PIF1_ARATH
ID PIF1_ARATH Reviewed; 478 AA.
AC Q8GZM7; Q0WQ83; Q3EBY0; Q9SL63;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Transcription factor PIF1;
DE AltName: Full=Basic helix-loop-helix protein 15;
DE Short=AtbHLH15;
DE Short=bHLH 15;
DE AltName: Full=Protein PHY-INTERACTING FACTOR 1;
DE AltName: Full=Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 5;
DE AltName: Full=Transcription factor EN 101;
DE AltName: Full=bHLH transcription factor bHLH015;
GN Name=PIF1; Synonyms=BHLH15, EN101, PIL5; OrderedLocusNames=At2g20180;
GN ORFNames=T2G17.2;
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), TISSUE SPECIFICITY, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH APRR1/TOC1.
RX PubMed=12826627; DOI=10.1093/pcp/pcg078;
RA Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S.,
RA Mizuno T.;
RT "A link between circadian-controlled bHLH factors and the APRR1/TOC1
RT quintet in Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:619-629(2003).
RN [3]
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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY RED AND
RP FAR-RED LIGHTS, AND INTERACTION WITH PHYA AND PHYB.
RX PubMed=15448264; DOI=10.1126/science.1099728;
RA Huq E., Al-Sady B., Hudson M., Kim C., Apel K., Quail P.H.;
RT "Phytochrome-interacting factor 1 is a critical bHLH regulator of
RT chlorophyll biosynthesis.";
RL Science 305:1937-1941(2004).
RN [10]
RP FUNCTION, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=16359394; DOI=10.1111/j.1365-313x.2005.02606.x;
RA Shen H., Moon J., Huq E.;
RT "PIF1 is regulated by light-mediated degradation through the ubiquitin-26S
RT proteasome pathway to optimize photomorphogenesis of seedlings in
RT Arabidopsis.";
RL Plant J. 44:1023-1035(2005).
RN [11]
RP FUNCTION.
RX PubMed=18487351; DOI=10.1105/tpc.108.058859;
RA Kim D.H., Yamaguchi S., Lim S., Oh E., Park J., Hanada A., Kamiya Y.,
RA Choi G.;
RT "SOMNUS, a CCCH-type zinc finger protein in Arabidopsis, negatively
RT regulates light-dependent seed germination downstream of PIL5.";
RL Plant Cell 20:1260-1277(2008).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18591656; DOI=10.1073/pnas.0803611105;
RA Moon J., Zhu L., Shen H., Huq E.;
RT "PIF1 directly and indirectly regulates chlorophyll biosynthesis to
RT optimize the greening process in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9433-9438(2008).
RN [13]
RP FUNCTION, MUTAGENESIS OF 1-MET--VAL-50; GLU-41; LEU-42; TRP-44; GLY-47;
RP 85-PHE--LEU-95; LEU-95; 118-ALA--GLY-160; SER-123; ASN-144; PHE-148;
RP GLY-153; PHE-155 AND GLY-160, INTERACTION WITH PHYA AND PHYB,
RP PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=18539749; DOI=10.1105/tpc.108.060020;
RA Shen H., Zhu L., Castillon A., Majee M., Downie B., Huq E.;
RT "Light-induced phosphorylation and degradation of the negative regulator
RT PHYTOCHROME-INTERACTING FACTOR1 from Arabidopsis depend upon its direct
RT physical interactions with photoactivated phytochromes.";
RL Plant Cell 20:1586-1602(2008).
RN [14]
RP INTERACTION WITH RGL2 AND RGA.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=20093430; DOI=10.1093/molbev/msq012;
RA Gallego-Bartolome J., Minguet E.G., Marin J.A., Prat S., Blazquez M.A.,
RA Alabadi D.;
RT "Transcriptional diversification and functional conservation between DELLA
RT proteins in Arabidopsis.";
RL Mol. Biol. Evol. 27:1247-1256(2010).
