ID PCH1_ARATH Reviewed; 778 AA. AC Q84V03; Q1PF61; Q94B23; Q9SIW6; DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 27-NOV-2024, entry version 110. DE RecName: Full=Protein PHOTOPERIODIC CONTROL OF HYPOCOTYL 1 {ECO:0000303|PubMed:29263319}; DE AltName: Full=F-box protein PCH1; GN Name=PCH1 {ECO:0000303|PubMed:29263319}; GN OrderedLocusNames=At2g16365 {ECO:0000312|Araport:AT2G16365}; GN ORFNames=F16F14.15 {ECO:0000312|EMBL:AAD22304.2}; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-778 (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=12481096; DOI=10.1104/pp.010207; RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.; RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2 RT of Arabidopsis."; RL Plant Physiol. 130:2118-2128(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-727 (ISOFORM 3). RC STRAIN=cv. Columbia; RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x; RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.; RT "Simultaneous high-throughput recombinational cloning of open reading RT frames in closed and open configurations."; RL Plant Biotechnol. J. 4:317-324(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-778 (ISOFORM 1). RC STRAIN=cv. Columbia; RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., RA Redman J.C., Wu H.C., Utterback T., Town C.D.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FAR-RED AND BLUE LIGHTS, RP INTERACTION WITH LIGHT-ACTIVATED PHYB, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=cv. Columbia; RX PubMed=29263319; DOI=10.1038/s41467-017-02311-8; RA Enderle B., Sheerin D.J., Paik I., Kathare P.K., Schwenk P., Klose C., RA Ulbrich M.H., Huq E., Hiltbrunner A.; RT "PCH1 and PCHL promote photomorphogenesis in plants by controlling RT phytochrome B dark reversion."; RL Nat. Commun. 8:2221-2221(2017). RN [8] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PIF1 AND COP1, AND RP UBIQUITINATION. RC STRAIN=cv. Columbia; RX PubMed=32061894; DOI=10.1016/j.molp.2020.02.003; RA Cheng M.-C., Enderle B., Kathare P.K., Islam R., Hiltbrunner A., Huq E.; RT "PCH1 and PCHL directly interact with PIF1, promote its degradation, and RT inhibit its transcriptional function during photomorphogenesis."; RL Mol. Plant 13:499-514(2020). CC -!- FUNCTION: Together with PCHL, regulates growth and development CC adaptation to the ambient environment by controlling negatively CC phytochrome B (phyB) dark reversion, a temperature-dependent thermal CC relaxation process during which phyB reverts from the active to the CC inactive state (PubMed:29263319, PubMed:32061894). Contributes to red CC (R) light-triggered photomorphogenesis (PubMed:29263319). Promotes CC various light responses such as seed germination, hypocotyl CC gravitropism and chlorophyll biosynthesis, via direct interaction with CC PIF1 and COP1 (PubMed:32061894). Prevents DNA-binding ability of PIF1 CC to negatively regulate the expressions of its target genes CC (PubMed:32061894). Facilitates the physical interaction between phyB CC and PIF1 and the subsequent light-induced degradation of PIF1 CC (PubMed:32061894). {ECO:0000269|PubMed:29263319, CC ECO:0000269|PubMed:32061894}. CC -!