PHYA_ARATH
ID PHYA_ARATH Reviewed; 1122 AA.
AC P14712; B3H6K9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Phytochrome A {ECO:0000303|PubMed:2606345};
DE AltName: Full=Protein ELONGATED HYPOCOTYL 8 {ECO:0000303|PubMed:8400877};
DE AltName: Full=Protein FAR RED ELONGATED 1;
DE AltName: Full=Protein FAR RED ELONGATED HYPOCOTYL 2;
GN Name=PHYA {ECO:0000303|PubMed:2606345};
GN Synonyms=FHY2, FRE1, HY8 {ECO:0000303|PubMed:8400877};
GN OrderedLocusNames=At1g09570 {ECO:0000312|Araport:AT1G09570};
GN ORFNames=F14J9.23 {ECO:0000312|EMBL:AAC33219.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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, evolution,
RT and differential expression of a plant regulatory photoreceptor family.";
RL Genes Dev. 3:1745-1757(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-727.
RC STRAIN=cv. RLD;
RX PubMed=8400877; DOI=10.2307/3869628;
RA Dehesh K., Franci C., Parks B.M., Seeley K.A., Short T.W., Tepperman J.M.,
RA Quail P.H.;
RT "Arabidopsis HY8 locus encodes phytochrome A.";
RL Plant Cell 5:1081-1088(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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., Park C.-M.;
RT "A phytochrome-associated protein phosphatase 2A modulates light signals in
RT flowering time control in Arabidopsis.";
RL Plant Cell 14:3043-3056(2002).
RN [7]
RP INTERACTION WITH NDPK2.
RX PubMed=15465053; DOI=10.1016/j.jmb.2004.08.054;
RA Im Y.J., Kim J.I., Shen Y., Na Y., Han Y.J., Kim S.H., Song P.S., Eom S.H.;
RT "Structural analysis of Arabidopsis thaliana nucleoside diphosphate kinase-
RT 2 for phytochrome-mediated light signaling.";
RL J. Mol. Biol. 343:659-670(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAPP5 AND NDPK2.
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., Kim S.-H.,
RA Fernandez A.P., Kim Y., Alonso J.M., Ecker J.R., Nagy F., Lim P.O.,
RA 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 transducer.";
RL Cell 120:395-406(2005).
RN [9]
RP FUNCTION.
RX PubMed=17566111; DOI=10.1073/pnas.0703855104;
RA Roesler J., Klein I., Zeidler M.;
RT "Arabidopsis fhl/fhy1 double mutant reveals a distinct cytoplasmic action
RT of phytochrome A.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10737-10742(2007).
RN [10]
RP INTERACTION WITH COP1; SPA1; FHY1 AND FHY3.
RX PubMed=18722184; DOI=10.1016/j.molcel.2008.08.003;
RA Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H.,
RA Deng X.W.;
RT "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct
RT phosphorylated forms of phytochrome A in balancing light signaling.";
RL Mol. Cell 31:607-613(2008).
RN [11]
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 of
RT hypocotyl growth orientation.";
RL Plant Physiol. 147:661-671(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH PHYA AND FHL.
RX PubMed=19208901; DOI=10.1105/tpc.108.061259;
RA Shen Y., Zhou Z., Feng S., Li J., Tan-Wilson A., Qu L.J., Wang H.,
RA Deng X.W.;
RT "Phytochrome A mediates rapid red light-induced phosphorylation of
RT Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a low fluence response.";
RL Plant Cell 21:494-506(2009).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP FHY1; HFR1 AND FHL.
RC STRAIN=cv. Columbia;
RX PubMed=19482971; DOI=10.1105/tpc.109.067215;
RA Yang S.W., Jang I.-C., Henriques R., Chua N.-H.;
RT "FAR-RED ELONGATED HYPOCOTYL1 and FHY1-LIKE associate with the Arabidopsis
RT transcription factors LAF1 and HFR1 to transmit phytochrome A signals for
RT inhibition of hypocotyl elongation.";
RL Plant Cell 21:1341-1359(2009).
RN [14]
RP INTERACTION WITH FHY1 AND FHL, AND MUTAGENESIS OF TYR-242 AND CYS-323.
