Reviewed, UniProtKB/Swiss-Prot Q56YP2 (PI5K1_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-4-phosphate 5-kinase 1
      Short name=AtPIP5K1
    EC=2.7.1.68
Alternative name(s):
    1-phosphatidylinositol-4-phosphate kinase 1
    PtdIns(4)P-5-kinase 1
    Diphosphoinositide kinase 1

Gene names

Name:	PIP5K1
Synonyms:	P5K1
Ordered Locus Names:	At1g21980
ORF Names:	F2E2.1

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Stress response
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphatidylinositol metabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from direct assay. Source: TAIR ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin filament binding Inferred from direct assay. Source: TAIR actin monomer binding Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 752	752	Phosphatidylinositol-4-phosphate 5-kinase 1		PRO_0000185473
Regions
	Repeat	81 – 103	23	MORN 1
	Repeat	104 – 126	23	MORN 2
	Repeat	127 – 149	23	MORN 3
	Repeat	150 – 172	23	MORN 4
	Repeat	173 – 195	23	MORN 5
	Repeat	196 – 218	23	MORN 6
	Repeat	219 – 241	23	MORN 7
	Domain	349 – 748	400	PIPK
	Region	708 – 729	22	Activation loop By similarity
	Compositional bias	5 – 12	8	Poly-Glu
Experimental info
	Sequence conflict	182	1	Q → P in AAB82658. Ref.1
	Sequence conflict	186	1	G → S in AAB82658. Ref.1
	Sequence conflict	202	1	S → I in BAA33501. Ref.2
	Sequence conflict	416	1	C → Y in BAA33501. Ref.2
	Sequence conflict	419	1	V → M in BAA33501. Ref.2
	Sequence conflict	456	1	F → L in BAA33501. Ref.2
	Sequence conflict	588	1	E → D in BAA33501. Ref.2
	Sequence conflict	602	1	H → P in BAA33501. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q56YP2-1 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 8A9E7D10A32CBF53	FASTA	752	85,945
	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

References

	« Hide 'large scale' referencesShow '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: 9753781] [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. , 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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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 (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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: 11672432] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[6]	"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: 11489170] [Abstract] Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[7]	"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: 12226484] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF019380 mRNA. Translation: AAB82658.1. AB005902 mRNA. Translation: BAA33501.1. Frameshift. AC069252 Genomic DNA. Translation: AAF86542.1. Sequence problems. AK221279 mRNA. Translation: BAD93975.1.
IPI	IPI00533641.
PIR	T51821.
RefSeq	NP_173617.1.
UniGene	At.22532
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q56YP2.
Genome annotation databases
GeneID	838801.
GenomeReviews	Gene locus AT1G21980 in contig CT485782_GR.
KEGG	ath:AT1G21980.
NMPDR	fig|3702.1.peg.2558.
Organism-specific databases
GeneFarm	5099.
TAIR	At1g21980.
Phylogenomic databases
OMA	DLYIGSF.
Enzyme and pathway databases
BRENDA	2.7.1.68. 302.
Gene expression databases
Genevestigator	Q56YP2.
GermOnline	AT1G21980. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR003409. MORN. IPR017163. PIno-4-P-5_kinase_pln. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
PANTHER	PTHR23086. PIP5K. 1 hit.
Pfam	PF02493. MORN. 7 hits. PF01504. PIP5K. 1 hit. [Graphical view]
PIRSF	PIRSF037274. PIP5K_plant_prd. 1 hit.
SMART	SM00698. MORN. 7 hits. SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PI5K1_ARATH

Accession

Primary (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:	November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)