PHYC_ARATH
ID PHYC_ARATH Reviewed; 1111 AA.
AC P14714;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Phytochrome C;
GN Name=PHYC; OrderedLocusNames=At5g35840; ORFNames=MIK22.15;
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].
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].
RX PubMed=7991704; DOI=10.1104/pp.106.2.813;
RA Cowl J.S., Hartley N., Xie D., Whitelam G.C., Murphy G., Harberd N.P.;
RT "The PHYC gene of Arabidopsis. Absence of the third intron found in PHYA
RT and PHYB.";
RL Plant Physiol. 106:813-814(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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).
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 morphogenic responses, whereas reconversion of Pfr
CC 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.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P14714; P14713: PHYB; NbExp=5; IntAct=EBI-624366, EBI-300727;
CC P14714; P42497: PHYD; NbExp=2; IntAct=EBI-624366, EBI-624382;
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; X17343; CAA35223.1; -; mRNA.
DR EMBL; Z32538; CAA83549.1; -; Genomic_DNA.
DR EMBL; AB005236; BAB09925.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94021.1; -; Genomic_DNA.
DR PIR; C33473; FKMUC.
DR RefSeq; NP_198433.1; NM_122975.3.
DR AlphaFoldDB; P14714; -.
DR SMR; P14714; -.
DR BioGRID; 18823; 7.
DR IntAct; P14714; 3.
DR STRING; 3702.AT5G35840.1; -.
DR PaxDb; P14714; -.
DR PRIDE; P14714; -.
DR ProteomicsDB; 234752; -.
DR EnsemblPlants; AT5G35840.1; AT5G35840.1; AT5G35840.
DR GeneID; 833570; -.
DR Gramene; AT5G35840.1; AT5G35840.1; AT5G35840.
DR KEGG; ath:AT5G35840; -.
DR Araport; AT5G35840; -.
DR TAIR; locus:2165199; AT5G35840.
DR eggNOG; ENOG502QT1B; Eukaryota.
DR HOGENOM; CLU_010418_0_0_1; -.
DR InParanoid; P14714; -.
DR OMA; NFGCRVK; -.
DR OrthoDB; 77253at2759; -.
DR PhylomeDB; P14714; -.
DR PRO; PR:P14714; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P14714; baseline and differential.
DR Genevisible; P14714; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0017006; P:protein-tetrapyrrole linkage; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009637; P:response to blue light; IEA:UniProt.
DR CDD; cd16932; HATPase_Phy-like; 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; IPR001610; PAC.
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; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
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 Chromophore; Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Transcription; Transcription regulation.
FT CHAIN 1..1111
FT /note="Phytochrome C"
FT /id="PRO_0000171964"
FT DOMAIN 213..393
FT /note="GAF"
FT DOMAIN 604..674
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 737..808
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 889..1111
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 318
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="C -> Y (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="E -> Q (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> S (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="N -> K (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="S -> T (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="T -> K (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="K -> Q (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="I -> M (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="E -> K (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017..1018
FT /note="LR -> WK (in Ref. 2; CAA83549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1111 AA; 123722 MW; 58FE4645501135CA CRC64;
MSSNTSRSCS TRSRQNSRVS SQVLVDAKLH GNFEESERLF DYSASINLNM PSSSCEIPSS
AVSTYLQKIQ RGMLIQPFGC LIVVDEKNLK VIAFSENTQE MLGLIPHTVP SMEQREALTI
GTDVKSLFLS PGCSALEKAV DFGEISILNP ITLHCRSSSK PFYAILHRIE EGLVIDLEPV
SPDEVPVTAA GALRSYKLAA KSISRLQALP SGNMLLLCDA LVKEVSELTG YDRVMVYKFH
EDGHGEVIAE CCREDMEPYL GLHYSATDIP QASRFLFMRN KVRMICDCSA VPVKVVQDKS
LSQPISLSGS TLRAPHGCHA QYMSNMGSVA SLVMSVTING SDSDEMNRDL QTGRHLWGLV
VCHHASPRFV PFPLRYACEF LTQVFGVQIN KEAESAVLLK EKRILQTQSV LCDMLFRNAP
IGIVTQSPNI MDLVKCDGAA LYYRDNLWSL GVTPTETQIR DLIDWVLKSH GGNTGFTTES
LMESGYPDAS VLGESICGMA AVYISEKDFL FWFRSSTAKQ IKWGGARHDP NDRDGKRMHP
RSSFKAFMEI VRWKSVPWDD MEMDAINSLQ LIIKGSLQEE HSKTVVDVPL VDNRVQKVDE
LCVIVNEMVR LIDTAAVPIF AVDASGVING WNSKAAEVTG LAVEQAIGKP VSDLVEDDSV
ETVKNMLALA LEGSEERGAE IRIRAFGPKR KSSPVELVVN TCCSRDMTNN VLGVCFIGQD
VTGQKTLTEN YSRVKGDYAR IMWSPSTLIP PIFITNENGV CSEWNNAMQK LSGIKREEVV
NKILLGEVFT TDDYGCCLKD HDTLTKLRIG FNAVISGQKN IEKLLFGFYH RDGSFIEALL
SANKRTDIEG KVTGVLCFLQ VPSPELQYAL QVQQISEHAI ACALNKLAYL RHEVKDPEKA
ISFLQDLLHS SGLSEDQKRL LRTSVLCREQ LAKVISDSDI EGIEEGYVEL DCSEFGLQES
LEAVVKQVME LSIERKVQIS CDYPQEVSSM RLYGDNLRLQ QILSETLLSS IRFTPALRGL
CVSFKVIARI EAIGKRMKRV ELEFRIIHPA PGLPEDLVRE MFQPLRKGTS REGLGLHITQ
KLVKLMERGT LRYLRESEMS AFVILTEFPL I
