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 12-APR-2017, entry version 109.
DE RecName: Full=Phytochrome-associated serine/threonine-protein phosphatase 3;
DE Short=AtFyPP3;
DE EC=3.1.3.16;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2736;
GN Name=FYPP3; Synonyms=EMB2736, STPP; OrderedLocusNames=At3g19980;
GN ORFNames=MZE19.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, TISSUE SPECIFICITY,
RP AND INTERACTION WITH PHYA AND 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.,
RA Park C.-M.;
RT "A phytochrome-associated protein phosphatase 2A modulates light
RT signals in 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.
RT Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
RT and BAC clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Portal (Araport);
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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).
CC -!- FUNCTION: Dephosphorylates phosphorylated phytochromes, with a
CC preference toward Pfr forms. Plays a major role in the
CC photoperiodic control of flowering time in long days by modulating
CC phytochrome signals in flowering time control.
CC {ECO:0000269|PubMed:12468726}.
CC -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
CC = [a protein]-serine/threonine + phosphate.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
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:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers. Also detected to
CC a lower extent in stems and leaves. {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; 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 UniGene; At.5940; -.
DR ProteinModelPortal; Q9LHE7; -.
DR SMR; Q9LHE7; -.
DR BioGrid; 6868; 5.
DR STRING; 3702.AT3G19980.1; -.
DR PaxDb; Q9LHE7; -.
DR PRIDE; Q9LHE7; -.
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 eggNOG; ENOG410XNR9; LUCA.
DR HOGENOM; HOG000172696; -.
DR InParanoid; Q9LHE7; -.
DR KO; K15498; -.
DR OMA; FYEECLT; -.
DR OrthoDB; EOG09360F5Z; -.
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; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP: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 Complete proteome; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1 303 Phytochrome-associated serine/threonine-
FT protein phosphatase 3.
FT /FTId=PRO_0000308990.
FT ACT_SITE 111 111 Proton donor. {ECO:0000250}.
FT METAL 50 50 Manganese 1. {ECO:0000250}.
FT METAL 52 52 Manganese 1. {ECO:0000250}.
FT METAL 78 78 Manganese 1. {ECO:0000250}.
FT METAL 78 78 Manganese 2. {ECO:0000250}.
FT METAL 110 110 Manganese 2. {ECO:0000250}.
FT METAL 160 160 Manganese 2. {ECO:0000250}.
FT METAL 234 234 Manganese 2. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 107 112 ipat:SER_THR_PHOSPHATASE [T]
FT MYHIT 44 235 ipfam:Metallophos [T]
FT MYHIT 16 287 ismart:PP2Ac [T]
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
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