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Q56YP2 (PI5K1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-phosphate 5-kinase 1

Short name=AtPIP5K1
EC=2.7.1.68
Alternative name(s):
1-phosphatidylinositol 4-phosphate kinase 1
Diphosphoinositide kinase 1
PtdIns(4)P-5-kinase 1
Gene names
Name:PIP5K1
Synonyms:P5K1
Ordered Locus Names:At1g21980
ORF Names:F2E2.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate. Ref.6

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

Tissue specificity

Expressed in the whole plant, preferentially in roots. Strongly expressed in meristematic tissues, namely procambial cell layers. Ref.2 Ref.7

Induction

By abscisic acid (ABA), drought and salt treatment. Ref.2

Post-translational modification

Phosphorylation inactivates the enzyme.

Sequence similarities

Contains 7 MORN repeats.

Contains 1 PIPK domain.

Sequence caution

The sequence AAF86542.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAA33501.1 differs from that shown. Reason: Frameshift at position 91.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Phosphatidylinositol 4-phosphate 5-kinase 1
PRO_0000185473

Regions

Repeat81 – 10323MORN 1
Repeat104 – 12623MORN 2
Repeat127 – 14923MORN 3
Repeat150 – 17223MORN 4
Repeat173 – 19523MORN 5
Repeat196 – 21823MORN 6
Repeat219 – 24123MORN 7
Domain349 – 748400PIPK
Region708 – 72922Activation loop By similarity
Compositional bias5 – 128Poly-Glu

Experimental info

Sequence conflict1821Q → P in AAB82658. Ref.1
Sequence conflict1861G → S in AAB82658. Ref.1
Sequence conflict2021S → I in BAA33501. Ref.2
Sequence conflict4161C → Y in BAA33501. Ref.2
Sequence conflict4191V → M in BAA33501. Ref.2
Sequence conflict4561F → L in BAA33501. Ref.2
Sequence conflict5881E → D in BAA33501. Ref.2
Sequence conflict6021H → P in BAA33501. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q56YP2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 8A9E7D10A32CBF53

FASTA75285,945
        10         20         30         40         50         60 
MSDSEEDEEE EEASEVILSS VVQKKKKKNL RFGEEVERRD GLVLLAQSTP MVRSRSQGTT 

        70         80         90        100        110        120 
RRVTPTPLVD VEKPLPNGDL YIGSFSGGFP HGSGKYLWKD GCMYEGDWKR GKASGKGKFS 

       130        140        150        160        170        180 
WPSGATYEGE FKSGRMEGFG TFTGADGDTY RGTWVADRKH GHGQKRYANG DFYEGTWRRN 

       190        200        210        220        230        240 
LQDGRGRYVW RNGNQYTGEW RSGVISGKGL LVWPNGNRYE GLWENGIPKG NGVFTWSDGS 

       250        260        270        280        290        300 
SCVGAWNESN IMRSFFNGVE KNDLIVGNRK RSSVDSGAGS LGGEKVFPRI CIWESDGEAG 

       310        320        330        340        350        360 
DITCDIIDNV EASMIYRDRI SVDRDGFRQF KKNPCWFNGE AKKPGQTISK GHKKYDLMLN 

       370        380        390        400        410        420 
LQLGIRYSVG KHASIVRDLK QTDFDPKEKF WTRFPPEGTK TTPPHQSVDF RWKDYCPLVF 

       430        440        450        460        470        480 
RRLRELFQVD PAKYMLAICG NDALRELSSP GKSGSFFYLT QDDRFMIKTV KKSEVKVLLR 

       490        500        510        520        530        540 
MLPSYYKHVC QYENSLVTRF YGVHCVKPVG GQKTRFIVMG NLFCSEYRIQ RRFDLKGSSH 

       550        560        570        580        590        600 
GRSTAKPEGE IDETTTLKDL DLNFSFRLQR NWYQELMKQI KRDCEFLEAE RIMDYSLLVG 

       610        620        630        640        650        660 
VHFRDDNTGE KMGLSPFVLR SGRIDSYQNE KFMRGCRFLE AELQDMDRIL AGRKPSIRLG 

       670        680        690        700        710        720 
ANMPAKAERM ARRSDFDQYS SGGASYPSHG EMYEVVLYFG VIDILQDYDI TKKIEHAYKS 

       730        740        750 
LQADPASISA VDPKLYSKRF RDFISRIFIE EG 

« Hide

References

« Hide 'large scale' references
[1]"An Arabidopsis phosphatidylinositol-4-phosphate 5-kinase homolog with seven novel repeats rich in aromatic and glycine residues."
Satterlee J.S., Sussman M.R.
Plant Gene Register PGR97-150
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana."
Mikami K., Katagiri T., Iuchi S., Yamaguchi-Shinozaki K., Shinozaki K.
Plant J. 15:563-568(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"AtPIP5K1, an Arabidopsis thaliana phosphatidylinositol phosphate kinase, synthesizes PtdIns(3,4)P(2) and PtdIns(4,5)P(2) in vitro and is inhibited by phosphorylation."
Westergren T., Dove S.K., Sommarin M., Pical C.
Biochem. J. 359:583-589(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[7]"An Arabidopsis inositol phospholipid kinase strongly expressed in procambial cells: synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 in insect cells by 5-phosphorylation of precursors."
Elge S., Brearley C., Xia H.J., Kehr J., Xue H.W., Mueller-Roeber B.
Plant J. 26:561-571(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[8]"Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C."
Mueller-Roeber B., Pical C.
Plant Physiol. 130:22-46(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019380 mRNA. Translation: AAB82658.1.
AB005902 mRNA. Translation: BAA33501.1. Frameshift.
AC069252 Genomic DNA. Translation: AAF86542.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE30181.1.
AK221279 mRNA. Translation: BAD93975.1.
PIRT51821.
RefSeqNP_173617.1. NM_102047.3.
UniGeneAt.22532.

3D structure databases

ProteinModelPortalQ56YP2.
SMRQ56YP2. Positions 91-254, 353-749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24040. 6 interactions.
MINTMINT-8067725.
STRING3702.AT1G21980.1-P.

Proteomic databases

PRIDEQ56YP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G21980.1; AT1G21980.1; AT1G21980.
GeneID838801.
KEGGath:AT1G21980.

Organism-specific databases

GeneFarm5099.
TAIRAT1G21980.

Phylogenomic databases

eggNOGCOG4642.
HOGENOMHOG000193875.
InParanoidQ56YP2.
KOK00889.
OMACDIIDNV.
PhylomeDBQ56YP2.
ProtClustDBCLSN2679235.

Enzyme and pathway databases

BioCycARA:AT1G21980-MONOMER.

Gene expression databases

ArrayExpressQ56YP2.
GenevestigatorQ56YP2.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
InterProIPR003409. MORN.
IPR017163. PIno-4-P-5_kinase_pln.
IPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERPTHR23086. PTHR23086. 1 hit.
PfamPF02493. MORN. 7 hits.
PF01504. PIP5K. 1 hit.
[Graphical view]
PIRSFPIRSF037274. PIP5K_plant_prd. 1 hit.
SMARTSM00698. MORN. 7 hits.
SM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePI5K1_ARATH
AccessionPrimary (citable) accession number: Q56YP2
Secondary accession number(s): O22503, O82120, Q9LM65
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 75 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