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Q9FN02 (PPP7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 7

EC=3.1.3.16
Gene names
Name:PP7
Ordered Locus Names:At5g63870
ORF Names:MGI19.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatase active on para-nitrophenylphosphate (pNPP) and on various phosphoproteins such as myelin basic protein. Seems to act as a positive regulator of cryptochrome signaling involved in hypocotyl growth inhibition and cotyledon expansion under white and blue light conditions. Confers thermotolerance. Required for heat shock mediated-signaling pathway that leads to the expression of heat shock proteins (HSPs). Ref.5 Ref.10 Ref.11

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit. Ref.5

Binds 1 manganese ion per subunit. Ref.5

Enzyme regulation

Inhibited by NaF and orthovanadate, as well as by divalent cations such as Ni2+ and Zn2+. Inhibited by polylysine with myelin basic protein as substrate, but activated by polylysine with pNPP as substrate. Reversibly regulated by redox agents. Inhibited by submillimolar Pi concentrations. Slightly repressed by calmodulin (CaM). Ref.6

Subunit structure

Monomer, homodimer, and heteropolymer. Interacts with calmodulin (CaM3 and CaM4) and HSFA1A/HSF1. Ref.6 Ref.8 Ref.11

Subcellular location

Nucleusnucleoplasm Ref.9.

Tissue specificity

Expressed in leaves, and, to a lower extent, in stems and flowers. Ref.10

Induction

By heat shock. Ref.6 Ref.11

Sequence similarities

Belongs to the PPP phosphatase family. PP-7 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=1.7 mM for pNPP (at pH 7.8 and 25 degrees Celsius) Ref.5 Ref.7

pH dependence:

Optimum pH is around 7.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9FN02-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9FN02-2)

The sequence of this isoform differs from the canonical sequence as follows:
     298-301: LIIR → VTPK
     302-413: Missing.
Note: May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Serine/threonine-protein phosphatase 7
PRO_0000308991

Sites

Active site1461Proton donor By similarity
Metal binding841Iron By similarity
Metal binding861Iron By similarity
Metal binding1131Iron By similarity
Metal binding1131Manganese By similarity
Metal binding1451Manganese By similarity
Metal binding1971Manganese By similarity
Metal binding3031Manganese By similarity

Amino acid modifications

Disulfide bond28 ↔ 67 Probable

Natural variations

Alternative sequence298 – 3014LIIR → VTPK in isoform 2.
VSP_029088
Alternative sequence302 – 413112Missing in isoform 2.
VSP_029089

Experimental info

Mutagenesis207 – 23125PKRTT…SSMKL → GGGGGGGGGGGGGGGGGGGG GGGGG: Normal subcellular location. Ref.9
Mutagenesis209 – 23123Missing: Reduced activity, but enhanced inducibility by polylysine with pNPP as substrate; reduced binding with calmodulin. Ref.8
Mutagenesis369 – 41345Missing: Loss of activity; normal binding with calmodulin; cytoplasmic instead of nuclear subcellular location. Ref.8 Ref.9
Sequence conflict2661M → I in CAA03886. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 111A9E01A222A058

FASTA41346,619
        10         20         30         40         50         60 
METVPPSPIT WPDGGALTND WVHGLMSCFE WSSWNLPPSQ LPSLLPVNVF DSLVLTAHKI 

        70         80         90        100        110        120 
LHKERNCVHI DDLDSVSNVV VVGDIHGQLH DLLFLLKDTG FPCQNRCYVF NGDYVDRGAW 

       130        140        150        160        170        180 
GLETFLVLLS WKVLMPDRVY LLRGNHESKY CTSMYGFEKE VLTKYGDKGK HVYRKCLGCF 

       190        200        210        220        230        240 
EGLPLASIIS GRVYTAHGGL FRSPVLPKRT TRGKKNRRVV LLEPEPSSMK LGTLDELMQA 

       250        260        270        280        290        300 
RRSVLDPPWE GSNLIPGDVL WSDPSMTPGL SPNEQRGIGL LWGPDCTEDF LKKYELKLII 

       310        320        330        340        350        360 
RSHEGPDARE KRTGLGGMDN GYTIDHNVES GKLITIFSAP DYPQFQATEE RYKNKGAYII 

       370        380        390        400        410 
LQAPDFSDPQ FHSFEAVKPR PKAHPYYDFE NVIDSDDEMD KSAMDTNNEQ PNS 

« Hide

Isoform 2 [UniParc].

