(data stored in ACNUC13479 zone)

SWISSPROT: PHYB_ARATH

ID   PHYB_ARATH              Reviewed;        1172 AA.
AC   P14713; Q6S4P0;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAY-2019, entry version 187.
DE   RecName: Full=Phytochrome B {ECO:0000303|PubMed:2606345};
DE   AltName: Full=Protein LONG HYPOCOTYL 3 {ECO:0000303|PubMed:8453299};
DE   AltName: Full=Protein OUT OF PHASE 1 {ECO:0000303|PubMed:12177480};
GN   Name=PHYB {ECO:0000303|PubMed:2606345};
GN   Synonyms=HY3 {ECO:0000303|PubMed:8453299},
GN   OOP1 {ECO:0000303|PubMed:12177480};
GN   OrderedLocusNames=At2g18790 {ECO:0000312|Araport:AT2G18790};
GN   ORFNames=MSF3.17 {ECO:0000312|EMBL:AAD08948.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=2606345; DOI=10.1101/gad.3.11.1745;
RA   Sharrock R.A., Quail P.H.;
RT   "Novel phytochrome sequences in Arabidopsis thaliana: structure,
RT   evolution, and differential expression of a plant regulatory
RT   photoreceptor family.";
RL   Genes Dev. 3:1745-1757(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8453299; DOI=10.1105/tpc.5.2.147;
RA   Reed J.W., Nagpal P., Poole D.S., Furuya M., Chory J.;
RT   "Mutations in the gene for the red/far-red light receptor phytochrome
RT   B alter cell elongation and physiological responses throughout
RT   Arabidopsis development.";
RL   Plant Cell 5:147-157(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 9-GLY--ARG-12 DEL;
RP   GLU-19; ILE-143; VAL-980 AND LEU-1072.
RC   STRAIN=cv. Kas-1;
RX   PubMed=15238539; DOI=10.1534/genetics.103.024810;
RA   Wolyn D.J., Borevitz J.O., Loudet O., Schwartz C., Maloof J.,
RA   Ecker J.R., Berry C.C., Chory J.;
RT   "Light-response quantitative trait loci identified with composite
RT   interval and eXtreme array mapping in Arabidopsis thaliana.";
RL   Genetics 167:907-917(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   INTERACTION WITH ADO1.
RX   PubMed=11260718; DOI=10.1038/35068589;
RA   Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M.,
RA   Ecker J.R., Cashmore A.R.;
RT   "An Arabidopsis circadian clock component interacts with both CRY1 and
RT   phyB.";
RL   Nature 410:487-490(2001).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH FYPP3.
RX   PubMed=12468726; DOI=10.1105/tpc.005306;
RA   Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S.,
RA   Park C.-M.;
RT   "A phytochrome-associated protein phosphatase 2A modulates light
RT   signals in flowering time control in Arabidopsis.";
RL   Plant Cell 14:3043-3056(2002).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12177480; DOI=10.1104/pp.003418;
RA   Salome P.A., Michael T.P., Kearns E.V., Fett-Neto A.G., Sharrock R.A.,
RA   McClung C.R.;
RT   "The out of phase 1 mutant defines a role for PHYB in circadian phase
RT   control in Arabidopsis.";
RL   Plant Physiol. 129:1674-1685(2002).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAPP5.
RX   PubMed=15707897; DOI=10.1016/j.cell.2004.12.019;
RA   Ryu J.S., Kim J.-I., Kunkel T., Kim B.C., Cho D.S., Hong S.H.,
RA   Kim S.-H., Fernandez A.P., Kim Y., Alonso J.M., Ecker J.R., Nagy F.,
RA   Lim P.O., Song P.-S., Schaefer E., Nam H.G.;
RT   "Phytochrome-specific type 5 phosphatase controls light signal flux by
RT   enhancing phytochrome stability and affinity for a signal
RT   transducer.";
RL   Cell 120:395-406(2005).
RN   [10]
RP   INTERACTION WITH PKS4.
