ID FYPP3_ARATH Reviewed; 303 AA. AC Q9LHE7; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=Phytochrome-associated serine/threonine-protein phosphatase 3 {ECO:0000303|PubMed:12468726}; DE Short=AtFyPP3 {ECO:0000303|PubMed:12468726}; DE EC=3.1.3.16 {ECO:0000269|PubMed:22715043}; DE AltName: Full=Protein EMBRYO DEFECTIVE 2736 {ECO:0000305}; GN Name=FYPP3 {ECO:0000303|PubMed:12468726}; GN Synonyms=EMB2736 {ECO:0000305}, STPP {ECO:0000305}; GN OrderedLocusNames=At3g19980; ORFNames=MZE19.3; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, INTERACTION WITH PHYA AND PHYB, AND DISRUPTION PHENOTYPE. 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10907853; DOI=10.1093/dnares/7.3.217; RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC RT clones."; RL DNA Res. 7:217-221(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003; RA Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.; RT "Arabidopsis PPP family of serine/threonine phosphatases."; RL Trends Plant Sci. 12:169-176(2007). RN [6] RP INTERACTION WITH TAP46. RX PubMed=24357600; DOI=10.1104/pp.113.233684; RA Hu R., Zhu Y., Shen G., Zhang H.; RT "TAP46 plays a positive role in the ABSCISIC ACID INSENSITIVE5-regulated RT gene expression in Arabidopsis."; RL Plant Physiol. 164:721-734(2014). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH PIN1 AND PIN2, RP SUBUNIT, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP ASP-81. RX PubMed=22715043; DOI=10.1105/tpc.112.098905; RA Dai M., Zhang C., Kania U., Chen F., Xue Q., McCray T., Li G., Qin G., RA Wakeley M., Terzaghi W., Wan J., Zhao Y., Xu J., Friml J., Deng X.W., RA Wang H.; RT "A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation RT and auxin efflux in Arabidopsis."; RL Plant Cell 24:2497-2514(2012). RN [8] RP FUNCTION, AND INTERACTION WITH ABI5. RX PubMed=23404889; DOI=10.1105/tpc.112.105767; RA Dai M., Xue Q., Mccray T., Margavage K., Chen F., Lee J.H., Nezames C.D., RA Guo L., Terzaghi W., Wan J., Deng X.W., Wang H.; RT "The PP6 phosphatase regulates ABI5 phosphorylation and abscisic acid RT signaling in Arabidopsis."; RL Plant Cell 25:517-534(2013). RN [9] RP FUNCTION. RX PubMed=30373470; DOI=10.1080/15592324.2018.1536631; RA Haga K., Sakai T.; RT "Involvement of PP6-type protein phosphatase in hypocotyl phototropism in RT Arabidopsis seedlings."; RL Plant Signal. Behav. 13:e1536631-e1536631(2018). RN [10] RP FUNCTION, AND INTERACTION WITH PIF3 AND PIF4. RX PubMed=31527236; DOI=10.1073/pnas.1907540116; RA Yu X., Dong J., Deng Z., Jiang Y., Wu C., Qin X., Terzaghi W., Chen H., RA Dai M., Deng X.W.; RT "Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress RT photomorphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 116:20218-20225(2019). CC -!- FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6) (Probable). CC Dephosphorylates phosphorylated phytochromes, with a preference toward CC Pfr forms (PubMed:12468726). Plays a major role in the photoperiodic CC control of flowering time in long days by modulating phytochrome CC signals in flowering time control (PubMed:12468726). Involved in the CC regulation of polar auxin transport in roots (PubMed:22715043). CC Dephosphorylates directly the auxin efflux carriers PIN1 and PIN2, thus CC promoting their proper polar localization in root cell plasma membrane CC (PubMed:22715043). Acts antagonistically with the protein kinase PID to CC regulate the reversible phosphorylation of PIN and polar targeting, CC subsequently impacting polar auxin transport and plant development CC (PubMed:22715043). Involved in the regulation of abscisic acid (ABA) CC signaling during seed germination and postgermination seedling growth CC (PubMed:23404889). Functions as a negative regulator of ABA signaling CC through direct dephosphorylation and destabilization of ABI5 protein CC (PubMed:23404889). Acts antagonistically with the protein kinase CC SRK2E/SNRK2.6 to regulate ABI5 phosphorylation and ABA responses CC (PubMed:23404889). Involved in the regulation of phosphorylation status CC in hypocotyl phototropism (PubMed:30373470). Involved in the negative CC regulation of photomorphogenesis by controlling the stability and CC transcriptional activity of PIF3 and PIF4 proteins in the dark, via the CC regulation of their phosphorylation status (PubMed:31527236). CC {ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:22715043, CC ECO:0000269|PubMed:23404889, ECO:0000269|PubMed:30373470, CC ECO:0000269|PubMed:31527236, ECO:0000305|PubMed:22715043}. 