PHYA5_AVESA
ID PHYA5_AVESA Reviewed; 495 AA.
AC P06595;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phytochrome A type 5;
DE Short=AP5;
DE Flags: Fragment;
GN Name=PHYA5; Synonyms=PHY5;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3001642; DOI=10.1093/nar/13.23.8543;
RA Hershey H.P., Barker R.F., Idler K.B., Lissemore J.L., Quail P.H.;
RT "Analysis of cloned cDNA and genomic sequences for phytochrome: complete
RT amino acid sequences for two gene products expressed in etiolated Avena.";
RL Nucleic Acids Res. 13:8543-8559(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-13.
RA Grimm R., Kellermann J., Schaefer W., Ruediger W.;
RT "The amino-terminal structure of oat phytochrome.";
RL FEBS Lett. 234:497-499(1988).
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 -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC -!- SIMILARITY: Belongs to the phytochrome family. {ECO:0000305}.
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DR EMBL; X03244; CAA27001.1; -; mRNA.
DR PIR; S00098; S00098.
DR AlphaFoldDB; P06595; -.
DR SMR; P06595; -.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013516; Phyto_chromo_BS.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 1: Evidence at protein level;
KW Chromophore; Direct protein sequencing; Photoreceptor protein; Receptor;
KW Sensory transduction; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..>495
FT /note="Phytochrome A type 5"
FT /id="PRO_0000171969"
FT DOMAIN 217..402
FT /note="GAF"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent, via 1 link"
FT NON_TER 495
SQ SEQUENCE 495 AA; 54803 MW; B24517DF9B53656C CRC64;
MSSSRPASSS SSRNRQSSQA RVLAQTTLDA ELNAEYEESG DSFDYSKLVE AQRDGPPVQQ
GRSEKVIAYL QHIQKGKLIQ TFGCLLALDE KSFNVIAFSE NAPEMLTTVS HAVPSVDDPP
RLGIGTNVRS LFSDQGATAL HKALGFADVS LLNPILVQCK TSGKPFYAIV HRATGCLVVD
FEPVKPTEFP ATAAGALQSY KLAAKAISKI QSLPGGSMEM LCNTVVKEVF DLTGYDRVMA
YKFHEDDHGE VFSEITKPGL EPYLGLHYPA TDIPQAARFL FMKNKVRMIC DCRARSIKVI
EAEALPFDIS LCGSALRAPH SCHLQYMENM NSIASLVMAV VVNENEEDDE AESEQPAQQQ
KKKKLWGLLV CHHESPRYVP FPLRYACEFL AQVFAVHVNR EFELEKQLRE KNILKMQTML
SDMLFREASP LTIVSGNPNI MDLVKCDGAA LLYGGKVWRL RNAPTESQIH DIAFWLSDVH
RDSTGLSTDS LHDAG