RX   PubMed=18390804; DOI=10.1104/pp.108.118166;
RA   Schepens I., Boccalandro H.E., Kami C., Casal J.J., Fankhauser C.;
RT   "PHYTOCHROME KINASE SUBSTRATE4 modulates phytochrome-mediated control
RT   of hypocotyl growth orientation.";
RL   Plant Physiol. 147:661-671(2008).
RN   [11]
RP   INTERACTION WITH PTAC12/HMR, AND MUTAGENESIS OF TYR-276.
RC   STRAIN=cv. Columbia;
RX   PubMed=22895253; DOI=10.1101/gad.193219.112;
RA   Galvao R.M., Li M., Kothadia S.M., Haskel J.D., Decker P.V.,
RA   Van Buskirk E.K., Chen M.;
RT   "Photoactivated phytochromes interact with HEMERA and promote its
RT   accumulation to establish photomorphogenesis in Arabidopsis.";
RL   Genes Dev. 26:1851-1863(2012).
RN   [12]
RP   INTERACTION WITH CRYA.
RX   PubMed=22577138; DOI=10.1074/jbc.M112.360545;
RA   Hughes R.M., Vrana J.D., Song J., Tucker C.L.;
RT   "Light-dependent, dark-promoted interaction between Arabidopsis
RT   cryptochrome 1 and phytochrome B proteins.";
RL   J. Biol. Chem. 287:22165-22172(2012).
RN   [13]
RP   INTERACTION WITH VOZ1 AND VOZ2.
RX   PubMed=22904146; DOI=10.1105/tpc.112.101915;
RA   Yasui Y., Mukougawa K., Uemoto M., Yokofuji A., Suzuri R.,
RA   Nishitani A., Kohchi T.;
RT   "The phytochrome-interacting VASCULAR PLANT ONE-ZINC FINGER1 and VOZ2
RT   redundantly regulate flowering in Arabidopsis.";
RL   Plant Cell 24:3248-3263(2012).
RN   [14]
RP   INTERACTION WITH PHL, AND SUBCELLULAR LOCATION.
RX   PubMed=24127609; DOI=10.1073/pnas.1310631110;
RA   Endo M., Tanigawa Y., Murakami T., Araki T., Nagatani A.;
RT   "PHYTOCHROME-DEPENDENT LATE-FLOWERING accelerates flowering through
RT   physical interactions with phytochrome B and CONSTANS.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18017-18022(2013).
RN   [15]
RP   INTERACTION WITH PIF4 AND PIF5.
RX   PubMed=26724867; DOI=10.1016/j.cell.2015.12.018;
RA   Pedmale U.V., Huang S.S., Zander M., Cole B.J., Hetzel J., Ljung K.,
RA   Reis P.A., Sridevi P., Nito K., Nery J.R., Ecker J.R., Chory J.;
RT   "Cryptochromes interact directly with PIFs to control plant growth in
RT   limiting blue light.";
RL   Cell 164:233-245(2016).
RN   [16]
RP   FUNCTION, MUTAGENESIS OF TYR-276, AND INDUCTION BY TEMPERATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=27789797; DOI=10.1126/science.aaf6005;
RA   Jung J.-H., Domijan M., Klose C., Biswas S., Ezer D., Gao M.,
RA   Khattak A.K., Box M.S., Charoensawan V., Cortijo S., Kumar M.,
RA   Grant A., Locke J.C.W., Schaefer E., Jaeger K.E., Wigge P.A.;
RT   "Phytochromes function as thermosensors in Arabidopsis.";
RL   Science 354:886-889(2016).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 90-624 IN COMPLEX WITH
RP   PHYTOCHROMOBILIN, AND HOMODIMERIZATION.
RX   PubMed=24982198; DOI=10.1073/pnas.1403096111;
RA   Burgie E.S., Bussell A.N., Walker J.M., Dubiel K., Vierstra R.D.;
RT   "Crystal structure of the photosensing module from a red/far-red
RT   light-absorbing plant phytochrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:10179-10184(2014).
