PHY1_PHYPA
ID PHY1_PHYPA Reviewed; 1123 AA.
AC P36505; A9THP5; I7GPR5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phytochrome 1;
GN Name=PHY1; ORFNames=PHYPADRAFT_222399;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8224238; DOI=10.1016/0014-5793(93)81689-w;
RA Kolukisaoglu H.U., Braun B., Martin W.F., Schneider-Poetsch H.A.W.;
RT "Mosses do express conventional, distantly B-type-related phytochromes.
RT Phytochrome of Physcomitrella patens (Hedw.).";
RL FEBS Lett. 334:95-100(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17662030; DOI=10.1111/j.1365-313x.2007.03202.x;
RA Uenaka H., Kadota A.;
RT "Functional analyses of the Physcomitrella patens phytochromes in
RT regulating chloroplast avoidance movement.";
RL Plant J. 51:1050-1061(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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 morphogenetic responses, whereas reconversion of
CC Pfr 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. Mediates chloroplast avoidance movement in cytoplasm.
CC {ECO:0000269|PubMed:17662030}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17662030}.
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; X75025; CAA52933.1; -; mRNA.
DR EMBL; AB275304; BAF51707.1; -; mRNA.
DR EMBL; DS545122; EDQ57045.1; -; Genomic_DNA.
DR PIR; S37206; S37206.
DR RefSeq; XP_001778155.1; XM_001778103.1.
DR AlphaFoldDB; P36505; -.
DR SMR; P36505; -.
DR STRING; 3218.PP1S233_24V6.1; -.
DR PRIDE; P36505; -.
DR EnsemblPlants; Pp3c25_2610V3.1; Pp3c25_2610V3.1; Pp3c25_2610.
DR EnsemblPlants; Pp3c25_2610V3.2; Pp3c25_2610V3.2; Pp3c25_2610.
DR Gramene; Pp3c25_2610V3.1; Pp3c25_2610V3.1; Pp3c25_2610.
DR Gramene; Pp3c25_2610V3.2; Pp3c25_2610V3.2; Pp3c25_2610.
DR eggNOG; ENOG502QRNS; Eukaryota.
DR HOGENOM; CLU_010418_0_0_1; -.
DR OrthoDB; 27870at2759; -.
DR Proteomes; UP000006727; Chromosome 25.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0009903; P:chloroplast avoidance movement; IDA:UniProtKB.
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 CDD; cd16932; HATPase_Phy-like; 1.
DR CDD; cd00082; HisKA; 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; IPR003661; HisK_dim/P.
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; PF00512; HisKA; 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; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 2: Evidence at transcript level;
KW Chromophore; Cytoplasm; Photoreceptor protein; Receptor;
KW Reference proteome; Repeat; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1..1123
FT /note="Phytochrome 1"
FT /id="PRO_0000171984"
FT DOMAIN 216..395
FT /note="GAF"
FT DOMAIN 610..681
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 744..815
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 895..1115
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 321
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250"
FT CONFLICT 216
FT /note="D -> N (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> S (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="R -> P (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 535..536
FT /note="KD -> NH (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="D -> A (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="M -> H (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 707..713
FT /note="NACSSRD -> DACSSIH (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 897..898
FT /note="RQ -> VR (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="I -> L (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="V -> S (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="M -> CRSLYSYLLA (in Ref. 1; CAA52933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1123 AA; 124369 MW; 1AC6B55C340FD75E CRC64;
MSTPKKTYSS TSSAKSKAHS VRVAQTTADA ALQAVFEKSG DSGDSFDYSK SVSKSTAESL
PSGAVTAYLQ RMQRGGLTQS FGCMIAVEGT GFRVIAYSEN APEILDLVPQ AVPSVGEMDT
LRIGTDVRTL FTASSVASLE KAAEAQEMSL LNPITVNCRR SGKQLYAIAH RIDIGIVIDF
EAVKTDDHLV SAAGALQSHK LAAKAITRLQ ALPGGDIGLL CDTVVEEVRE LTGYDRVMAY
RFHEDEHGEV VAEIRRADLE PYLGLHYPGT DIPQASRFLF MKNKVRIIAD CSAPPVKVIQ
DPTLRQPVSL AGSTLRSPHG CHAQYMGNMG SIASLVMAVI INDNEEDSHG SVQRGRKLWG
LVVCHHTSPR TVPFPLRSAC GFLMQVFGLQ LNMEVELAAQ LREKHILRTQ TLLCDMLLRD
APIGIVSQIP NIMDLVKCDG AALYYGKRFW LLGTTPTESQ IKDIAEWLLE YHKDSTGLST
DSLADANYPA AHLLGDAVCG MAAAKITAKD FLFWFRSHTA KEIKWGGAKH DPGEKDDGRK
MHPRSSFKAF LEVVKRRSLP WEDVEMDAIH SLQLILRGSF QDIDDSDTKT MIHARLNDLK
LHDMDELSVV ANEMVRLIET ATAPILAVDS NGMINGWNAK IAQVTGLPVS EAMGRSLVKD
LVTDESVAVV ERLLYLALRG EEEQNVEIKL KTFGTQTEKG VVILIVNACS SRDVSENVVG
VCFVGQDVTG QKMFMDKFTR IQGDYKTIVQ NPHPLIPPIF GADEFGYCFE WNPAMEGLTG
WKKDEVVGKL LVGEIFGMQM MCCRMKSQDA MTKFMIALNT AMDGQSTDKF TFSFFDREGK
YVDVLLSTNK RTNADGVITG VFCFLQIASS ELQQALKVQR ATEKVAVAKL KELAYIRQEI
KNPLCGITFT RQLLEDTDLS DDQQQFLDTS AVCEQQLQKV LNDMDLESIE DGYLELDTAE
FEMGTVMNAV ISQGMTTSRE KGLQIFRETP REINTMRLLG DQIRLQQVLS DFLLNTVRFT
PSPEGWVKIK VVPTRKRLGG SVHVVHLEFR VSHPGAGLPE ELVLEMYDRG KGMTQEGLGL
NMCRKLVRLM NGDVHYVREA MQCYFVVNVE LPMAQRDDAS SQM