RN [15]
RP PHOSPHORYLATION AT THR-10; THR-197; SER-202; SER-464; SER-465; SER-466 AND
RP SER-469, UBIQUITINATION, AND MUTAGENESIS OF THR-10; THR-197; SER-202;
RP SER-464; SER-465; SER-466 AND SER-469.
RX PubMed=21330376; DOI=10.1074/jbc.m110.186882;
RA Bu Q., Zhu L., Dennis M.D., Yu L., Lu S.X., Person M.D., Tobin E.M.,
RA Browning K.S., Huq E.;
RT "Phosphorylation by CK2 enhances the rapid light-induced degradation of
RT phytochrome interacting factor 1 in Arabidopsis.";
RL J. Biol. Chem. 286:12066-12074(2011).
RN [16]
RP INTERACTION WITH FHY3.
RX PubMed=22634759; DOI=10.1105/tpc.112.097022;
RA Tang W., Wang W., Chen D., Ji Q., Jing Y., Wang H., Lin R.;
RT "Transposase-derived proteins FHY3/FAR1 interact with PHYTOCHROME-
RT INTERACTING FACTOR1 to regulate chlorophyll biosynthesis by modulating
RT HEMB1 during deetiolation in Arabidopsis.";
RL Plant Cell 24:1984-2000(2012).
CC -!- FUNCTION: Transcription activator. Regulates negatively chlorophyll
CC biosynthesis and seed germination in the dark, and lightinduced
CC degradation of PIF1 relieves this negative regulation to promote
CC photomorphogenesis. Binds to the G-box motif (5'-CACGTG-3') found in
CC many light-regulated promoters. Promotes the expression of SOM, and
CC thus modulates responses to abscisic acid (ABA) and gibberellic acid
CC (GA). {ECO:0000269|PubMed:15448264, ECO:0000269|PubMed:16359394,
CC ECO:0000269|PubMed:18487351, ECO:0000269|PubMed:18539749,
CC ECO:0000269|PubMed:18591656}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with the photoactivated
CC conformer (Pfr) of phytochromes A and B, PHYA and PHYB. Interacts also
CC with APRR1/TOC1. Binds to RGL2, RGA and FHY3 (via N-terminus).
CC {ECO:0000269|PubMed:12826627, ECO:0000269|PubMed:15448264,
CC ECO:0000269|PubMed:18539749, ECO:0000269|PubMed:20093430,
CC ECO:0000269|PubMed:22634759, ECO:0000305}.
CC -!- INTERACTION:
CC Q8GZM7; Q8S307: BZR1; NbExp=2; IntAct=EBI-630400, EBI-1803261;
CC Q8GZM7; Q9FE22: HFR1; NbExp=3; IntAct=EBI-630400, EBI-626001;
CC Q8GZM7; P14713: PHYB; NbExp=3; IntAct=EBI-630400, EBI-300727;
CC Q8GZM7; Q8GZM7: PIF1; NbExp=3; IntAct=EBI-630400, EBI-630400;
CC Q8GZM7; O80536: PIF3; NbExp=6; IntAct=EBI-630400, EBI-625701;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:15448264, ECO:0000269|PubMed:16359394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GZM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GZM7-2; Sequence=VSP_036107;
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, stems,
CC and flowers. {ECO:0000269|PubMed:12679534}.
CC -!- INDUCTION: Repressed by red (R) and far red (FR) light treatments in a
CC phyB- and phyA-dependent manner. {ECO:0000269|PubMed:15448264}.
CC -!- PTM: Phosphorylated at Thr-10, Thr-197, Ser-202, Ser-464, Ser-465, Ser-
CC 466 and Ser-469 by CK2 (PubMed:21330376). Phosphorylated and
CC ubiquitinated after an exposure to light (especially red and far-red),
CC in a phytochrome-dependent manner. Modified proteins undergo a
CC proteasome-dependent degradation. Its stability and degradation plays a
CC central role in photomorphogenesis of seedlings.
CC {ECO:0000269|PubMed:16359394, ECO:0000269|PubMed:18539749,
CC ECO:0000269|PubMed:21330376}.