CC   -!- FUNCTION: Regulatory photoreceptor which exists in two forms that
CC       are reversibly interconvertible by light: the Pr form that absorbs
CC       maximally in the red region of the spectrum and the Pfr form that
CC       absorbs maximally in the far-red region. Photoconversion of Pr to
CC       Pfr induces an array of morphogenetic responses, whereas
CC       reconversion of Pfr to Pr cancels the induction of those
CC       responses. Pfr controls the expression of a number of nuclear
CC       genes including those encoding the small subunit of ribulose-
CC       bisphosphate carboxylase, chlorophyll A/B binding protein,
CC       protochlorophyllide reductase, rRNA, etc. It also controls the
CC       expression of its own gene(s) in a negative feedback fashion.
CC       Involved in the flowering time regulation. Involved in light-
CC       regulated circadian phase control that triggers stomatal aperture,
CC       stomatal conductance, and CO(2) assimilation. Implicated in red
CC       light perception, and, to a lower extent, in blue light signaling
CC       (PubMed:12177480). Regulates temperature responses by associating
CC       with the promoters of key target genes in a temperature-dependent
CC       manner and subsequently repressing their expression probably in a
CC       PIF4-dependent manner. Thermal timer that integrates temperature
CC       information over the course of the night (PubMed:27789797).
CC       {ECO:0000269|PubMed:12177480, ECO:0000269|PubMed:12468726,
CC       ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:27789797}.
CC   -!- SUBUNIT: Homodimer (PubMed:24982198). Interacts with ADO1 and
CC       PKS4. Stabilized by interactions with PAPP5 and FYPP3 which are
CC       enhanced in the phosphorylated Pfr form. Interacts with VOZ1 and
CC       VOZ2 (PubMed:11260718, PubMed:12468726, PubMed:15707897,
CC       PubMed:18390804, PubMed:22904146). Binds, via its photosensory
CC       domain, to PTAC12/HMR when photoactivated; this interaction
CC       stimulates its localization to photobodies (PubMed:22895253).
CC       Interacts with CRY1 specifically when in the dark/far-red (Pr)
CC       state, but not when red light-activated (Pfr) (PubMed:22577138).
CC       Interacts with PIF4 AND PIF5 in response to low blue light (LBL)
CC       (PubMed:26724867). Component of a red light-dependent nuclear
CC       complex made of PHL, PHYB and CO. Interacts directly with PHL
CC       (PubMed:24127609). {ECO:0000269|PubMed:11260718,
CC       ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15707897,
CC       ECO:0000269|PubMed:18390804, ECO:0000269|PubMed:22577138,
CC       ECO:0000269|PubMed:22895253, ECO:0000269|PubMed:22904146,
CC       ECO:0000269|PubMed:24127609, ECO:0000269|PubMed:24982198,
CC       ECO:0000269|PubMed:26724867}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-300727, EBI-300727;
CC       O82798:ARR4; NbExp=3; IntAct=EBI-300727, EBI-625213;
CC       Q96524:CRY2; NbExp=3; IntAct=EBI-300727, EBI-531555;
CC       P14714:PHYC; NbExp=5; IntAct=EBI-300727, EBI-624366;
CC       P42497:PHYD; NbExp=6; IntAct=EBI-300727, EBI-624382;
CC       P42498:PHYE; NbExp=5; IntAct=EBI-300727, EBI-624404;
CC       Q8GZM7:PIF1; NbExp=3; IntAct=EBI-300727, EBI-630400;
CC       O80536:PIF3; NbExp=22; IntAct=EBI-300727, EBI-625701;
CC       Q8W2F3-2:PIF4; NbExp=3; IntAct=EBI-300727, EBI-625732;
CC       Q9SWI1:PKS1; NbExp=2; IntAct=EBI-300727, EBI-626200;
CC       Q9SGQ0:VOZ1; NbExp=4; IntAct=EBI-300727, EBI-6306928;
CC       Q9SLB9:VOZ2; NbExp=4; IntAct=EBI-300727, EBI-6306942;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897}.