- SUBUNIT: Interacts with light-activated phyB (PubMed:29263319). Binds CC directly to PIF1 and COP1 (PubMed:32061894). CC {ECO:0000269|PubMed:29263319, ECO:0000269|PubMed:32061894}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29263319}. CC Note=Observed in subnuclear light-induced structures called CC photobodies. {ECO:0000269|PubMed:29263319}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q84V03-1; Sequence=Displayed; CC Name=2; CC IsoId=Q84V03-2; Sequence=VSP_039574, VSP_039575; CC Name=3; CC IsoId=Q84V03-3; Sequence=VSP_039573, VSP_039576; CC -!- TISSUE SPECIFICITY: Mainly expressed in cotyledons, hypocotyls, leaves CC and roots. {ECO:0000269|PubMed:29263319}. CC -!- INDUCTION: Induced by far-red (FR) and blue (B) lights, as well as CC transiently following transition from darkness to red light (R) in a CC phyB-independent manner; responses to red and far-red lights depend on CC phyA, and responses to blue light rely on both phyA and cryptochromes CC (PubMed:29263319). In the dark, binds to COP1 and undergo degradation CC through the 26S proteasome pathway (PubMed:32061894). CC {ECO:0000269|PubMed:29263319, ECO:0000269|PubMed:32061894}. CC -!- PTM: Ubiquitinated by COP1 in darkness; this leads to proteasomal CC degradation. {ECO:0000269|PubMed:32061894}. CC -!- DISRUPTION PHENOTYPE: Reduced seed germination in red (R) light; this CC phenotype is reversed in plants lacking PIF1 (PubMed:32061894). Reduced CC PIF1 degradation in response to red light pulse (PubMed:32061894). CC Hypersensitivity to gravity stimulus and increased greening CC (PubMed:32061894). Increased hypocotyl growth independently of far-red CC (FR) pulse at light-off, as the result of a rapid loss of active phyB CC due to increased dark reversion (PubMed:29263319). Suppression of cop1 CC phenotype in darkness (PubMed:32061894). Highly unstable phyB- CC containing photobodies in plants lacking both PCH1 and PCHL CC (PubMed:29263319). {ECO:0000269|PubMed:29263319, CC ECO:0000269|PubMed:32061894}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO73431.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AC007047; AAD22304.2; -; Genomic_DNA. DR EMBL; CP002685; AEC06484.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06485.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06486.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06487.1; -; Genomic_DNA. DR EMBL; CP002685; ANM61300.1; -; Genomic_DNA. DR EMBL; CP002685; ANM61301.1; -; Genomic_DNA. DR EMBL; AY042900; AAK68840.1; -; mRNA. DR EMBL; BT006598; AAP31942.1; -; mRNA. DR EMBL; AY227650; AAO73431.1; ALT_INIT; mRNA. DR EMBL; DQ446505; ABE65815.1; -; mRNA. DR EMBL; AY773845; AAV63874.1; -; mRNA. DR PIR; C84539; C84539. DR RefSeq; NP_001118328.1; NM_001124856.2. [Q84V03-1] DR RefSeq; NP_001118329.1; NM_001124857.2. [Q84V03-3] DR RefSeq; NP_001323527.1; NM_001335470.1. [Q84V03-2] DR RefSeq; NP_001323528.1; NM_001335471.1. [Q84V03-2] DR RefSeq; NP_671856.2; NM_147321.2. [Q84V03-1] DR RefSeq; NP_973716.1; NM_201987.2. [Q84V03-2] DR AlphaFoldDB; Q84V03; -. DR BioGRID; 1491; 18. DR STRING; 3702.Q84V03; -. DR iPTMnet; Q84V03; -. DR PaxDb; 3702-AT2G16365.1; -. DR ProteomicsDB; 230884; -. [Q84V03-1] DR EnsemblPlants; AT2G16365.1; AT2G16365.1; AT2G16365. [Q84V03-1] DR EnsemblPlants; AT2G16365.2; AT2G16365.2; AT2G16365. [Q84V03-2] DR