CC -!- DISRUPTION PHENOTYPE: Plants overaccumulate free protochlorophyllide in
CC the darkness and exhibit photooxidative damage (bleaching) in
CC subsequent light, probably caused by the photosensitizing activity of
CC this tetrapyrrole intermediate. {ECO:0000269|PubMed:15448264,
CC ECO:0000269|PubMed:18591656}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF488560; AAN78308.1; -; mRNA.
DR EMBL; AB103113; BAC56979.1; -; Transcribed_RNA.
DR EMBL; AC006081; AAD24380.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06977.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06978.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06979.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61700.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61701.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61702.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61703.1; -; Genomic_DNA.
DR EMBL; AK228820; BAF00716.1; -; mRNA.
DR EMBL; BT029775; ABM06045.1; -; mRNA.
DR PIR; A84586; A84586.
DR RefSeq; NP_001189559.1; NM_001202630.2. [Q8GZM7-1]
DR RefSeq; NP_001318252.1; NM_001335663.1. [Q8GZM7-1]
DR RefSeq; NP_001323902.1; NM_001335664.1. [Q8GZM7-1]
DR RefSeq; NP_001323903.1; NM_001335665.1. [Q8GZM7-2]
DR RefSeq; NP_001323904.1; NM_001335666.1. [Q8GZM7-1]
DR RefSeq; NP_001323905.1; NM_001335667.1. [Q8GZM7-2]
DR RefSeq; NP_849996.1; NM_179665.3. [Q8GZM7-2]
DR AlphaFoldDB; Q8GZM7; -.
DR SMR; Q8GZM7; -.
DR BioGRID; 1892; 24.
DR DIP; DIP-61853N; -.
DR IntAct; Q8GZM7; 10.
DR STRING; 3702.AT2G20180.2; -.
DR iPTMnet; Q8GZM7; -.
DR PaxDb; Q8GZM7; -.
DR EnsemblPlants; AT2G20180.1; AT2G20180.1; AT2G20180. [Q8GZM7-2]
DR EnsemblPlants; AT2G20180.2; AT2G20180.2; AT2G20180. [Q8GZM7-1]
DR EnsemblPlants; AT2G20180.3; AT2G20180.3; AT2G20180. [Q8GZM7-1]
DR EnsemblPlants; AT2G20180.4; AT2G20180.4; AT2G20180. [Q8GZM7-1]
DR EnsemblPlants; AT2G20180.5; AT2G20180.5; AT2G20180. [Q8GZM7-2]
DR EnsemblPlants; AT2G20180.6; AT2G20180.6; AT2G20180. [Q8GZM7-1]
DR EnsemblPlants; AT2G20180.7; AT2G20180.7; AT2G20180. [Q8GZM7-2]
DR GeneID; 816538; -.
DR Gramene; AT2G20180.1; AT2G20180.1; AT2G20180. [Q8GZM7-2]
DR Gramene; AT2G20180.2; AT2G20180.2; AT2G20180. [Q8GZM7-1]
DR Gramene; AT2G20180.3; AT2G20180.3; AT2G20180. [Q8GZM7-1]
DR Gramene; AT2G20180.4; AT2G20180.4; AT2G20180. [Q8GZM7-1]
DR Gramene; AT2G20180.5; AT2G20180.5; AT2G20180. [Q8GZM7-2]
DR Gramene; AT2G20180.6; AT2G20180.6; AT2G20180. [Q8GZM7-1]
DR Gramene; AT2G20180.7; AT2G20180.7; AT2G20180. [Q8GZM7-2]
DR KEGG; ath:AT2G20180; -.
DR Araport; AT2G20180; -.
DR TAIR; locus:2061634; AT2G20180.
DR eggNOG; ENOG502QR6A; Eukaryota.
DR InParanoid; Q8GZM7; -.
DR OMA; MAEEDIM; -.
DR OrthoDB; 1384644at2759; -.
