ID   PI5K9_ARATH             Reviewed;         815 AA.
AC   Q8L850; Q0WMK5; Q9SF93;
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 9;
DE            Short=AtPIP5K9;
DE            EC=2.7.1.68;
DE   AltName: Full=1-phosphatidylinositol 4-phosphate kinase 9;
DE   AltName: Full=Diphosphoinositide kinase 9;
DE   AltName: Full=PtdIns(4)P-5-kinase 9;
GN   Name=PIP5K9; OrderedLocusNames=At3g09920; ORFNames=F8A24.2;
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 [MRNA].
RA   Lou Y.;
RT   "Arabidopsis thaliana putative phosphatidylinositol-4-phosphate 5-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   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   [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;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
RN   [7]
RP   FUNCTION, INTERACTION WITH CINV1, TISSUE SPECIFICITY, AND INDUCTION BY
RP   COLD.
RC   STRAIN=cv. Columbia;
RX   PubMed=17220200; DOI=10.1105/tpc.106.045658;
RA   Lou Y., Gou J.Y., Xue H.W.;
RT   "PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase,
RT   interacts with a cytosolic invertase to negatively regulate sugar-mediated
RT   root growth.";
RL   Plant Cell 19:163-181(2007).
CC   -!- FUNCTION: Plays a role in sugar-mediated root development. Interaction
CC       with CINV1 induces repression of CINV1 activity and negative regulation
CC       of sugar-mediated root cell elongation. {ECO:0000269|PubMed:17220200}.
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   -!- SUBUNIT: Interacts with CINV1. {ECO:0000269|PubMed:17220200}.
CC   -!- INTERACTION:
CC       Q8L850; Q9LQF2: CINV1; NbExp=6; IntAct=EBI-2008013, EBI-2008033;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}. Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17220200}.
CC   -!- INDUCTION: Transiently down-regulated by cold.
CC       {ECO:0000269|PubMed:17220200}.
CC   -!- MISCELLANEOUS: The gain-of-function mutant pip5k9-d (T-DNA insertion
CC       line) has reduced primary root length. {ECO:0000305|PubMed:17220200}.
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DR   EMBL; AJ810853; CAH18644.1; -; mRNA.
DR   EMBL; AC015985; AAF23244.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74832.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74833.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74834.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65698.1; -; Genomic_DNA.
DR   EMBL; AY120742; AAM53300.1; -; mRNA.
DR   EMBL; AK229815; BAF01646.1; -; mRNA.
DR   RefSeq; NP_001030666.1; NM_001035589.3.
DR   RefSeq; NP_001189852.1; NM_001202923.1.
DR   RefSeq; NP_001327647.1; NM_001337850.1.
DR   RefSeq; NP_187603.1; NM_111827.3.
DR   AlphaFoldDB; Q8L850; -.
DR   SMR; Q8L850; -.
DR   BioGRID; 5485; 1.
DR   IntAct; Q8L850; 1.
DR   STRING; 3702.Q8L850; -.
DR   iPTMnet; Q8L850; -.
DR   PaxDb; 3702-AT3G09920-3; -.
DR   ProteomicsDB; 234754; -.
DR   EnsemblPlants; AT3G09920.1; AT3G09920.1; AT3G09920.
DR   EnsemblPlants; AT3G09920.2; AT3G09920.2; AT3G09920.
DR   EnsemblPlants; AT3G09920.3; AT3G09920.3; AT3G09920.
DR   EnsemblPlants; AT3G09920.4; AT3G09920.4; AT3G09920.
DR   GeneID; 820151; -.
DR   Gramene; AT3G09920.1; AT3G09920.1; AT3G09920.
DR   Gramene; AT3G09920.2; AT3G09920.2; AT3G09920.
DR   Gramene; AT3G09920.3; AT3G09920.3; AT3G09920.
DR   Gramene; AT3G09920.4; AT3G09920.4; AT3G09920.
DR   KEGG; ath:AT3G09920; -.
DR   Araport; AT3G09920; -.
DR   TAIR; AT3G09920; PIP5K9.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   InParanoid; Q8L850; -.
DR   OMA; PPHEMAG; -.
DR   OrthoDB; 340426at2759; -.
DR   PhylomeDB; Q8L850; -.
DR   BioCyc; ARA:AT3G09920-MONOMER; -.
DR   BRENDA; 2.7.1.68; 399.
DR   PRO; PR:Q8L850; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8L850; baseline and differential.
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 activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; 2.
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:SF8; PHOSPHATIDYLINOSITOL 5-PHOSPHATE 4-KINASE, ISOFORM A; 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; 8.
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; Q8L850; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..815
FT                   /note="Phosphatidylinositol 4-phosphate 5-kinase 9"
FT                   /id="PRO_0000185481"
FT   REPEAT          58..80
FT                   /note="MORN 1"
FT   REPEAT          81..103
FT                   /note="MORN 2"
FT   REPEAT          104..126
FT                   /note="MORN 3"
FT   REPEAT          127..149
FT                   /note="MORN 4"
FT   REPEAT          150..172
FT                   /note="MORN 5"
FT   REPEAT          173..195
FT                   /note="MORN 6"
FT   REPEAT          196..218
FT                   /note="MORN 7"
FT   REPEAT          219..240
FT                   /note="MORN 8"
FT   DOMAIN          391..809
FT                   /note="PIPK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT   REGION          769..790
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        482
FT                   /note="N -> K (in Ref. 4; AAM53300)"
FT                   /evidence="ECO:0000305"
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
//