ID   PI5K4_ARATH             Reviewed;         779 AA.
AC   Q9M1K2;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 4;
DE            Short=AtPIP5K4;
DE            EC=2.7.1.68;
DE   AltName: Full=1-phosphatidylinositol 4-phosphate kinase 4;
DE   AltName: Full=Diphosphoinositide kinase 4;
DE   AltName: Full=PtdIns(4)P-5-kinase 4;
GN   Name=PIP5K4; OrderedLocusNames=At3g56960; ORFNames=F24I3.40;
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   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;
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DR   EMBL; AL138655; CAB72166.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79593.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63864.1; -; Genomic_DNA.
DR   PIR; T47756; T47756.
DR   RefSeq; NP_001319773.1; NM_001339834.1.
DR   RefSeq; NP_191255.1; NM_115555.2.
DR   AlphaFoldDB; Q9M1K2; -.
DR   SMR; Q9M1K2; -.
DR   BioGRID; 10179; 2.
DR   STRING; 3702.Q9M1K2; -.
DR   iPTMnet; Q9M1K2; -.
DR   PaxDb; 3702-AT3G56960-1; -.
DR   ProteomicsDB; 236736; -.
DR   EnsemblPlants; AT3G56960.1; AT3G56960.1; AT3G56960.
DR   EnsemblPlants; AT3G56960.2; AT3G56960.2; AT3G56960.
DR   GeneID; 824863; -.
DR   Gramene; AT3G56960.1; AT3G56960.1; AT3G56960.
DR   Gramene; AT3G56960.2; AT3G56960.2; AT3G56960.
DR   KEGG; ath:AT3G56960; -.
DR   Araport; AT3G56960; -.
DR   TAIR; AT3G56960; PIP5K4.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   InParanoid; Q9M1K2; -.
DR   OMA; EENLEWD; -.
DR   OrthoDB; 340426at2759; -.
DR   PhylomeDB; Q9M1K2; -.
DR   BioCyc; ARA:AT3G56960-MONOMER; -.
DR   PRO; PR:Q9M1K2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1K2; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C: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:0006897; P:endocytosis; IMP:TAIR.
DR   GO; GO:0007164; P:establishment of tissue polarity; IMP:TAIR.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR   GO; GO:0009846; P:pollen germination; IGI:TAIR.
DR   GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR   GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR   CDD; cd17302; PIPKc_AtPIP5K_like; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 2.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 4.
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:SF29; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 4; 1.
DR   PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR   Pfam; PF02493; MORN; 8.
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; Q9M1K2; AT.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Transferase.
FT   CHAIN           1..779
FT                   /note="Phosphatidylinositol 4-phosphate 5-kinase 4"
FT                   /id="PRO_0000185476"
FT   REPEAT          77..99
FT                   /note="MORN 1"
FT   REPEAT          100..122
FT                   /note="MORN 2"
FT   REPEAT          123..145
FT                   /note="MORN 3"
FT   REPEAT          146..168
FT                   /note="MORN 4"
FT   REPEAT          169..191
FT                   /note="MORN 5"
FT   REPEAT          192..214
FT                   /note="MORN 6"
FT   REPEAT          215..237
FT                   /note="MORN 7"
FT   REPEAT          238..259
FT                   /note="MORN 8"
FT   DOMAIN          382..775
FT                   /note="PIPK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT   REGION          20..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..756
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        21..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  89238 MW;  FAEB3BF1603C18B0 CRC64;
     MSKEQSCVLK AWEVTVRKTQ QAKKRANSIF GTVSVAPQTD DDATTTTEEN DDETSTNRSS
     IGELYHAERI LPNGDYYTGQ WYDSFPHGHG KYLWTDGCMY IGDWYNGKTM GRGKFGWPSG
     ATYEGEFKSG YMDGVGLYTG PSGDTYKGQW VMNLKHGHGI KRFANGDVYD GEWRRGLQEA
     QGKYQWRDGS YYMGEWKNAT ICGKGTFIWT DGNRYDGFWD DGFPRGNGTF KWADGSFYVG
     HWSNDPEEMN GTYYPSGDDG SPEWDPKDVF TNLSEYKICS GERVPVLPSQ KKLSVWNSSK
     RVEKPRRMSV DGRVSVGVDR AFEKMNMWGT ESGEGAADID STTRRDLDAE MMRLEAEGFI
     QSLRPSPAPM RLPRAGRKQG ETISKGHRNY ELMLNLQLGI RHAVGKQAPV VSLDLKHSAF
     DPKEKVWTRF PPEGTKYTPP HQSSEFKWKD YCPLVFRSLR KLFKVDPADY MLSICGNDAL
     RELSSPGKSG SFFYLTNDDR YMIKTMKKSE TKVLLRMLAA YYNHVRAFEN TLVIRFYGLH
     CVKLTGPIQK KVRFVIMGNL FCSEYSIHRR FDLKGSSLGR TTDKPESEIN SNTILKDLDL
     NFIFRLQKAW YQEFIRQVDK DCEFLEQERI MDYSLLVGIH FREASVAGEL IPSGARTPIG
     EFEDESAPRL SRADVDQLLS DPTRWASIRL GGNMPARAER TMRRSDCEFQ LVGEPTGEYY
     EVVMIFGIID ILQDYDISKK LEHAYKSIQY DPTSISAVDP RLYSRRFRDF IFKVFTEDN
//