CC       Nucleus, nucleoplasm {ECO:0000269|PubMed:15707897}. Nucleus
CC       speckle {ECO:0000269|PubMed:15707897}. Nucleus
CC       {ECO:0000269|PubMed:24127609}. Note=Cytoplasmic in darkness, but
CC       translocated to the nucleus upon illumination, when associated
CC       with PAPP5 into speckles. {ECO:0000269|PubMed:15707897}.
CC   -!- INDUCTION: Inactivation is proportional to temperature in the
CC       dark. {ECO:0000269|PubMed:27789797}.
CC   -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC       {ECO:0000269|PubMed:24982198}.
CC   -!- DISRUPTION PHENOTYPE: In oop1, defects in circadian timing with
CC       altered phase; early timing of the peak (acrophase) of multiple
CC       circadian rhythms such as leaf movement, CO(2) assimilation and
CC       light-induced gene expression. Strong photoperception defect in
CC       red light leading to long hypocotyls; this phenotype is increased
CC       when blue lights are combined to red lights. Increased sensitivity
CC       to SO(2). Elongated internodes before the transition to flowering
CC       when grown in short day conditions. {ECO:0000269|PubMed:12177480}.
CC   -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
DR   EMBL; X17342; CAA35222.1; -; mRNA.
DR   EMBL; L09262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY466496; AAR32737.1; -; Genomic_DNA.
DR   EMBL; AC005724; AAD08948.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06808.1; -; Genomic_DNA.
DR   PIR; B33473; FKMUB.
DR   RefSeq; NP_179469.1; NM_127435.4.
DR   PDB; 4OUR; X-ray; 3.40 A; A/B=90-624.
DR   PDBsum; 4OUR; -.
DR   SMR; P14713; -.
DR   BioGrid; 1751; 68.
DR   DIP; DIP-31742N; -.
DR   IntAct; P14713; 19.
DR   MINT; P14713; -.
DR   STRING; 3702.AT2G18790.1; -.
DR   iPTMnet; P14713; -.
DR   PaxDb; P14713; -.
DR   PRIDE; P14713; -.
DR   EnsemblPlants; AT2G18790.1; AT2G18790.1; AT2G18790.
DR   GeneID; 816394; -.
DR   Gramene; AT2G18790.1; AT2G18790.1; AT2G18790.
DR   KEGG; ath:AT2G18790; -.
DR   Araport; AT2G18790; -.
DR   TAIR; locus:2005515; AT2G18790.
DR   eggNOG; ENOG410IJ3B; Eukaryota.
DR   eggNOG; COG4251; LUCA.
DR   HOGENOM; HOG000272703; -.
DR   InParanoid; P14713; -.
DR   KO; K12121; -.
DR   OrthoDB; 59136at2759; -.
DR   PhylomeDB; P14713; -.
DR   PRO; PR:P14713; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P14713; baseline and differential.
DR   Genevisible; P14713; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031516; F:far-red light photoreceptor activity; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0031517; F:red light photoreceptor activity; IDA:TAIR.
DR   GO; GO:0009883; F:red or far-red light photoreceptor activity; IMP:TAIR.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0009687; P:abscisic acid metabolic process; IMP:TAIR.
DR   GO; GO:0006325; P:chromatin organization; IMP:TAIR.
DR   GO; GO:0010617; P:circadian regulation of calcium ion oscillation; IMP:TAIR.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR   GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR   GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR   GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR   GO; GO:0009638; P:phototropism; IMP:TAIR.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0017012; P:protein-phytochromobilin linkage; IDA:UniProtKB.
DR   GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
DR   GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR   GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IMP:TAIR.
DR   GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR   GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IDA:UniProtKB.
DR   GO; GO:0010202; P:response to low fluence red light stimulus; IMP:TAIR.
DR   GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR   GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
DR   GO; GO:0010148; P:transpiration; IMP:TAIR.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013654; PAS_2.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR013516; Phyto_chromo_BS.
DR   InterPro; IPR001294; Phytochrome.
DR   InterPro; IPR012129; Phytochrome_A-E.
DR   InterPro; IPR013515; Phytochrome_cen-reg.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08446; PAS_2; 1.
DR   Pfam; PF00360; PHY; 1.
