Q9SUI2 (PI5K7_ARATH) Reviewed, UniProtKB/Swiss-Prot

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
Diphosphoinositide kinase 7
Short name=AtP5K2
PtdIns(4)P-5-kinase 7

Gene names

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

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	754 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	plasma membrane Inferred from direct assay PubMed 17317660. 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.6

Sequences

	Sequence		Length	Mass (Da)
	Q9SUI2 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"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.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ009782 mRNA. Translation: CAB53377.1. U95973 Genomic DNA. Translation: AAB65487.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28661.1. AY062718 mRNA. Translation: AAL32796.1. BT010342 mRNA. Translation: AAQ56785.1.
IPI	IPI00517052.
PIR	G86242.
RefSeq	NP_172559.2. NM_100965.4.
UniGene	At.485.
3D structure databases
ProteinModelPortal	Q9SUI2.
SMR	Q9SUI2. Positions 339-579.
ModBase	Search...
Proteomic databases
PaxDb	Q9SUI2.
PRIDE	Q9SUI2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G10900.1; AT1G10900.1; AT1G10900.
GeneID	837633.
KEGG	ath:AT1G10900.
Organism-specific databases
GeneFarm	5100.
TAIR	At1g10900.
Phylogenomic databases
eggNOG	COG4642.
HOGENOM	HOG000193875.
InParanoid	Q9SUI2.
KO	K00889.
OMA	DHENTLI.
PhylomeDB	Q9SUI2.
ProtClustDB	CLSN2690395.
Gene expression databases
Genevestigator	Q9SUI2.
GermOnline	AT1G10900. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.30.800.10. 1 hit. 3.30.810.10. 2 hits.
InterPro	IPR003409. 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]
PANTHER	PTHR23086. PTHR23086. 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:	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