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Database: UniProt
Entry: P14714
LinkDB: P14714
Original site: P14714 
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   01-OCT-2014, entry version 134.
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; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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,
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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 GAF domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00107}.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00140}.
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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_122975.2.
DR   UniGene; At.97; -.
DR   ProteinModelPortal; P14714; -.
DR   SMR; P14714; 69-726.
DR   BioGrid; 18823; 2.
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; NACCSRD; -.
DR   PhylomeDB; P14714; -.
DR   BioCyc; ARA:GQT-1838-MONOMER; -.
DR   Genevestigator; P14714; -.
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:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0009584; P:detection of visible light; IEA:InterPro.
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-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003661; EnvZ-like_dim/P.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF_dom_like.
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; 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; SSF55781; SSF55781; 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; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN      737    808       PAS 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN      889   1111       Histidine kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00107}.
FT   BINDING     318    318       Phytochromobilin chromophore (covalent;
FT                                via 1 link). {ECO:0000250}.
FT   CONFLICT      9      9       C -> Y (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    137    137       E -> Q (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       G -> S (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    446    446       N -> K (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    505    505       S -> T (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    726    726       T -> K (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    735    735       K -> Q (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    754    754       I -> M (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT    822    822       E -> K (in Ref. 2; CAA83549).
FT                                {ECO:0000305}.
FT   CONFLICT   1017   1018       LR -> WK (in Ref. 2; CAA83549).
FT                                {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
//
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