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 29-MAY-2013, entry version 123.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=2606345;
RA Sharrock R.A., Quail P.H.;
RT "Novel phytochrome sequences in Arabidopsis thaliana: structure,
RT evolution, and differential expression of a plant regulatory
RT 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
RT PHYA 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
RT P1 clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that
CC are 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
CC Pfr induces an array of morphogenic responses, whereas
CC reconversion of Pfr to Pr cancels the induction of those
CC responses. Pfr controls the expression of a number of nuclear
CC genes including those encoding the small subunit of ribulose-
CC bisphosphate carboxylase, chlorophyll A/B binding protein,
CC protochlorophyllide reductase, rRNA, etc. It also controls the
CC expression of its own gene(s) in a negative feedback fashion.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P14713:PHYB; NbExp=5; IntAct=EBI-624366, EBI-300727;
CC P42497:PHYD; NbExp=2; IntAct=EBI-624366, EBI-624382;
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore
CC (By similarity).
CC -!- SIMILARITY: Belongs to the phytochrome family.
CC -!- SIMILARITY: Contains 1 GAF domain.
CC -!- SIMILARITY: Contains 1 histidine kinase domain.
CC -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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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 IPI; IPI00516887; -.
DR PIR; C33473; FKMUC.
DR RefSeq; NP_198433.1; NM_122975.2.
DR UniGene; At.97; -.
DR ProteinModelPortal; P14714; -.
DR SMR; P14714; 69-726.
DR IntAct; P14714; 3.
DR PaxDb; P14714; -.
DR PRIDE; P14714; -.
DR EnsemblPlants; AT5G35840.1; AT5G35840.1; AT5G35840.
DR GeneID; 833570; -.
DR KEGG; ath:AT5G35840; -.
DR TAIR; At5g35840; -.
DR eggNOG; COG0642; -.
DR HOGENOM; HOG000272703; -.
DR InParanoid; P14714; -.
DR OMA; LYGDNLR; -.
DR PhylomeDB; P14714; -.
DR ProtClustDB; CLSN2679275; -.
DR ArrayExpress; P14714; -.
DR Genevestigator; P14714; -.
DR GermOnline; AT5G35840; Arabidopsis thaliana.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:GOC.
DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
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-dependent; IEA:UniProtKB-KW.
DR GO; GO:0023014; P:signal transduction by phosphorylation; IEA:GOC.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR003594; HATPase_ATP-bd.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR013767; PAS_fold.
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; IPR003661; Sig_transdc_His_kin_sub1_dim/P.
DR InterPro; IPR005467; Sig_transdc_His_kinase_core.
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; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
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; Complete proteome; Photoreceptor protein; Receptor;
KW Reference proteome; Repeat; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1 1111 Phytochrome C.
FT /FTId=PRO_0000171964.
FT DOMAIN 213 393 GAF.
FT DOMAIN 604 674 PAS 1.
FT DOMAIN 737 808 PAS 2.
FT DOMAIN 889 1111 Histidine kinase.
FT BINDING 318 318 Phytochromobilin chromophore (covalent;
FT via 1 link) (By similarity).
FT CONFLICT 9 9 C -> Y (in Ref. 2; CAA83549).
FT CONFLICT 137 137 E -> Q (in Ref. 2; CAA83549).
FT CONFLICT 230 230 G -> S (in Ref. 2; CAA83549).
FT CONFLICT 446 446 N -> K (in Ref. 2; CAA83549).
FT CONFLICT 505 505 S -> T (in Ref. 2; CAA83549).
FT CONFLICT 726 726 T -> K (in Ref. 2; CAA83549).
FT CONFLICT 735 735 K -> Q (in Ref. 2; CAA83549).
FT CONFLICT 754 754 I -> M (in Ref. 2; CAA83549).
FT CONFLICT 822 822 E -> K (in Ref. 2; CAA83549).
FT CONFLICT 1017 1018 LR -> WK (in Ref. 2; CAA83549).
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
//
