Q9SX52 (FYPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phytochrome-associated serine/threonine-protein phosphatase 1
Short name=AtFyPP1
EC=3.1.3.16

Gene names

Name:	FYPP1
Ordered Locus Names:	At1g50370
ORF Names:	F14I3.5

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	303 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms. Plays a major role in the photoperiodic control of flowering time in long days by modulating phytochrome signals in flowering time control By similarity. Ref.7
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron or zinc ion per subunit. Ref.7 Binds 1 manganese ion per subunit By similarity. Ref.7
Subunit structure	Interacts with PHYA and PHYB, mostly when they are phosphorylated and in Pfr forms By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Mostly expressed in flowers. Also detected to a lower extent in stems and leaves. Ref.7
Sequence similarities	Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Phytochrome-associated serine/threonine-protein phosphatase 1		PRO_0000308989
Sites
	Active site	111	1	Proton donor By similarity
	Metal binding	50	1	Iron By similarity
	Metal binding	52	1	Iron By similarity
	Metal binding	78	1	Iron By similarity
	Metal binding	78	1	Manganese By similarity
	Metal binding	110	1	Manganese By similarity
	Metal binding	160	1	Manganese By similarity
	Metal binding	234	1	Manganese By similarity
Experimental info
	Sequence conflict	68	1	V → F in BAE98396. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9SX52 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 44598694DD92D626	FASTA	303	34,819
	10 20 30 40 50 60 MDLDQWISKV KDGQHLSEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD IHGQFHDLMK 70 80 90 100 110 120 LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARH PANITLLRGN HESRQLTQVY 130 140 150 160 170 180 GFYDECQRKY GNANAWRYCT DVFDYLTLSA IIDGTVLCVH GGLSPDVRTI DQIRLIERNC 190 200 210 220 230 240 EIPHEGPFCD LMWSDPEDIE TWAVSPRGAG WLFGSRVTTE FNHINNLDLV CRAHQLVQEG 250 260 270 280 290 300 LKYMFQDKGL VTVWSAPNYC YRCGNVASIL SFNDNMEREV KFFTETEENN QMRGPRTGVP YFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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]. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"A phytochrome-associated protein phosphatase 2A modulates light signals in flowering time control in Arabidopsis." Kim D.-H., Kang J.-G., Yang S.-S., Chung K.-S., Song P.-S., Park C.-M. Plant Cell 14:3043-3056(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTORS, TISSUE SPECIFICITY.
[8]	"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	AC007980 Genomic DNA. Translation: AAD50050.1. CP002684 Genomic DNA. Translation: AEE32541.1. AF428374 mRNA. Translation: AAL16304.1. BT020404 mRNA. Translation: AAV97795.1. AK226232 mRNA. Translation: BAE98396.1. AY087422 mRNA. Translation: AAM64970.1.
IPI	IPI00531932.
PIR	H96539.
RefSeq	NP_175454.1. NM_103920.3.
UniGene	At.18962. At.5940.
3D structure databases
ProteinModelPortal	Q9SX52.
SMR	Q9SX52. Positions 2-277.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SX52. 1 interaction.
Proteomic databases
PaxDb	Q9SX52.
PRIDE	Q9SX52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G50370.1; AT1G50370.1; AT1G50370.
GeneID	841459.
KEGG	ath:AT1G50370.
Organism-specific databases
TAIR	At1g50370.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172696.
InParanoid	Q9SX52.
KO	K15498.
OMA	DEEYLCT.
PhylomeDB	Q9SX52.
ProtClustDB	CLSN2682722.
Gene expression databases
Genevestigator	Q9SX52.
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

FYPP1_ARATH

Accession

Primary (citable) accession number: Q9SX52
Secondary accession number(s): Q0WWV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program