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Phosphatidylinositol 4-kinase beta 1 (PI4-kinase beta 1) (PtdIns-4-kinase beta 1) (EC 2.7.1.67) (Phosphatidylinositol 4-OH kinase beta1) (AtPI4Kbeta1) (PI-4Kbeta1)

 P4KB1_ARATH             Reviewed;        1121 AA.
Q9FMJ0; Q9ZPE1;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-JUL-2017, entry version 127.
RecName: Full=Phosphatidylinositol 4-kinase beta 1;
Short=PI4-kinase beta 1;
Short=PtdIns-4-kinase beta 1;
EC=2.7.1.67;
AltName: Full=Phosphatidylinositol 4-OH kinase beta1;
Short=AtPI4Kbeta1;
Short=PI-4Kbeta1;
Name=PI4KB1; Synonyms=PI4K, PI4KBETA1; OrderedLocusNames=At5g64070;
ORFNames=MHJ24.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, REPEATS, ENZYME
REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Hypocotyl;
PubMed=10026194; DOI=10.1074/jbc.274.9.5738;
Xue H.-W., Pical C., Brearley C., Elge S., Mueller-Roeber B.;
"A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat
structure. Cloning and functional expression in baculovirus-infected
insect cells.";
J. Biol. Chem. 274:5738-5745(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12226484; DOI=10.1104/pp.004770;
Mueller-Roeber B., Pical C.;
"Inositol phospholipid metabolism in Arabidopsis. Characterized and
putative isoforms of inositol phospholipid kinase and
phosphoinositide-specific phospholipase C.";
Plant Physiol. 130:22-46(2002).
[6]
ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=12805633; DOI=10.1104/pp.103.021758;
Stevenson-Paulik J., Love J., Boss W.F.;
"Differential regulation of two Arabidopsis type III
phosphatidylinositol 4-kinase isoforms. A regulatory role for the
pleckstrin homology domain.";
Plant Physiol. 132:1053-1064(2003).
[7]
INTERACTION WITH RABA4B AND CBL1, FUNCTION, DISRUPTION PHENOTYPE, AND
SUBCELLULAR LOCATION.
PubMed=16567499; DOI=10.1083/jcb.200508116;
Preuss M.L., Schmitz A.J., Thole J.M., Bonner H.K.S., Otegui M.S.,
Nielsen E.;
"A role for the RabA4b effector protein PI-4Kbeta1 in polarized
expansion of root hair cells in Arabidopsis thaliana.";
J. Cell Biol. 172:991-998(2006).
[8]
SUBCELLULAR LOCATION.
PubMed=16649109; DOI=10.1007/s11103-005-5548-x;
Lou Y., Ma H., Lin W.H., Chu Z.Q., Mueller-Roeber B., Xu Z.H.,
Xue H.W.;
"The highly charged region of plant beta-type phosphatidylinositol 4-
kinase is involved in membrane targeting and phospholipid binding.";
Plant Mol. Biol. 60:729-746(2006).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-449 AND SER-454, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[10]
INTERACTION WITH AHK2.
PubMed=18642946; DOI=10.1021/pr0703831;
Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T.,
Heyl A.;
"Toward an interaction map of the two-component signaling pathway of
Arabidopsis thaliana.";
J. Proteome Res. 7:3649-3660(2008).
[11]
INTERACTION WITH RABA4D, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19208902; DOI=10.1105/tpc.108.060277;
Szumlanski A.L., Nielsen E.;
"The Rab GTPase RabA4d regulates pollen tube tip growth in Arabidopsis
thaliana.";
Plant Cell 21:526-544(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[13]
FUNCTION, AND MUTAGENESIS OF LYS-864.
PubMed=20603382; DOI=10.1093/mp/ssq031;
Ischebeck T., Vu L.H., Jin X., Stenzel I., Loefke C., Heilmann I.;
"Functional cooperativity of enzymes of phosphoinositide conversion
according to synergistic effects on pectin secretion in tobacco pollen
tubes.";
Mol. Plant 3:870-881(2010).
[14] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21134079; DOI=10.1111/j.1600-0854.2010.01146.x;
Kang B.H., Nielsen E., Preuss M.L., Mastronarde D., Staehelin L.A.;
"Electron tomography of RabA4b- and PI-4Kbeta1-labeled trans Golgi
network compartments in Arabidopsis.";
Traffic 12:313-329(2011).