DR   PIRSF; PIRSF000084; Phytochrome; 1.
DR   PRINTS; PR01033; PHYTOCHROME.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; SSF55785; 3.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS00245; PHYTOCHROME_1; 1.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P14713.
DR   SWISS-2DPAGE; P14713.
KW   3D-structure; Chromophore; Complete proteome; Cytoplasm; DNA-binding;
KW   Nucleus; Photoreceptor protein; Phytochrome signaling pathway;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Repressor;
KW   Sensory transduction; Transcription; Transcription regulation.
FT   CHAIN         1   1172       Phytochrome B.
FT                                /FTId=PRO_0000171963.
FT   DOMAIN      252    433       GAF. {ECO:0000305}.
FT   DOMAIN      652    723       PAS 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN      786    857       PAS 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN      934   1153       Histidine kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00107}.
FT   COMPBIAS      3     25       Gly/Ser-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00008}.
FT   BINDING     357    357       Phytochromobilin chromophore (covalent;
FT                                via 1 link). {ECO:0000244|PDB:4OUR}.
FT   VARIANT       9     12       Missing (in strain: cv. Kas-1).
FT                                {ECO:0000269|PubMed:15238539}.
FT   VARIANT      19     19       E -> K (in strain: cv. Kas-1).
FT                                {ECO:0000269|PubMed:15238539}.
FT   VARIANT     143    143       I -> L (in strain: cv. Kas-1).
FT                                {ECO:0000269|PubMed:15238539}.
FT   VARIANT     980    980       V -> I (in strain: cv. Kas-1).
FT                                {ECO:0000269|PubMed:15238539}.
FT   VARIANT    1072   1072       L -> V (in strain: cv. Kas-1).
FT                                {ECO:0000269|PubMed:15238539}.
FT   MUTAGEN     276    276       Y->H: In YHB; constitutively active and
FT                                stronger interaction with PTAC12/HMR in
FT                                the dark. Constitutive warm-temperature
FT                                response with the warm-temperature
FT                                transcriptome derepressed at low
FT                                temperatures.
FT                                {ECO:0000269|PubMed:22895253,
FT                                ECO:0000269|PubMed:27789797}.
FT   TURN         98    100       {ECO:0000244|PDB:4OUR}.
FT   HELIX       105    109       {ECO:0000244|PDB:4OUR}.
FT   STRAND      112    114       {ECO:0000244|PDB:4OUR}.
FT   STRAND      118    123       {ECO:0000244|PDB:4OUR}.
FT   TURN        125    127       {ECO:0000244|PDB:4OUR}.
FT   STRAND      129    134       {ECO:0000244|PDB:4OUR}.
FT   HELIX       137    140       {ECO:0000244|PDB:4OUR}.
FT   HELIX       163    165       {ECO:0000244|PDB:4OUR}.
FT   HELIX       169    180       {ECO:0000244|PDB:4OUR}.
FT   HELIX       184    187       {ECO:0000244|PDB:4OUR}.
FT   STRAND      189    197       {ECO:0000244|PDB:4OUR}.
FT   STRAND      200    207       {ECO:0000244|PDB:4OUR}.
FT   STRAND      209    218       {ECO:0000244|PDB:4OUR}.
FT   HELIX       224    246       {ECO:0000244|PDB:4OUR}.
FT   HELIX       253    268       {ECO:0000244|PDB:4OUR}.
FT   STRAND      271    278       {ECO:0000244|PDB:4OUR}.
FT   STRAND      284    289       {ECO:0000244|PDB:4OUR}.
FT   HELIX       305    307       {ECO:0000244|PDB:4OUR}.
FT   HELIX       310    318       {ECO:0000244|PDB:4OUR}.
FT   STRAND      321    325       {ECO:0000244|PDB:4OUR}.
FT   STRAND      327    329       {ECO:0000244|PDB:4OUR}.
FT   STRAND      332    336       {ECO:0000244|PDB:4OUR}.
FT   HELIX       356    365       {ECO:0000244|PDB:4OUR}.
FT   STRAND      368    378       {ECO:0000244|PDB:4OUR}.
