ID FYPP_PEA Reviewed; 303 AA. AC Q8LSN3; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Phytochrome-associated serine/threonine-protein phosphatase {ECO:0000303|PubMed:12468726}; DE EC=3.1.3.16 {ECO:0000269|PubMed:12468726}; DE AltName: Full=PsFyPP {ECO:0000303|PubMed:12468726}; GN Name=FYPP {ECO:0000303|PubMed:12468726}; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PHYA AND RP PHYB. RX PubMed=12468726; DOI=10.1105/tpc.005306; RA Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S., Park C.-M.; RT "A phytochrome-associated protein phosphatase 2A modulates light signals in RT flowering time control in Arabidopsis."; RL Plant Cell 14:3043-3056(2002). CC -!- FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6) (Probable). CC Dephosphorylates phosphorylated phytochromes, with a preference toward CC Pfr forms. Plays a major role in the photoperiodic control of flowering CC time in long days by modulating phytochrome signals in flowering time CC control. {ECO:0000269|PubMed:12468726, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12468726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; CC Evidence={ECO:0000269|PubMed:12468726}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12468726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; CC Evidence={ECO:0000269|PubMed:12468726}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:12468726}; CC Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:P36873}; CC -!- SUBUNIT: Interacts with PHYA and PHYB, mostly when they are CC phosphorylated and in Pfr forms. {ECO:0000269|PubMed:12468726}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12468726}. CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and stems. CC {ECO:0000269|PubMed:12468726}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V) CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF305635; AAM21172.1; -; mRNA. DR AlphaFoldDB; Q8LSN3; -. DR SMR; Q8LSN3; -. DR EnsemblPlants; Psat6g101520.2; Psat6g101520.2.cds; Psat6g101520. DR Gramene; Psat6g101520.2; Psat6g101520.2.cds; Psat6g101520. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0009910; P:negative regulation of flower development; IMP:UniProtKB. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR047129; PPA2-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1. DR PANTHER; PTHR45619:SF10; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase; Zinc. FT CHAIN 1..303 FT /note="Phytochrome-associated serine/threonine-protein FT phosphatase" FT /id="PRO_0000308994" FT ACT_SITE 111 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" SQ SEQUENCE 303 AA; 34871 MW; 32AF9A225DF9F9ED CRC64; MDLDQWISKV KDGQHLLEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD IHGQFHDLMK LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARY PANITLLRGN HESRQLTQVY GFYDECQRKY GNANAWRYCT DVFDYLTLSA IIDGTVLCVH GGLSPDIRTI DQIRVIERNC EIPHEGPFCD LMWSDPEDIE TWAVSPRGAG WLFGSRVTSE FNHINNLDLV CRAHQLVQEG LKYMFQDKGL VTVWSAPNYC YRCGNVASIL SFNENMEREV KFFTETEENN QMRGPRTGVP YFL //