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};
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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
//