FYPP_PEA
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 03-AUG-2022, entry version 75.
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).
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}.
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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 Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
