Q9FN02 (PPP7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 7
EC=3.1.3.16

Gene names

Name:	PP7
Ordered Locus Names:	At5g63870
ORF Names:	MGI19.7

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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	Nucleus › nucleoplasm 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

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blue light signaling pathway Inferred from mutant phenotype Ref.10. Source: TAIR response to heat Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular_component	nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.9. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.5. Source: TAIR
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 413	413	Serine/threonine-protein phosphatase 7		PRO_0000308991
Sites
	Active site	146	1	Proton donor By similarity
	Metal binding	84	1	Iron By similarity
	Metal binding	86	1	Iron By similarity
	Metal binding	113	1	Iron By similarity
	Metal binding	113	1	Manganese By similarity
	Metal binding	145	1	Manganese By similarity
	Metal binding	197	1	Manganese By similarity
	Metal binding	303	1	Manganese By similarity
Amino acid modifications
	Disulfide bond	28 ↔ 67		Probable
Natural variations
	Alternative sequence	298 – 301	4	LIIR → VTPK in isoform 2.		VSP_029088
	Alternative sequence	302 – 413	112	Missing in isoform 2.		VSP_029089
Experimental info
	Mutagenesis	207 – 231	25	PKRTT…SSMKL → GGGGGGGGGGGGGGGGGGGG GGGGG: Normal subcellular location. Ref.9
	Mutagenesis	209 – 231	23	Missing: Reduced activity, but enhanced inducibility by polylysine with pNPP as substrate; reduced binding with calmodulin. Ref.8
	Mutagenesis	369 – 413	45	Missing: Loss of activity; normal binding with calmodulin; cytoplasmic instead of nuclear subcellular location. Ref.8 Ref.9
	Sequence conflict	266	1	M → I in CAA03886. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 111A9E01A222A058	FASTA	413	46,619
	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
	Isoform 2 [UniParc]. Checksum: A8D09318702B0C62	FASTA	301	33,880
	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 LKKYELKVTP K

References

	« Hide 'large scale' referencesShow '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. , 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, COFACTORS.
[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.
IPI	IPI00531246. IPI00542251.
PIR	T51611.
RefSeq	NP_568979.1. NM_125782.3. NP_851258.2. NM_180927.3. NP_851259.1. NM_180928.1.
UniGene	At.20661.
3D structure databases
HSSP	HSSP built from PDB template 1S95 based on UniProtKB P53041.
ProteinModelPortal	Q9FN02.
SMR	Q9FN02. Positions 52-385.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-222502.
Proteomic databases
PaxDb	Q9FN02.
PRIDE	Q9FN02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G63870.1; AT5G63870.1; AT5G63870. AT5G63870.2; AT5G63870.2; AT5G63870.
GeneID	836507.
KEGG	ath:AT5G63870.
Organism-specific databases
TAIR	At5g63870.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000242900.
InParanoid	Q9FN02.
OMA	MDNGYTI.
PhylomeDB	Q9FN02.
ProtClustDB	CLSN2680605.
Gene expression databases
Genevestigator	Q9FN02.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPP7_ARATH

Accession

Primary (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:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program