FYPP1_ARATH
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 03-AUG-2022, entry version 130.
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 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}.
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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; 30.
DR IntAct; Q9SX52; 2.
DR STRING; 3702.AT1G50370.1; -.
DR PaxDb; Q9SX52; -.
DR PRIDE; Q9SX52; -.
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; locus:2011907; AT1G50370.
DR eggNOG; KOG0373; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q9SX52; -.
DR OMA; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q9SX52; -.
DR PRO; PR:Q9SX52; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX52; baseline and differential.
DR Genevisible; Q9SX52; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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 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
