ID PI5K9_ARATH Reviewed; 815 AA. AC Q8L850; Q9SF93; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 2. DT 07-JUL-2009, entry version 44. DE RecName: Full=Phosphatidylinositol-4-phosphate 5-kinase 9; DE Short=AtPIP5K9; DE EC=2.7.1.68; DE AltName: Full=1-phosphatidylinositol-4-phosphate kinase 9; DE AltName: Full=PtdIns(4)P-5-kinase 9; DE AltName: Full=Diphosphoinositide kinase 9; GN Name=PIP5K9; OrderedLocusNames=At3g09920; ORFNames=F8A24.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lou Y.; RT "Arabidopsis thaliana putative phosphatidylinositol-4-phosphate 5- RT kinase."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12226484; DOI=10.1104/pp.004770; RA Mueller-Roeber B., Pical C.; RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and RT putative isoforms of inositol phospholipid kinase and RT phosphoinositide-specific phospholipase C."; RL Plant Physiol. 130:22-46(2002). CC -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4- CC phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. CC -!- INTERACTION: CC Q9LQF2:At1g35580; NbExp=4; IntAct=EBI-2008013, EBI-2008033; CC -!- SIMILARITY: Contains 8 MORN repeats. CC -!- SIMILARITY: Contains 1 PIPK domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ810853; CAH18644.1; -; mRNA. DR EMBL; AC015985; AAF23244.1; -; Genomic_DNA. DR EMBL; AY120742; AAM53300.1; -; mRNA. DR IPI; IPI00523155; -. DR RefSeq; NP_001030666.1; -. DR RefSeq; NP_187603.1; -. DR UniGene; At.40019; -. DR HSSP; P78356; 1BO1. DR IntAct; Q8L850; 1. DR GeneID; 820151; -. DR GenomeReviews; BA000014_GR; AT3G09920. DR KEGG; ath:AT3G09920; -. DR NMPDR; fig|3702.1.peg.13012; -. DR TAIR; At3g09920; -. DR OMA; Q8L850; RRWSLEV. DR BRENDA; 2.7.1.68; 302. DR GermOnline; AT3G09920; Arabidopsis thaliana. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase...; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006520; P:amino acid metabolic process; IMP:TAIR. DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro. DR InterPro; IPR003409; MORN. DR InterPro; IPR017163; PIno-4-P-5_kinase_pln. DR InterPro; IPR002498; PInositol-4-P-5-kinase_core. DR InterPro; IPR016034; PInositol-4P-5-kinase_core_sub. DR PANTHER; PTHR23086; PIP5K; 1. DR Pfam; PF02493; MORN; 8. DR Pfam; PF01504; PIP5K; 1. DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1. DR SMART; SM00698; MORN; 8. DR SMART; SM00330; PIPKc; 1. DR PROSITE; PS51455; PIPK; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Repeat; KW Transferase. FT CHAIN 1 815 Phosphatidylinositol-4-phosphate 5-kinase FT 9. FT /FTId=PRO_0000185481. FT REPEAT 58 80 MORN 1. FT REPEAT 81 103 MORN 2. FT REPEAT 104 126 MORN 3. FT REPEAT 127 149 MORN 4. FT REPEAT 150 172 MORN 5. FT REPEAT 173 195 MORN 6. FT REPEAT 196 218 MORN 7. FT REPEAT 219 240 MORN 8. FT DOMAIN 391 809 PIPK. FT REGION 769 790 Activation loop (By similarity). FT CONFLICT 482 482 N -> K (in Ref. 3; AAM53300). SQ SEQUENCE 815 AA; 92092 MW; 3194F009D2C50130 CRC64; MSGLDVRGAV SFAERTKSVD ALTKKEILSA LNSGEVSETS EDARFRVREL VLPDGESYSG SLLGNVPEGP GKYIWSDGCV YDGEWRRGMR HGIGNMRWAS GASYDGEFSG GYMHGSGTYV DANKLTYKGR WRLNLKHGLG YQVYPNGDVF EGSWIQGLGE GPGKYTWANK NVYLGDMKGG KMSGKGTLTW VTGDSYEGSW LNGMMHGVGV YTWSDGGCYV GTWTRGLKDG KGSFYSAGTR VPVVQEFYLN ALRKRGVLPD MRRQNQVASS VNMENLRVGV NRNKLSKGSL INLEQSRNGR VSLERRWSLE VSIEKVIGHG YSDLSTAVLD SGSSVQYKAN IPILEREYMQ GVLISELVVN NGFSRTSRRA KRKHKRLVKE AKKPGEVVIK GHRSYDLMLS LQLGIRYTVG KITPIQRRQV RTADFGPRAS FWMTFPRAGS TMTPPHHSED FKWKDYCPMV FRNLREMFKI DAADYMMSIC GNDTLRELSS PGKSGSVFFL SQDDRFMIKT LRKSEVKVLL RMLPDYHHHV KTYENTLITK FFGLHRIKPS SGQKFRFVVM GNMFFTDLRI HRRFDLKGSS LGRSADKVEI DENTILKDLD LNYSFFLETS WREGLLRQLE IDSKFLEAQN IMDYSLLLGV HHRAPQHLRS QLVRSQSITT DALESVAEDD TIEDDMLSYH EGLVLVPRGS ENTVTGPHIR GSRLRASAVG DEEVDLLLPG TARLQIQQGV NMPARAELIP GREDKEKQIL HDCCDVVLYL GIIDILQEYN MTKKIEHAYK SLHFDSLSIS AVDPTFYSQR FLEFIKKVFP QNNKS //