Checksum: A8D09318702B0C62
Show »

FASTA30133,880

References

« Hide 'large scale' references
[1]"PP7, a plant phosphatase representing a novel evolutionary branch of eukaryotic protein Ser/Thr phosphatases."
Andreeva A.V., Evans D.E., Hawes C.R., Bennett N., Kutuzov M.A.
Biochem. Mol. Biol. Int. 44:703-715(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[5]"Expression and characterization of PP7, a novel plant protein Ser/Thr phosphatase distantly related to RdgC/PPEF and PP5."
Kutuzov M.A., Evans D.E., Andreeva A.V.
FEBS Lett. 440:147-152(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION, DISULFIDE BOND, COFACTOR.
[6]"Purification of plant protein phosphatase PP7 and evidence for its redox regulation."
Andreeva A.V., Solov'eva O.V., Kakuev D.L., Kutuzov M.A.
Arch. Biochem. Biophys. 396:65-70(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBUNIT.
[7]"Noncompetitive inhibition of plant protein Ser/Thr phosphatase PP7 by phosphate."
Kutuzov M.A., Andreeva A.V.
Biochem. Biophys. Res. Commun. 283:93-96(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION BY INORGANIC PHOSPHATE.
[8]"Interaction of plant protein Ser/Thr phosphatase PP7 with calmodulin."
Kutuzov M.A., Bennett N., Andreeva A.V.
Biochem. Biophys. Res. Commun. 289:634-640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF 209-ARG--LEU-231 AND 369-PRO--SER-413.
[9]"Nuclear localization of the plant protein Ser/Thr phosphatase PP7."
Andreeva A.V., Kutuzov M.A.
Mol. Cell Biol. Res. Commun. 4:345-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 207-PRO--LEU-231 AND 369-PRO--SER-413, SUBCELLULAR LOCATION.
[10]"PP7 is a positive regulator of blue light signaling in Arabidopsis."
Moeller S.G., Kim Y.-S., Kunkel T., Chua N.-H.
Plant Cell 15:1111-1119(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"Calmodulin-binding protein phosphatase PP7 is involved in thermotolerance in Arabidopsis."
Liu H.-T., Li G.-L., Chang H., Sun D.-Y., Zhou R.-G., Li B.
Plant Cell Environ. 30:156-164(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CALMODULIN AND HSFA1A, INDUCTION BY HEAT SHOCK.
[12]"Arabidopsis PPP family of serine/threonine phosphatases."
Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000057 mRNA. Translation: CAA03886.1.
AB007646 Genomic DNA. Translation: BAB11035.1.
CP002688 Genomic DNA. Translation: AED97806.1.
CP002688 Genomic DNA. Translation: AED97807.1.
CP002688 Genomic DNA. Translation: AED97808.1.
AY050898 mRNA. No translation available.
PIRT51611.
RefSeqNP_568979.1. NM_125782.3.
NP_851258.2. NM_180927.3.
NP_851259.1. NM_180928.1.
UniGeneAt.20661.

3D structure databases

ProteinModelPortalQ9FN02.
SMRQ9FN02. Positions 11-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid21749. 4 interactions.
MINTMINT-222502.

Proteomic databases

PaxDbQ9FN02.
PRIDEQ9FN02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G63870.1; AT5G63870.1; AT5G63870. [Q9FN02-1]
AT5G63870.2; AT5G63870.2; AT5G63870. [Q9FN02-1]
GeneID836507.
KEGGath:AT5G63870.

Organism-specific databases

TAIRAT5G63870.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000242900.
InParanoidQ9FN02.
KOK15423.
OMAMDNGYTI.
PhylomeDBQ9FN02.
ProtClustDBCLSN2680605.

Enzyme and pathway databases

BioCycARA:AT5G63870-MONOMER.
ARA:GQT-397-MONOMER.
ARA:GQT-398-MONOMER.

Gene expression databases

GenevestigatorQ9FN02.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPP7_ARATH
AccessionPrimary (citable) accession number: Q9FN02
Secondary accession number(s): O49346, Q3E865
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names