FT   STRAND      394    406       {ECO:0000244|PDB:4OUR}.
FT   HELIX       412    448       {ECO:0000244|PDB:4OUR}.
FT   STRAND      473    475       {ECO:0000244|PDB:4OUR}.
FT   STRAND      477    480       {ECO:0000244|PDB:4OUR}.
FT   HELIX       496    506       {ECO:0000244|PDB:4OUR}.
FT   STRAND      516    519       {ECO:0000244|PDB:4OUR}.
FT   HELIX       529    531       {ECO:0000244|PDB:4OUR}.
FT   STRAND      538    541       {ECO:0000244|PDB:4OUR}.
FT   STRAND      551    554       {ECO:0000244|PDB:4OUR}.
FT   STRAND      561    566       {ECO:0000244|PDB:4OUR}.
FT   STRAND      587    590       {ECO:0000244|PDB:4OUR}.
FT   HELIX       601    616       {ECO:0000244|PDB:4OUR}.
SQ   SEQUENCE   1172 AA;  129331 MW;  7B5348CB1091B813 CRC64;
     MVSGVGGSGG GRGGGRGGEE EPSSSHTPNN RRGGEQAQSS GTKSLRPRSN TESMSKAIQQ
     YTVDARLHAV FEQSGESGKS FDYSQSLKTT TYGSSVPEQQ ITAYLSRIQR GGYIQPFGCM
     IAVDESSFRI IGYSENAREM LGIMPQSVPT LEKPEILAMG TDVRSLFTSS SSILLERAFV
     AREITLLNPV WIHSKNTGKP FYAILHRIDV GVVIDLEPAR TEDPALSIAG AVQSQKLAVR
     AISQLQALPG GDIKLLCDTV VESVRDLTGY DRVMVYKFHE DEHGEVVAES KRDDLEPYIG
     LHYPATDIPQ ASRFLFKQNR VRMIVDCNAT PVLVVQDDRL TQSMCLVGST LRAPHGCHSQ
     YMANMGSIAS LAMAVIINGN EDDGSNVASG RSSMRLWGLV VCHHTSSRCI PFPLRYACEF
     LMQAFGLQLN MELQLALQMS EKRVLRTQTL LCDMLLRDSP AGIVTQSPSI MDLVKCDGAA
     FLYHGKYYPL GVAPSEVQIK DVVEWLLANH ADSTGLSTDS LGDAGYPGAA ALGDAVCGMA
     VAYITKRDFL FWFRSHTAKE IKWGGAKHHP EDKDDGQRMH PRSSFQAFLE VVKSRSQPWE
     TAEMDAIHSL QLILRDSFKE SEAAMNSKVV DGVVQPCRDM AGEQGIDELG AVAREMVRLI
     ETATVPIFAV DAGGCINGWN AKIAELTGLS VEEAMGKSLV SDLIYKENEA TVNKLLSRAL
     RGDEEKNVEV KLKTFSPELQ GKAVFVVVNA CSSKDYLNNI VGVCFVGQDV TSQKIVMDKF
     INIQGDYKAI VHSPNPLIPP IFAADENTCC LEWNMAMEKL TGWSRSEVIG KMIVGEVFGS
     CCMLKGPDAL TKFMIVLHNA IGGQDTDKFP FPFFDRNGKF VQALLTANKR VSLEGKVIGA
     FCFLQIPSPE LQQALAVQRR QDTECFTKAK ELAYICQVIK NPLSGMRFAN SLLEATDLNE
     DQKQLLETSV SCEKQISRIV GDMDLESIED GSFVLKREEF FLGSVINAIV SQAMFLLRDR
     GLQLIRDIPE EIKSIEVFGD QIRIQQLLAE FLLSIIRYAP SQEWVEIHLS QLSKQMADGF
     AAIRTEFRMA CPGEGLPPEL VRDMFHSSRW TSPEGLGLSV CRKILKLMNG EVQYIRESER
     SYFLIILELP VPRKRPLSTA SGSGDMMLMM PY
//

If you have problems or comments...

PBIL Back to PBIL home page