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Protein

Phytochrome-associated serine/threonine-protein phosphatase

Gene

FYPP

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Manganese 1By similarity
Metal bindingi52 – 521Manganese 1By similarity
Metal bindingi78 – 781Manganese 1By similarity
Metal bindingi78 – 781Manganese 2By similarity
Metal bindingi110 – 1101Manganese 2By similarity
Active sitei111 – 1111Proton donorBy similarity
Metal bindingi160 – 1601Manganese 2By similarity
Metal bindingi234 – 2341Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Phytochrome-associated serine/threonine-protein phosphatase (EC:3.1.3.16)
Alternative name(s):
PsFyPP
Gene namesi
Name:FYPP
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Phytochrome-associated serine/threonine-protein phosphatasePRO_0000308994Add
BLAST

Expressioni

Tissue specificityi

Mostly expressed in flowers and stems.1 Publication

Interactioni

Subunit structurei

Interacts with PHYA and PHYB, mostly when they are phosphorylated and in Pfr forms.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8LSN3.
SMRiQ8LSN3. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8LSN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLDQWISKV KDGQHLLEDE LQLLCEYVKE ILIEESNVQP VNSPVTVCGD
60 70 80 90 100
IHGQFHDLMK LFQTGGHVPE TNYIFMGDFV DRGYNSLEVF TILLLLKARY
110 120 130 140 150
PANITLLRGN HESRQLTQVY GFYDECQRKY GNANAWRYCT DVFDYLTLSA
160 170 180 190 200
IIDGTVLCVH GGLSPDIRTI DQIRVIERNC EIPHEGPFCD LMWSDPEDIE
210 220 230 240 250
TWAVSPRGAG WLFGSRVTSE FNHINNLDLV CRAHQLVQEG LKYMFQDKGL
260 270 280 290 300
VTVWSAPNYC YRCGNVASIL SFNENMEREV KFFTETEENN QMRGPRTGVP

YFL
Length:303
Mass (Da):34,871
Last modified:October 1, 2002 - v1
Checksum:i32AF9A225DF9F9ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305635 mRNA. Translation: AAM21172.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305635 mRNA. Translation: AAM21172.1.

3D structure databases

ProteinModelPortaliQ8LSN3.
SMRiQ8LSN3. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PHYA AND PHYB.

Entry informationi

Entry nameiFYPP_PEA
AccessioniPrimary (citable) accession number: Q8LSN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.