ID FYPP1_ARATH Reviewed; 303 AA. AC Q9SX52; Q0WWV2; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Phytochrome-associated serine/threonine-protein phosphatase 1 {ECO:0000303|PubMed:12468726}; DE Short=AtFyPP1 {ECO:0000303|PubMed:12468726}; DE EC=3.1.3.16 {ECO:0000269|PubMed:22715043}; GN Name=FYPP1 {ECO:0000303|PubMed:12468726}; GN OrderedLocusNames=At1g50370 {ECO:0000312|Araport:AT1G50370}; GN ORFNames=F14I3.5 {ECO:0000312|EMBL:AAD50050.1}; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP TISSUE SPECIFICITY. 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 [8] 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 [9] RP INTERACTION WITH TAP46. RX PubMed=21216945; DOI=10.1105/tpc.110.074005; RA Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.; RT "The PP2A regulatory subunit Tap46, a component of the TOR signaling RT pathway, modulates growth and metabolism in plants."; RL Plant Cell 23:185-209(2011). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH PIN1 AND PIN2, RP SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 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 [11] 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 [12] 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 [13] 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 [14] 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. Plays a major role in the photoperiodic control of flowering CC time in long days by modulating phytochrome signals in flowering time CC control (By similarity). Involved in the regulation of polar auxin CC transport in roots (PubMed:22715043). Dephosphorylates directly the CC auxin efflux carriers PIN1 and PIN2, thus promoting their proper polar CC localization in root cell plasma membrane (PubMed:22715043). Acts CC antagonistically with the protein kinase PID to regulate the reversible CC phosphorylation of PIN and polar targeting, subsequently impacting CC polar auxin transport and plant development (PubMed:22715043). Involved CC in the regulation of abscisic acid (ABA) signaling during seed CC germination and postgermination seedling growth (PubMed:23404889). CC Functions as a negative regulator of ABA signaling through direct CC dephosphorylation and destabilization of ABI5 (PubMed:23404889). Acts CC antagonistically with the protein kinase SRK2E/SNRK2.6 to regulate ABI5 CC phosphorylation and ABA responses (PubMed:23404889). Involved in the CC regulation of phosphorylation status in hypocotyl phototropism CC (PubMed:30373470). Involved in the negative regulation of CC photomorphogenesis by controlling the stability and transcriptional CC activity of PIF3 and PIF4 proteins in the dark, via the regulation of CC their phosphorylation status (PubMed:31527236). CC {ECO:0000250|UniProtKB:Q9LHE7, 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 (By similarity). Interacts with TAP46 CC (PubMed:21216945, PubMed:24357600) (By similarity). Interacts with PIN1 CC and PIN2 (PubMed:22715043). Interacts with ABI5 (PubMed:23404889). CC Interacts with PIF3 and PIF4 (PubMed:31527236). Protein phosphatase 6 CC (PP6) holoenzyme is a heterotrimeric complex formed by the catalytic CC subunit FYPP, a SAPS domain-containing subunit (SAL) and a protein CC phosphatase 2A regulatory subunit A (PP2AA) (PubMed:22715043). CC {ECO:0000250|UniProtKB:Q9LHE7, ECO:0000269|PubMed:21216945, CC ECO:0000269|PubMed:22715043, ECO:0000269|PubMed:23404889, CC ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:31527236}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9LHE7}. 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: No visible phenotype under normal growth CC conditions, but the double mutant plants fypp1 and fypp3 exhibit severe CC developmental defects in roots and leaves, and show defective CC gravitropism. {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; AC007980; AAD50050.1; -; Genomic_DNA. DR EMBL; CP002684; AEE32541.1; -; Genomic_DNA. DR EMBL; AF428374; AAL16304.1; -; mRNA. DR EMBL; BT020404; AAV97795.1; -; mRNA. DR EMBL; AK226232; BAE98396.1; -; mRNA. DR EMBL; AY087422; AAM64970.1; -; mRNA. DR PIR; H96539; H96539. DR RefSeq; NP_175454.1; NM_103920.4. DR AlphaFoldDB; Q9SX52; -. DR SMR; Q9SX52; -. DR BioGRID; 26684; 31. DR IntAct; Q9SX52; 2. DR STRING; 3702.Q9SX52; -. DR PaxDb; 3702-AT1G50370-1; -. DR ProteomicsDB; 230540; -. DR EnsemblPlants; AT1G50370.1; AT1G50370.1; AT1G50370. DR GeneID; 841459; -. DR Gramene; AT1G50370.1; AT1G50370.1; AT1G50370. DR KEGG; ath:AT1G50370; -. DR Araport; AT1G50370; -. DR TAIR; AT1G50370; FYPP1. DR eggNOG; KOG0373; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; Q9SX52; -. DR OMA; MEGFKYH; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; Q9SX52; -. DR PRO; PR:Q9SX52; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9SX52; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 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. DR Genevisible; Q9SX52; 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 1" FT /id="PRO_0000308989" 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" FT CONFLICT 68 FT /note="V -> F (in Ref. 5; BAE98396)" FT /evidence="ECO:0000305" SQ SEQUENCE 303 AA; 34819 MW; 44598694DD92D626 CRC64; MDLDQWISKV KDGQHLSEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD IHGQFHDLMK LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARH PANITLLRGN HESRQLTQVY GFYDECQRKY GNANAWRYCT DVFDYLTLSA IIDGTVLCVH GGLSPDVRTI DQIRLIERNC EIPHEGPFCD LMWSDPEDIE TWAVSPRGAG WLFGSRVTTE FNHINNLDLV CRAHQLVQEG LKYMFQDKGL VTVWSAPNYC YRCGNVASIL SFNDNMEREV KFFTETEENN QMRGPRTGVP YFL //