Reviewed, UniProtKB/Swiss-Prot Q9SUI2 (PI5K7_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-4-phosphate 5-kinase 7
      Short name=AtPIP5K7
    EC=2.7.1.68
Alternative name(s):
    1-phosphatidylinositol-4-phosphate kinase 7
    PtdIns(4)P-5-kinase 7
    Diphosphoinositide kinase 7
      Short name=AtP5K2

Gene names

Name:	PIP5K7
Synonyms:	P5K2
Ordered Locus Names:	At1g10900
ORF Names:	T19D16.18

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

General annotation (Comments)

Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Sequence similarities	Contains 8 MORN repeats. Contains 1 PIPK domain.
Sequence caution	The sequence AAB65487.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
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
Cellular component	plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from electronic annotation. Source: EC ATP binding 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 – 754	754	Phosphatidylinositol-4-phosphate 5-kinase 7		PRO_0000185479
Regions
	Repeat	16 – 38	23	MORN 1
	Repeat	39 – 61	23	MORN 2
	Repeat	62 – 84	23	MORN 3
	Repeat	85 – 107	23	MORN 4
	Repeat	108 – 130	23	MORN 5
	Repeat	131 – 153	23	MORN 6
	Repeat	154 – 176	23	MORN 7
	Repeat	177 – 198	22	MORN 8
	Domain	329 – 750	422	PIPK
	Region	710 – 731	22	Activation loop By similarity
Amino acid modifications
	Modified residue	224	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9SUI2-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D2310E6AABBA4F00	FASTA	754	85,955
	10 20 30 40 50 60 MDMRSGDREF PNGDFYSGEV KGIIPNGKGK YAWSDGTIYE GDWDEGKISG KGKLIWSSGA 70 80 90 100 110 120 KYEGDFSGGY LHGFGTMTSP DESVYSGAWR MNVRHGLGRK EYCNSDLYDG LWKEGLQDGR 130 140 150 160 170 180 GSYSWTNGNR YIGNWKKGKM CERGVMRWEN GDLYDGFWLN GFRHGSGVYK FADGCLYYGT 190 200 210 220 230 240 WSRGLKDGKG VFYPAGTKQP SLKKWCRSLE YDDTGKFVLS RSASVNVEEL RSLNTVTQSL 250 260 270 280 290 300 SVKTSAGETT CDPPRDFTCH GPVSKSARFS GSGQSEGQDK NRIVYEREYM QGVLIRETIM 310 320 330 340 350 360 SSVDRSHKIK PPNRPREVRA RSLMTFLRGE HNYYLMLNLQ LGIRYTVGKI TPVPRREVRA 370 380 390 400 410 420 SDFGKNARTK MFFPRDGSNF TPPHKSVDFS WKDYCPMVFR NLRQMFKLDA AEYMMSICGD 430 440 450 460 470 480 DGLTEISSPG KSGSIFYLSH DDRFVIKTLK KSELQVLLRM LPKYYEHVGD HENTLITKFF 490 500 510 520 530 540 GVHRITLKWG KKVRFVVMGN MFCTELKIHR RYDLKGSTQG RFTEKIKIQE KTTLKDLDLA 550 560 570 580 590 600 YEFHMDKLLR EALFKQIYLD CSFLESLNII DYSLLLGLHF RAPGQLNDIL EPPNAMSDQE 610 620 630 640 650 660 SVSSVDVGLT QEHSIPPKGL LLVTHEPNSV NTAPGPHIRG STLRAFSVGE QEVDLILPGT 670 680 690 700 710 720 ARLRVQLGVN MPAQAHHKLI EDKEESATIE LFEVYDVVVY MGIIDILQEY NTKKKVEHTC 730 740 750 KSLQYDPMTI SVTEPSTYSK RFVNFLHKVF PEER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular aspects of AtP5K2 in stomatal guard cells a phosphatidyinositol-4-phosphate 5-kinase." Elge S., Mueller-Roeber B. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[2]	"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.
[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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ009782 mRNA. Translation: CAB53377.1. U95973 Genomic DNA. Translation: AAB65487.1. Sequence problems. AY062718 mRNA. Translation: AAL32796.1. BT010342 mRNA. Translation: AAQ56785.1.
IPI	IPI00517052.
PIR	G86242.
RefSeq	NP_172559.2.
UniGene	At.485
3D structure databases
HSSP	HSSP built from PDB template 1BO1 based on UniProtKB P78356.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SUI2.
Proteomic databases
PRIDE	Q9SUI2.
Genome annotation databases
GeneID	837633.
GenomeReviews	Gene locus AT1G10900 in contig CT485782_GR.
KEGG	ath:AT1G10900.
NMPDR	fig|3702.1.peg.1339.
Organism-specific databases
GeneFarm	5100.
TAIR	At1g10900.
Phylogenomic databases
OMA	EYMMSIC.
Enzyme and pathway databases
BRENDA	2.7.1.68. 302.
Gene expression databases
Genevestigator	Q9SUI2.
GermOnline	AT1G10900. 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. 8 hits. PF01504. PIP5K. 1 hit. [Graphical view]
PIRSF	PIRSF037274. PIP5K_plant_prd. 1 hit.
SMART	SM00698. MORN. 8 hits. SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PI5K7_ARATH

Accession

Primary (citable) accession number: Q9SUI2
Secondary accession number(s): O04095

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)