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UniProtKB/Swiss-Prot entry Q84LH8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIF5_ARATH
Primary accession number Q84LH8
Secondary accession numbers Q8RXG4 Q8S3D7 Q9LYT0
Integrated into Swiss-Prot on April 8, 2008
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 29)
Name and origin of the protein
Protein name Phytochrome-interacting factor 5
Synonyms Basic helix-loop-helix protein 65
bHLH 65
AtbHLH065
Phytochrome interacting factor-like 6
Gene name
Name: PIF5
Synonyms: PIL6
OrderedLocusNames: At3g59060
ORFNames: F17J16.110
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), GENE FAMILY, AND NOMENCLATURE.
DOI=10.1093/molbev/msg088; PubMed=12679534 [NCBI, ExPASy, EBI, Israel, Japan]
Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
"The basic helix-loop-helix transcription factor family in plants: a genome-wide study of protein structure and functional diversity.";
Mol. Biol. Evol. 20:735-747(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, INDUCTION, AND INTERACTION WITH TOC1/APRR1.
STRAIN=cv. Columbia;
DOI=10.1093/pcp/pcg078; PubMed=12826627 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S., Mizuno T.;
"A Link between circadian-controlled bHLH factors and the APRR1/TOC1 quintet in Arabidopsis thaliana.";
Plant Cell Physiol. 44:619-629(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
FUNCTION, MUTAGENESIS OF GLU-31; LEU-32; GLY-37 AND GLN-38, AND INTERACTION WITH PHYB.
DOI=10.1105/tpc.104.025643; PubMed=15486100 [NCBI, ExPASy, EBI, Israel, Japan]
Khanna R., Huq E., Kikis E.A., Al-Sady B., Lanzatella C., Quail P.H.;
"A novel molecular recognition motif necessary for targeting photoactivated phytochrome signaling to specific basic helix-loop-helix transcription factors.";
Plant Cell 16:3033-3044(2004).
[6]
FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH TOC1/APRR1 AND PIF3.
DOI=10.1093/pcp/pch124; PubMed=15356333 [NCBI, ExPASy, EBI, Israel, Japan]
Fujimori T., Yamashino T., Kato T., Mizuno T.;
"Circadian-controlled basic/helix-loop-helix factor, PIL6, implicated in light-signal transduction in Arabidopsis thaliana.";
Plant Cell Physiol. 45:1078-1086(2004).
[7]
FUNCTION, AND INDUCTION.
DOI=10.1038/nature05946; PubMed=17589502 [NCBI, ExPASy, EBI, Israel, Japan]
Nozue K., Covington M.F., Duek P.D., Lorrain S., Fankhauser C., Harmer S.L., Maloof J.N.;
"Rhythmic growth explained by coincidence between internal and external cues.";
Nature 448:358-361(2007).
[8]
FUNCTION, AND MUTAGENESIS OF GLY-37.
DOI=10.1105/tpc.107.051508; PubMed=18065691 [NCBI, ExPASy, EBI, Israel, Japan]
Khanna R., Shen Y., Marion C.M., Tsuchisaka A., Theologis A., Schaefer E., Quail P.H.;
"The basic helix-loop-helix transcription factor PIF5 acts on ethylene biosynthesis and phytochrome signaling by distinct mechanisms.";
Plant Cell 19:3915-3929(2007).
[9]
PHOSPHORYLATION.
DOI=10.1104/pp.107.105601; PubMed=17827270 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Y., Khanna R., Carle C.M., Quail P.H.;
"Phytochrome induces rapid PIF5 phosphorylation and degradation in response to red-light activation.";
Plant Physiol. 145:1043-1051(2007).
[10]
FUNCTION, PHOSPHORYLATION, AND INDUCTION.
DOI=10.1111/j.1365-313X.2007.03341.x; PubMed=18047474 [NCBI, ExPASy, EBI, Israel, Japan]
Lorrain S., Allen T., Duek P.D., Whitelam G.C., Fankhauser C.;
"Phytochrome-mediated inhibition of shade avoidance involves degradation of growth-promoting bHLH transcription factors.";
Plant J. 53:312-323(2008).
Comments
  • FUNCTION: Transcription factor acting negatively in the phytochrome B signaling pathway to promote the shade-avoidance response. Regulates PHYB abundance at the post-transcriptional level, possibly via the ubiquitin-proteasome pathway. Promotes ethylene activity in the dark. May regulate the expression of a subset of genes by binding to the G-box motif. Might be involved in the integration of light-signals to control both circadian and photomorphogenic processes.
  • SUBUNIT: Interacts specifically with the Pfr form of phytochrome B and with TOC1/APRR1. May form a heterodimer with PIF3.
  • INTERACTION:
    P14713:PHYB; NbExp=1; IntAct=EBI-631622, EBI-300727;
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ84LH8-1
    Note: No experimental confirmation available.
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ84LH8-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_032846.