EnsemblPlants; AT2G16365.3; AT2G16365.3; AT2G16365. [Q84V03-1] DR EnsemblPlants; AT2G16365.4; AT2G16365.4; AT2G16365. [Q84V03-3] DR EnsemblPlants; AT2G16365.5; AT2G16365.5; AT2G16365. [Q84V03-2] DR EnsemblPlants; AT2G16365.6; AT2G16365.6; AT2G16365. [Q84V03-2] DR GeneID; 816133; -. DR Gramene; AT2G16365.1; AT2G16365.1; AT2G16365. [Q84V03-1] DR Gramene; AT2G16365.2; AT2G16365.2; AT2G16365. [Q84V03-2] DR Gramene; AT2G16365.3; AT2G16365.3; AT2G16365. [Q84V03-1] DR Gramene; AT2G16365.4; AT2G16365.4; AT2G16365. [Q84V03-3] DR Gramene; AT2G16365.5; AT2G16365.5; AT2G16365. [Q84V03-2] DR Gramene; AT2G16365.6; AT2G16365.6; AT2G16365. [Q84V03-2] DR KEGG; ath:AT2G16365; -. DR Araport; AT2G16365; -. DR TAIR; AT2G16365; PCH1. DR eggNOG; ENOG502QVXQ; Eukaryota. DR HOGENOM; CLU_381014_0_0_1; -. DR InParanoid; Q84V03; -. DR OMA; HESAWLG; -. DR OrthoDB; 1221715at2759; -. DR PRO; PR:Q84V03; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q84V03; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR. DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:TAIR. DR GO; GO:0010099; P:regulation of photomorphogenesis; IGI:TAIR. DR CDD; cd09917; F-box_SF; 1. DR InterPro; IPR005174; DUF295. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR037476; PCH1. DR PANTHER; PTHR36062:SF7; BNAA07G03600D PROTEIN; 1. DR PANTHER; PTHR36062; OS01G0687300 PROTEIN; 1. DR Pfam; PF03478; DUF295; 1. DR Pfam; PF00646; F-box; 1. DR SMART; SM00256; FBOX; 1. DR SUPFAM; SSF81383; F-box domain; 1. PE 1: Evidence at protein level; KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation. FT CHAIN 1..778 FT /note="Protein PHOTOPERIODIC CONTROL OF HYPOCOTYL 1" FT /id="PRO_0000396064" FT DOMAIN 470..505 FT /note="F-box" FT REGION 74..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 186..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 74..91 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..242 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 455..458 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17147637" FT /id="VSP_039573" FT VAR_SEQ 455 FT /note="S -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14593172" FT /id="VSP_039574" FT VAR_SEQ 456..778 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14593172" FT /id="VSP_039575" FT VAR_SEQ 515..561 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17147637" FT /id="VSP_039576" SQ SEQUENCE 778 AA; 88623 MW; DC34D0EDACE92DF5 CRC64; MSEHVMVLGK GNKGISKNSS VNPYESAWLG RWTQSGSEVK FHDGETNCSK QLIRPEDENH GVEVLPFPMF KVSQKRETTT TTTTKPSFHE DVGSSSRAMV NRMPWMYPQG ENFSSSNRLD FPIQEKTTQN LLELIRPVRI YATVDSVNLP KEDSHQLLKG STVSMKLKGK IFGGYLDLFP NQDHSHNRGG VRLQSLESSK DTQEDGPRKN ESSAETNTLE MDRLQTIHLS GSISSSSTKG KGIKGYSAIP RTEIPDMNEE PPLVPDRENS VDGHQGETSN SATQSMNVEH FLSRDCKRVR LEPEVEASSR WVKRLKTSPS DSSETKSMMK MKEASLGEKE NNNLFLEILK SGINNLQPRN QEPVVSQSND LRQGGDDITL LHPWIQRWCK KKTTSTDQPT GQEASFEPES HKEFEKKQYP SIAAMALMGK ALSGLNPYGL RKTNSLMVWN ARDLSFTYRS LRWNLTMADW PLLPNDLLEL IMGHLETSFE IFLFRSVCSS WRSVVPPLDH SRCLGIKTHD ISFNVGFSFN GRPTNEYCTL KKIPIYLVKF WTPFGDDYLL AEMRERNDGE PKLLLSPLSS NGIKYGMGIN KVLFNSLTSP IIPFGQYYEI TYIEKRPSEY RFGFPYKLEW VEITERVEFL KLDSEDSRDF AVLFAGRMCN LVMYRSRNMS WTQVVEHPEK YAYQDLVAFK GKFYAVDSSG RGRVFVVELS FEVTEIPSVG GSQQSSKESL VQSGEELLLV QRFTPVGRRY DEYIYIHGSE CLDLMKKEER ESGFKLMT //