RX PubMed=21884939; DOI=10.1016/j.cell.2011.07.023;
RA Rausenberger J., Tscheuschler A., Nordmeier W., Wuest F., Timmer J.,
RA Schaefer E., Fleck C., Hiltbrunner A.;
RT "Photoconversion and nuclear trafficking cycles determine phytochrome A's
RT response profile to far-red light.";
RL Cell 146:813-825(2011).
RN [15]
RP INTERACTION WITH PTAC12/HMR.
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 [16]
RP FUNCTION, MUTAGENESIS OF ALA-30, INTERACTION WITH FHY1 AND FHL, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21969386; DOI=10.1104/pp.111.186288;
RA Sokolova V., Bindics J., Kircher S., Adam E., Schaefer E., Nagy F.,
RA Viczian A.;
RT "Missense mutation in the amino terminus of phytochrome A disrupts the
RT nuclear import of the photoreceptor.";
RL Plant Physiol. 158:107-118(2012).
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are
CC 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 Pfr
CC induces an array of morphogenetic responses, whereas reconversion of
CC Pfr to Pr cancels the induction of those responses. Pfr controls the
CC expression of a number of nuclear genes including those encoding the
CC small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B
CC binding protein, protochlorophyllide reductase, rRNA, etc. It also
CC controls the expression of its own gene(s) in a negative feedback
CC fashion. Involved in the flowering time regulation. Can phosphorylate
CC FHY1 and, possibly, FHL, in red light conditions; this inactivates
CC their co-shuttling to the nucleus (PubMed:19208901). Regulates
CC phototropic responses both in the nucleus (e.g. hypocotyl elongation
CC and cotyledon opening under high-irradiance conditions and seed
CC germination under very-low-fluence conditions) and in the cytoplasm
CC (e.g. negative gravitropism in blue light and red-enhanced
CC phototropism) (PubMed:17566111). {ECO:0000269|PubMed:12468726,
CC ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:17566111,
CC ECO:0000269|PubMed:19208901, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:21969386}.
CC -!- SUBUNIT: Homodimer. Interacts with NDPK2 and PKS4. Stabilized by
CC interactions with PAPP5 and FYPP3 which are enhanced in the
CC phosphorylated Pfr form. Interacts with COP1/SPA1 complex
CC (PubMed:12468726, PubMed:15465053, PubMed:15707897, PubMed:18390804,
CC PubMed:18722184). Binds, via its photosensory domain, to PTAC12/HMR
CC when photoactivated; this interaction stimulates its localization to
CC photobodies (PubMed:22895253). Interacts with FHY1, FHL and FHY3,
CC especially upon far-red (FR) light illumination; when
CC underphosphorylated (PubMed:18722184, PubMed:19208901, PubMed:21884939,
CC PubMed:19482971). Forms PHYA/FHY1/HFR1 complex (PubMed:19482971).
CC {ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:15465053,
CC ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:18390804,
CC ECO:0000269|PubMed:18722184, ECO:0000269|PubMed:19208901,
CC ECO:0000269|PubMed:19482971, ECO:0000269|PubMed:21884939,
CC ECO:0000269|PubMed:22895253}.
CC -!- INTERACTION:
CC P14712; A8MR65: FHL; NbExp=3; IntAct=EBI-624446, EBI-1163353;
CC P14712; Q8S4Q6: FHY1; NbExp=4; IntAct=EBI-624446, EBI-1163379;
CC P14712; O64903: NDPK2; NbExp=3; IntAct=EBI-624446, EBI-349517;
CC P14712; P14712: PHYA; NbExp=3; IntAct=EBI-624446, EBI-624446;
CC P14712; O80536: PIF3; NbExp=8; IntAct=EBI-624446, EBI-625701;
CC P14712; Q8W2F3-2: PIF4; NbExp=2; IntAct=EBI-624446, EBI-625732;
CC P14712; Q9SWI1: PKS1; NbExp=3; IntAct=EBI-624446, EBI-626200;
CC P14712; Q80936: E1; Xeno; NbExp=2; IntAct=EBI-624446, EBI-1163369;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897,
CC ECO:0000269|PubMed:21969386}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}. Nucleus
CC speckle {ECO:0000269|PubMed:15707897}. Note=Cytoplasmic in darkness,
CC but translocated to the nucleus upon illumination, when associated with
CC PAPP5 into speckles. {ECO:0000269|PubMed:15707897,
CC ECO:0000269|PubMed:21969386}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P14712-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14712-2; Sequence=VSP_036311;
CC -!- PTM: Phosphorylated.
