ID PI5K6_ARATH Reviewed; 715 AA. AC Q9SFB8; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 147. DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 6; DE Short=AtPIP5K6; DE EC=2.7.1.68; DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 6; DE AltName: Full=Diphosphoinositide kinase 6; DE AltName: Full=PtdIns(4)P-5-kinase 6; GN Name=PIP5K6; OrderedLocusNames=At3g07960; ORFNames=F17A17.30; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., 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., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., 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 thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA 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 phosphoinositide- RT specific phospholipase C."; RL Plant Physiol. 130:22-46(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4- CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC013483; AAF21206.1; -; Genomic_DNA. DR EMBL; CP002686; AEE74625.1; -; Genomic_DNA. DR EMBL; BT008595; AAP40421.1; -; mRNA. DR RefSeq; NP_187453.1; NM_111675.6. DR AlphaFoldDB; Q9SFB8; -. DR SMR; Q9SFB8; -. DR BioGRID; 5322; 1. DR STRING; 3702.Q9SFB8; -. DR iPTMnet; Q9SFB8; -. DR PaxDb; 3702-AT3G07960-1; -. DR ProteomicsDB; 234955; -. DR EnsemblPlants; AT3G07960.1; AT3G07960.1; AT3G07960. DR GeneID; 819987; -. DR Gramene; AT3G07960.1; AT3G07960.1; AT3G07960. DR KEGG; ath:AT3G07960; -. DR Araport; AT3G07960; -. DR TAIR; AT3G07960; PIP5K6. DR eggNOG; KOG0229; Eukaryota. DR HOGENOM; CLU_004312_6_4_1; -. DR InParanoid; Q9SFB8; -. DR OrthoDB; 340426at2759; -. DR PhylomeDB; Q9SFB8; -. DR BioCyc; ARA:AT3G07960-MONOMER; -. DR PRO; PR:Q9SFB8; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SFB8; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR. DR GO; GO:0090406; C:pollen tube; IDA:TAIR. DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:TAIR. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd17302; PIPKc_AtPIP5K_like; 1. DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1. DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3. DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1. DR InterPro; IPR003409; MORN. DR InterPro; IPR017163; PIno-4-P-5_kinase_pln. DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf. DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core. DR InterPro; IPR027484; PInositol-4-P-5-kinase_N. DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase. DR PANTHER; PTHR23086:SF113; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 6; 1. DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1. DR Pfam; PF02493; MORN; 7. DR Pfam; PF01504; PIP5K; 1. DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1. DR SMART; SM00698; MORN; 7. DR SMART; SM00330; PIPKc; 1. DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2. DR SUPFAM; SSF56104; SAICAR synthase-like; 1. DR PROSITE; PS51455; PIPK; 1. DR Genevisible; Q9SFB8; AT. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat; KW Transferase. FT CHAIN 1..715 FT /note="Phosphatidylinositol 4-phosphate 5-kinase 6" FT /id="PRO_0000185478" FT REPEAT 32..54 FT /note="MORN 1" FT REPEAT 55..77 FT /note="MORN 2" FT REPEAT 78..100 FT /note="MORN 3" FT REPEAT 101..123 FT /note="MORN 4" FT REPEAT 124..146 FT /note="MORN 5" FT REPEAT 147..169 FT /note="MORN 6" FT REPEAT 170..192 FT /note="MORN 7" FT REPEAT 193..214 FT /note="MORN 8" FT DOMAIN 321..711 FT /note="PIPK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 253..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..692 FT /note="Activation loop" FT /evidence="ECO:0000250" FT COMPBIAS 265..280 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 284..306 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 715 AA; 81422 MW; 795D86CEB1FB52E9 CRC64; MSVAHADDAD DYSRPTGESY HAEKALPSGD FYTGQWRDNL PHGHGKYLWT DGCMYVGDWH RGKTMGKGRF SWPSGATYEG DFKNGYMDGK GTYIDSSGDL YRGSWVMNLR HGQGTKSYVN GDCYDGEWRR GLQDGHGRYQ WKNENHYIGQ WKNGLMNGNG TMIWSNGNRY DGSWEDGAPK GNGTFRWSDG SFYVGVWSKD PKEQNGTYYP STSSGNFDWQ PQQVFYVDLS ECVVCTCQRI PVLPSQKMPV WYGASEQSSS GNRTKNSERP RRRSVDGRVS NGEMELRSNG SGYLQVDDNA ESTRSSLGPL RIQPAKKQGQ TISKGHKNYE LMLNLQLGIR HSVGRPAPAT SLDLKASAFD PKEKLWTKFP SEGSKYTPPH QSCEFKWKDY CPVVFRTLRK LFSVDAADYM LSICGNDALR ELSSPGKSGS FFYLTNDDRY MIKTMKKAET KVLIRMLPAY YNHVRACENT LVTKFFGLHC VKLTGTAQKK VRFVIMGNLF CTGHSIHRRF DLKGSSHGRL TTKPESEIDP NTTLKDLDLN FAFRLQKNWF QEFCRQVDRD CEFLEQERIM DYSLLVGLHF REAAIKDSAT PTSGARTPTG NSETRLSRAE MDRFLLDASK LASIKLGINM PARVERTARR SDCENQLVGD PTGEFYDVIV YFGIIDILQD YDISKKLEHA YKSMQYDPTS ISAVDPKQYS RRFRDFIFRV FVEDA //