FYPP3_ARATH
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 03-AUG-2022, entry version 130.
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 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}.
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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.AT3G19980.1; -.
DR PaxDb; Q9LHE7; -.
DR PRIDE; Q9LHE7; -.
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; locus:2095380; AT3G19980.
DR eggNOG; KOG0373; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q9LHE7; -.
DR OMA; TVHENGE; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q9LHE7; -.
DR PRO; PR:Q9LHE7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHE7; baseline and differential.
DR Genevisible; Q9LHE7; AT.
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 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;
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
