ID PI5KA_ARATH Reviewed; 427 AA. AC Q9LMN1; O23705; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 2. DT 27-MAR-2024, entry version 135. DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 10; DE Short=AtPIP5K10; DE EC=2.7.1.68; DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 10; DE AltName: Full=Diphosphoinositide kinase 10; DE AltName: Full=PtdIns(4)P-5-kinase 10; GN Name=PIP5K10; OrderedLocusNames=At1g01460; ORFNames=F22L4.2; 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 [GENOMIC DNA]. RX PubMed=9666060; DOI=10.1016/s0378-1119(98)00286-8; RA Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P., RA De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P., RA van Montagu M.; RT "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located RT at the top of chromosome 1."; RL Gene 215:11-17(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., RA Redman J.C., Wu H.C., Utterback T., Town C.D.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [5] 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 -!- SEQUENCE CAUTION: CC Sequence=AAF81306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; Y12776; CAA73312.1; -; Genomic_DNA. DR EMBL; AC061957; AAF81306.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE27290.1; -; Genomic_DNA. DR EMBL; DQ056443; AAY78600.1; -; mRNA. DR PIR; C86145; C86145. DR RefSeq; NP_171653.2; NM_100028.3. DR AlphaFoldDB; Q9LMN1; -. DR SMR; Q9LMN1; -. DR STRING; 3702.Q9LMN1; -. DR PaxDb; 3702-AT1G01460-1; -. DR ProteomicsDB; 234755; -. DR EnsemblPlants; AT1G01460.1; AT1G01460.1; AT1G01460. DR GeneID; 839469; -. DR Gramene; AT1G01460.1; AT1G01460.1; AT1G01460. DR KEGG; ath:AT1G01460; -. DR Araport; AT1G01460; -. DR TAIR; AT1G01460; PIPK11. DR eggNOG; KOG0229; Eukaryota. DR HOGENOM; CLU_004312_6_3_1; -. DR InParanoid; Q9LMN1; -. DR OMA; MFTREIT; -. DR OrthoDB; 340426at2759; -. DR PhylomeDB; Q9LMN1; -. DR BioCyc; ARA:AT1G01460-MONOMER; -. DR BRENDA; 2.7.1.68; 399. DR PRO; PR:Q9LMN1; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9LMN1; baseline and differential. DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1. DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1. 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:SF111; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 10; 1. DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1. DR Pfam; PF01504; PIP5K; 1. DR SMART; SM00330; PIPKc; 1. DR SUPFAM; SSF56104; SAICAR synthase-like; 1. DR PROSITE; PS51455; PIPK; 1. DR Genevisible; Q9LMN1; AT. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..427 FT /note="Phosphatidylinositol 4-phosphate 5-kinase 10" FT /id="PRO_0000185482" FT DOMAIN 1..419 FT /note="PIPK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781" FT REGION 247..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 334..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 379..400 FT /note="Activation loop" FT /evidence="ECO:0000250" SQ SEQUENCE 427 AA; 48549 MW; 87EDC9019FAFC28F CRC64; MFTREITAKD VKATEKNRIR YSSKHIKHLP PGTITEFEWK DYCPLGFRLI QELEDINHDE YMKSICNDET LRKLSTSKVG NMFLLSKDDR FLIKILRKSE IKVILEMLPG YFRHIHKYRS TLLSKNYGAH SVKPIGGVKT YFVVMSNILQ SDVFMNKVYD LKGSSQGRTN KKIKVRDKTI LKDIDLDFCF YVDSLARHRL IKQTKLDCEL LEDEGIMDYS LMLGLQVKGS CHGSIDELIP VYDSFTSRGS VDSNSSKFMK TASNSPDRSS STMYSCTPSR NSVDSENSVN IQSVASISPS PAQTNASDSP YESLVSKTNL TNIFQNSSST NFGMKIPGRA RRVGRGESGS VVGKQSREGG EEWYDVILYL GIIDIFQDYG VRKRLEHCYK SIQHSSKTIS AVHPKMYSSR FQDFVSQIFL PDEDPSH //