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:22715043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; CC Evidence={ECO:0000269|PubMed:22715043}; 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:22715043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; CC Evidence={ECO:0000269|PubMed:22715043}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:22715043}; 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 (PubMed:12468726). Interacts with TAP46 CC (PubMed:24357600, PubMed:12468726). Interacts with NRP CC (PubMed:24357600). Interacts with PIN1 and PIN2 (PubMed:22715043). CC Interacts with ABI5 (PubMed:23404889). Interacts with PIF3 and PIF4 CC (PubMed:31527236). Protein phosphatase 6 (PP6) holoenzyme is a CC heterotrimeric complex formed by the catalytic subunit FYPP, a SAPS CC domain-containing subunit (SAL) and a protein phosphatase 2A regulatory CC subunit A (PP2AA) (PubMed:22715043). {ECO:0000269|PubMed:12468726, CC ECO:0000269|PubMed:22715043, ECO:0000269|PubMed:23404889, CC ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:31527236}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12468726}. CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers (PubMed:12468726). Also CC detected to a lower extent in stems and leaves (PubMed:12468726). CC Expressed in roots (PubMed:22715043). {ECO:0000269|PubMed:12468726, CC ECO:0000269|PubMed:22715043}. CC -!- DISRUPTION PHENOTYPE: Early flowering (PubMed:12468726). No visible CC phenotype under normal growth conditions, but the double mutant plants CC fypp1 and fypp3 exhibit severe developmental defects in roots and CC leaves, and show defective gravitropism (PubMed:22715043). CC {ECO:0000269|PubMed:12468726, ECO:0000269|PubMed:22715043}. 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; AF275664; AAK69404.1; -; mRNA. DR EMBL; AP002050; BAB03163.1; -; Genomic_DNA. DR EMBL; CP002686; AEE76315.1; -; Genomic_DNA. DR EMBL; AY064136; AAL36043.1; -; mRNA. DR EMBL; AY097414; AAM19930.1; -; mRNA. DR RefSeq; NP_188632.1; NM_112888.4. DR AlphaFoldDB; Q9LHE7; -. DR SMR; Q9LHE7; -. DR BioGRID; 6868; 27. DR IntAct; Q9LHE7; 1. DR STRING; 3702.Q9LHE7; -. DR PaxDb; 3702-AT3G19980-1; -. DR ProteomicsDB; 230007; -. DR EnsemblPlants; AT3G19980.1; AT3G19980.1; AT3G19980. DR GeneID; 821536; -. DR Gramene; AT3G19980.1; AT3G19980.1; AT3G19980. DR KEGG; ath:AT3G19980; -. DR Araport; AT3G19980; -. DR TAIR; AT3G19980; FYPP3. DR eggNOG; KOG0373; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; Q9LHE7; -. DR OMA; ANAWRWC; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; Q9LHE7; -. DR PRO; PR:Q9LHE7; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9LHE7; baseline and differential. DR GO; GO:0005737; C:cytoplasm; HDA:TAIR. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:TAIR. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR. 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:TAIR. DR GO; GO:0006470; P:protein dephosphorylation; IDA:TAIR. 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:SF67; PHYTOCHROME-ASSOCIATED SERINE_THREONINE-PROTEIN PHOSPHATASE 3; 1. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 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. DR Genevisible; Q9LHE7; AT. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome; Zinc. FT CHAIN 1..303 FT /note="Phytochrome-associated serine/threonine-protein FT phosphatase 3" FT /id="PRO_0000308990" 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" FT SITE 81 FT /note="Required for catalytic activity" FT /evidence="ECO:0000269|PubMed:22715043" FT MUTAGEN 81 FT /note="D->N: Almost abolishes catalytic activity." FT /evidence="ECO:0000269|PubMed:22715043" SQ SEQUENCE 303 AA; 34845 MW; 342FD1E21BC7D2B1 CRC64; MDLDQWISKV KDGQHLSEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD IHGQFHDLMK LFQTGGHVPD TNYIFMGDFV DRGYNSLEVF TILLLLKARY PANITLLRGN HESRQLTQVY GFYDECQRKY GNANAWRYCT DVFDYLTLSA IIDGTVLCVH GGLSPDVRTI DQIRLIERNC EIPHEGPFCD LMWSDPEDIE TWAVSPRGAG WLFGSRVTTE FNHINKLDLV CRAHQLVQEG LKYMFQDKGL VTVWSAPNYC YRCGNVASIL SFNDNMEREV KFFTETEENN QMRGPRTGVP YFL //