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Blind to far-red (FR). Impaired inhibition of
CC hypocotyl elongation and cotyledons expansion under continuous FR light
CC conditions. {ECO:0000269|PubMed:19482971}.
CC -!- MISCELLANEOUS: PHYA association with FHY1 and FHY3 protect
CC underphosphorylated PHYA from being recognized by the COP1/SPA complex.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; X17341; CAA35221.1; -; mRNA.
DR EMBL; L21154; AAA21351.1; -; Genomic_DNA.
DR EMBL; AC003970; AAC33219.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28462.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28463.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60635.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60636.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60637.1; -; Genomic_DNA.
DR EMBL; AY039520; AAK62577.1; -; mRNA.
DR PIR; A33473; FKMUA.
DR PIR; D86229; D86229.
DR RefSeq; NP_001117256.1; NM_001123784.1. [P14712-2]
DR RefSeq; NP_001322907.1; NM_001331843.1. [P14712-1]
DR RefSeq; NP_001322908.1; NM_001331842.1. [P14712-1]
DR RefSeq; NP_001322909.1; NM_001331841.1. [P14712-1]
DR RefSeq; NP_172428.1; NM_100828.4. [P14712-1]
DR AlphaFoldDB; P14712; -.
DR SMR; P14712; -.
DR BioGRID; 22724; 26.
DR DIP; DIP-33461N; -.
DR IntAct; P14712; 12.
DR MINT; P14712; -.
DR STRING; 3702.AT1G09570.1; -.
DR PaxDb; P14712; -.
DR PRIDE; P14712; -.
DR ProteomicsDB; 234753; -. [P14712-1]
DR EnsemblPlants; AT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
DR EnsemblPlants; AT1G09570.2; AT1G09570.2; AT1G09570. [P14712-2]
DR EnsemblPlants; AT1G09570.4; AT1G09570.4; AT1G09570. [P14712-1]
DR EnsemblPlants; AT1G09570.5; AT1G09570.5; AT1G09570. [P14712-1]
DR EnsemblPlants; AT1G09570.6; AT1G09570.6; AT1G09570. [P14712-1]
DR GeneID; 837483; -.
DR Gramene; AT1G09570.1; AT1G09570.1; AT1G09570. [P14712-1]
DR Gramene; AT1G09570.2; AT1G09570.2; AT1G09570. [P14712-2]
DR Gramene; AT1G09570.4; AT1G09570.4; AT1G09570. [P14712-1]
DR Gramene; AT1G09570.5; AT1G09570.5; AT1G09570. [P14712-1]
DR Gramene; AT1G09570.6; AT1G09570.6; AT1G09570. [P14712-1]
DR KEGG; ath:AT1G09570; -.
DR Araport; AT1G09570; -.
DR TAIR; locus:2012300; AT1G09570.
DR eggNOG; ENOG502QRSA; Eukaryota.
DR InParanoid; P14712; -.
DR PhylomeDB; P14712; -.
DR PRO; PR:P14712; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P14712; baseline and differential.
DR Genevisible; P14712; AT.
DR GO; GO:0005737; C:cytoplasm; 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:TAIR.
DR GO; GO:0031516; F:far-red light photoreceptor activity; IMP:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0009883; F:red or far-red light photoreceptor activity; TAS:TAIR.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0017148; P:negative regulation of translation; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0017006; P:protein-tetrapyrrole linkage; IEA:InterPro.
DR GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
DR GO; GO:0010201; P:response to continuous far red light stimulus by the high-irradiance response system; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
DR GO; GO:0010203; P:response to very low fluence red light stimulus; IMP:TAIR.
DR CDD; cd16932; HATPase_Phy-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.270; -; 1.
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; IPR044767; Phy_HATPase-like.