DR PhylomeDB; Q8GZM7; -.
DR PRO; PR:Q8GZM7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GZM7; baseline and differential.
DR Genevisible; Q8GZM7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0010313; F:phytochrome binding; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IMP:TAIR.
DR GO; GO:0006783; P:heme biosynthetic process; IMP:TAIR.
DR GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0010161; P:red light signaling pathway; IDA:TAIR.
DR GO; GO:0010099; P:regulation of photomorphogenesis; TAS:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; TAS:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR031066; bHLH_ALC-like_plant.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR45855; PTHR45855; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..478
FT /note="Transcription factor PIF1"
FT /id="PRO_0000358829"
FT DOMAIN 284..333
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 47
FT /note="Pfr PHYB binding"
FT SITE 95
FT /note="Pfr PHYA binding"
FT SITE 144
FT /note="Pfr PHYA binding"
FT MOD_RES 10
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 197
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 202
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 464
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 465
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 466
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT MOD_RES 469
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:21330376"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_036107"
FT MUTAGEN 1..50
FT /note="Missing: Normal interaction with PHYA (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 10
FT /note="T->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 41
FT /note="E->A: Loss of interaction with PHYB (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 42
FT /note="L->A: Loss of interaction with PHYB (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 44
FT /note="W->A: Reduced interaction with PHYB (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 47
FT /note="G->A: Loss of interaction with PHYB (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 85..95
FT /note="Missing: Reduced interaction with PHYA (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 95
FT /note="L->A: Reduced interaction with PHYA (Pfr form).
FT Reduced interaction with PHYA (Pfr form); when associated
FT with A-123; A-153; or A-160. Loss of interaction with PHYA
FT (Pfr form); when associated with A-144."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 118..160
FT /note="Missing: Reduced interaction with PHYA (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 123
FT /note="S->A: Reduced interaction with PHYA (Pfr form); when
FT associated with A-95."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 144
FT /note="N->A: Loss of interaction with PHYA (Pfr form); when
FT associated with A-95."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 148
FT /note="F->A: Normal interaction with PHYA (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 153
FT /note="G->A: Reduced interaction with PHYA (Pfr form); when
FT associated with A-95."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 155
FT /note="F->A: Normal interaction with PHYA (Pfr form)."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 160
FT /note="G->A: Reduced interaction with PHYA (Pfr form); when
FT associated with A-95."
FT /evidence="ECO:0000269|PubMed:18539749"
FT MUTAGEN 197
FT /note="T->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 202
FT /note="S->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 464
FT /note="S->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 465
FT /note="S->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 466
FT /note="S->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT MUTAGEN 469
FT /note="S->A: Loss of phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:21330376"
FT CONFLICT 102
FT /note="D -> G (in Ref. 5; BAF00716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52864 MW; 93572A0D4669D350 CRC64;
MHHFVPDFDT DDDYVNNHNS SLNHLPRKSI TTMGEDDDLM ELLWQNGQVV VQNQRLHTKK
PSSSPPKLLP SMDPQQQPSS DQNLFIQEDE MTSWLHYPLR DDDFCSDLLF SAAPTATATA
TVSQVTAARP PVSSTNESRP PVRNFMNFSR LRGDFNNGRG GESGPLLSKA VVRESTQVSP
SATPSAAASE SGLTRRTDGT DSSAVAGGGA YNRKGKAVAM TAPAIEITGT SSSVVSKSEI
EPEKTNVDDR KRKEREATTT DETESRSEET KQARVSTTST KRSRAAEVHN LSERKRRDRI
NERMKALQEL IPRCNKSDKA SMLDEAIEYM KSLQLQIQMM SMGCGMMPMM YPGMQQYMPH
MAMGMGMNQP IPPPSFMPFP NMLAAQRPLP TQTHMAGSGP QYPVHASDPS RVFVPNQQYD
PTSGQPQYPA GYTDPYQQFR GLHPTQPPQF QNQATSYPSS SRVSSSKESE DHGNHTTG
