIRCADIAN PROTEIN HOMOLOG 3; 1. DR Pfam; PF08447; PAS_3; 1. DR Pfam; PF21353; Per3-like_PAS-A; 1. DR Pfam; PF12114; Period_C; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50112; PAS; 1. DR Genevisible; O70361; MM. 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 //