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 InterPro; IPR043150; Phytochrome_PHY.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 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;
KW Alternative splicing; Chromophore; Cytoplasm; Kinase; Nucleus;
KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW Repeat; Sensory transduction; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..1122
FT /note="Phytochrome A"
FT /id="PRO_0000171962"
FT DOMAIN 218..402
FT /note="GAF"
FT /evidence="ECO:0000255"
FT DOMAIN 618..688
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 695..747
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 748..822
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 902..1119
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036311"
FT MUTAGEN 30
FT /note="A->V: In phyA-5; reduced binding to FHY1 and FHL
FT leading to a reduced nuclear import under low fluences of
FT far-red light (FR) light. Hyposensitivity to continuous
FT low-intensity FR, and reduced very-low-fluence response and
FT high-irradiance response."
FT /evidence="ECO:0000269|PubMed:21969386"
FT MUTAGEN 242
FT /note="Y->H: Constitutively active in the Pfr form, leading
FT to a constitutively photomorphogenic (cop) phenotype and
FT reduced accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:21884939"
FT MUTAGEN 323
FT /note="C->A: Unable to bind the chromophore and cannot be
FT converted to Pfr, fails to accumulate in the nucleus and to
FT interact with FHY1."
FT /evidence="ECO:0000269|PubMed:21884939"
FT MUTAGEN 727
FT /note="G->E: In HY8-3; no regulatory activity."
FT /evidence="ECO:0000269|PubMed:8400877"
FT CONFLICT 835
FT /note="E -> D (in Ref. 1; CAA35221)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="E -> K (in Ref. 1; CAA35221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1122 AA; 124501 MW; D8B359713430744B CRC64;
MSGSRPTQSS EGSRRSRHSA RIIAQTTVDA KLHADFEESG SSFDYSTSVR VTGPVVENQP
PRSDKVTTTY LHHIQKGKLI QPFGCLLALD EKTFKVIAYS ENASELLTMA SHAVPSVGEH
PVLGIGTDIR SLFTAPSASA LQKALGFGDV SLLNPILVHC RTSAKPFYAI IHRVTGSIII
DFEPVKPYEV PMTAAGALQS YKLAAKAITR LQSLPSGSME RLCDTMVQEV FELTGYDRVM
AYKFHEDDHG EVVSEVTKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI VDCNAKHARV
LQDEKLSFDL TLCGSTLRAP HSCHLQYMAN MDSIASLVMA VVVNEEDGEG DAPDATTQPQ
KRKRLWGLVV CHNTTPRFVP FPLRYACEFL AQVFAIHVNK EVELDNQMVE KNILRTQTLL
CDMLMRDAPL GIVSQSPNIM DLVKCDGAAL LYKDKIWKLG TTPSEFHLQE IASWLCEYHM
DSTGLSTDSL HDAGFPRALS LGDSVCGMAA VRISSKDMIF WFRSHTAGEV RWGGAKHDPD
DRDDARRMHP RSSFKAFLEV VKTRSLPWKD YEMDAIHSLQ LILRNAFKDS ETTDVNTKVI
YSKLNDLKID GIQELEAVTS EMVRLIETAT VPILAVDSDG LVNGWNTKIA ELTGLSVDEA
IGKHFLTLVE DSSVEIVKRM LENALEGTEE QNVQFEIKTH LSRADAGPIS LVVNACASRD
LHENVVGVCF VAHDLTGQKT VMDKFTRIEG DYKAIIQNPN PLIPPIFGTD EFGWCTEWNP
AMSKLTGLKR EEVIDKMLLG EVFGTQKSCC RLKNQEAFVN LGIVLNNAVT SQDPEKVSFA
FFTRGGKYVE CLLCVSKKLD REGVVTGVFC FLQLASHELQ QALHVQRLAE RTAVKRLKAL
AYIKRQIRNP LSGIMFTRKM IEGTELGPEQ RRILQTSALC QKQLSKILDD SDLESIIEGC
LDLEMKEFTL NEVLTASTSQ VMMKSNGKSV RITNETGEEV MSDTLYGDSI RLQQVLADFM
LMAVNFTPSG GQLTVSASLR KDQLGRSVHL ANLEIRLTHT GAGIPEFLLN QMFGTEEDVS
EEGLSLMVSR KLVKLMNGDV QYLRQAGKSS FIITAELAAA NK