    Name3
    Isoform IDQ84LH8-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_032844, VSP_032845.
  • DEVELOPMENTAL STAGE: Circadian-controlled expression.
  • INDUCTION: Up-regulated by white light. Rapid degradation after red light exposure (at protein level). Accumulates to high levels in the dark, is selectively degraded in response to red light and remains at high levels under shade-mimicking conditions.
  • DOMAIN: The active phytochrome binding (APB) motif (26-39) is involved in interaction with PHYB and is required for proteasome-mediated degradation.
  • PTM: Phosphorylated. Additional phosphorylations induced within 60 seconds following phytochrome B photoactivation.
  • SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF488598; AAM10954.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB103112; BAC56978.1; -; pre-RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163527; CAB86934.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081271; AAL91160.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000049; AAN15368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T47788; T47788.
RefSeq NP_001030889.1; -.
NP_001030890.1; -.
NP_191465.3; -.
UniGene At.43437
3D structure databases
HSSP P22415; 1AN4. [HSSP ENTRY / PDB]
ModBase Q84LH8.
Protein-protein interaction databases
IntAct Q84LH8; -.
Organism-specific databases
TAIR At3g59060; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001092; HLH_basic.
IPR011598; HLH_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:4.10.280.10; HLH_DNA_bd; 1.
Pfam PF00010; HLH; 1.
Pfam graphical view of domain structure.
SMART SM00353; HLH; 1.
SMART graphical view of domain structure.
PROSITE PS50888; HLH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q84LH8.
Genome annotation databases
GeneID 825075; -.
GenomeReviews BA000014_GR; AT3G59060.
KEGG ath:AT3G59060; -.
NMPDR fig|3702.1.peg.17252; -.
Other
ProtoNet Q84LH8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Phytochrome signaling pathway; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   444  444     Phytochrome-interacting factor 5. PRO_0000328935
DOMAIN   278   306  29     Helix-loop-helix motif. 
DNA_BIND   253   277  25     Basic motif. 
REGION   26    39  14     Involved in interaction with phyB. 
COMPBIAS   266   271  6     Poly-Arg. 
COMPBIAS   319   326  8     Poly-Ala. 
COMPBIAS   342   412  71     Gln-rich. 
VAR_SEQ   289   300        TDKASILDEAID -> IKLRYWMKQLIT (in isoform 3). VSP_032844
VAR_SEQ   301   444        Missing (in isoform 3). VSP_032845
VAR_SEQ   405   406        Missing (in isoform 2). VSP_032846
MUTAGEN   31    31        E->A: Loss of binding to PHYB. 
MUTAGEN   32    32        L->A: Loss of binding to PHYB. 
MUTAGEN   37    37        G->A: Loss of binding to PHYB. 
MUTAGEN   38    38        Q->A: Loss of binding to PHYB. 
CONFLICT   126   126        T -> M (in Ref. 1; AAM10954). 
CONFLICT   174   174        S -> N (in Ref. 4; AAN15368/AAL91160). 
CONFLICT   371   371        Q -> L (in Ref. 1; AAM10954). 
Sequence information
Length: 444 AA [This is the length of the unprocessed precursor] Molecular weight: 49302 Da [This is the MW of the unprocessed precursor] CRC64: 593D72C1F2ED86C7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEQVFADWNF EDNFHMSTNK RSIRPEDELV ELLWRDGQVV LQSQARREPS VQVQTHKQET 

        70         80         90        100        110        120 
LRKPNNIFLD NQETVQKPNY AALDDQETVS WIQYPPDDVI DPFESEFSSH FFSSIDHLGG 

       130        140        150        160        170        180 
PEKPRTIEET VKHEAQAMAP PKFRSSVITV GPSHCGSNQS TNIHQATTLP VSMSDRSKNV 

       190        200        210        220        230        240 
EERLDTSSGG SSGCSYGRNN KETVSGTSVT IDRKRKHVMD ADQESVSQSD IGLTSTDDQT 

       250        260        270        280        290        300 
MGNKSSQRSG STRRSRAAEV HNLSERRRRD RINERMKALQ ELIPHCSRTD KASILDEAID 

       310        320        330        340        350        360 
YLKSLQMQLQ VMWMGSGMAA AAAAAASPMM FPGVQSSPYI NQMAMQSQMQ LSQFPVMNRS 

       370        380        390        400        410        420 
APQNHPGLVC QNPVQLQLQA QNQILSEQLA RYMGGIPQMP PAGNQMQTVQ QQPADMLGFG 

       430        440 
SPAGPQSQLS APATTDSLHM GKIG 

Q84LH8 in FASTA format

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View entry in raw text format (no links)
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