PI5K9_ARATH
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 03-AUG-2022, entry version 127.
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.AT3G09920.3; -.
DR iPTMnet; Q8L850; -.
DR PaxDb; Q8L850; -.
DR PRIDE; Q8L850; -.
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; locus:2085074; AT3G09920.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; Q8L850; -.
DR OMA; WIQGLGE; -.
DR OrthoDB; 209866at2759; -.
DR PhylomeDB; Q8L850; -.
DR BioCyc; ARA:AT3G09920-MON; -.
DR BRENDA; 2.7.1.68; 399.
DR PRO; PR:Q8L850; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L850; baseline and differential.
DR Genevisible; Q8L850; AT.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IMP:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 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; 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