[15]
FUNCTION.
PubMed=22318862; DOI=10.1093/pcp/pcs011;
Delage E., Ruelland E., Guillas I., Zachowski A., Puyaubert J.;
"Arabidopsis type-III phosphatidylinositol 4-kinases ?1 and ?2 are
upstream of the phospholipase C pathway triggered by cold exposure.";
Plant Cell Physiol. 53:565-576(2012).
[16]
REVIEW.
PubMed=22899063; DOI=10.4161/psb.21305;
Delage E., Ruelland E., Zachowski A., Puyaubert J.;
"Eat in or take away? How phosphatidylinositol 4-kinases feed the
phospholipase C pathway with substrate.";
Plant Signal. Behav. 7:1197-1199(2012).
-!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first
committed step in the production of the second messenger inositol-
1,4,5-trisphosphate. Necessary for proper organization of the
trans-Golgi network (TGN) and post-Golgi secretion in root hairs.
Together with PI4KB2, required during polarized root hair
expansion and pollen tube elongation. Functions redundantly with
PI4KB2 upstream of the cold response phosphoinositide-dependent
phospholipase C (PI-PLC) pathway. {ECO:0000269|PubMed:10026194,
ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:19208902,
ECO:0000269|PubMed:20603382, ECO:0000269|PubMed:21134079,
ECO:0000269|PubMed:22318862}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
1-phosphatidyl-1D-myo-inositol 4-phosphate.
-!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4-phosphate
(PtdIns4P). Slightly repressed by phosphatidyl-choline (PtdCho),
wortmannin and adenosine. {ECO:0000269|PubMed:10026194,
ECO:0000269|PubMed:12805633}.
-!- SUBUNIT: Interacts with AHK2, CBL1 and RABA4D.
{ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:18642946,
ECO:0000269|PubMed:19208902}.
-!- INTERACTION:
Q9C5U2:AHK2; NbExp=2; IntAct=EBI-1807432, EBI-1100634;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16649109,
ECO:0000269|PubMed:21134079}. Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:21134079}.
Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12805633};
Peripheral membrane protein {ECO:0000269|PubMed:12805633};
Cytoplasmic side {ECO:0000269|PubMed:12805633,
ECO:0000269|PubMed:18433157}. Note=Associated to tip-localized
membranes in growing root hairs. {ECO:0000269|PubMed:16567499}.
-!- TISSUE SPECIFICITY: Expressed constitutively in leaves, roots,
flowers, and stems. {ECO:0000269|PubMed:10026194}.
-!- DOMAIN: The PPC (Plant PI4K Charged) region is involved in
membrane targeting and phospholipid binding.
{ECO:0000269|PubMed:16649109}.
-!- DISRUPTION PHENOTYPE: When associated with PI4KB2 disruption:
aberrant root hair morphologies, and short and wavy pollen tubes.
{ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:19208902}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ002685; CAB37928.1; -; Genomic_DNA.
EMBL; AB008266; BAB10275.1; -; Genomic_DNA.
EMBL; CP002688; AED97836.1; -; Genomic_DNA.
EMBL; AF462854; AAL58940.1; -; mRNA.
EMBL; AY139795; AAM98101.1; -; mRNA.
PIR; T52631; T52631.
RefSeq; NP_201212.1; NM_125803.4.
UniGene; At.28255; -.
ProteinModelPortal; Q9FMJ0; -.
SMR; Q9FMJ0; -.
BioGrid; 21770; 4.
IntAct; Q9FMJ0; 1.
STRING; 3702.AT5G64070.1; -.
iPTMnet; Q9FMJ0; -.
PaxDb; Q9FMJ0; -.
EnsemblPlants; AT5G64070.1; AT5G64070.1; AT5G64070.
GeneID; 836528; -.
Gramene; AT5G64070.1; AT5G64070.1; AT5G64070.
KEGG; ath:AT5G64070; -.
Araport; AT5G64070; -.
TAIR; locus:2164401; AT5G64070.
eggNOG; KOG0903; Eukaryota.
eggNOG; ENOG410XPH3; LUCA.
HOGENOM; HOG000265626; -.
InParanoid; Q9FMJ0; -.
KO; K19801; -.
OMA; HIPEDEC; -.
OrthoDB; EOG093600Z8; -.
PhylomeDB; Q9FMJ0; -.
BioCyc; ARA:AT5G64070-MONOMER; -.
Reactome; R-ATH-1660514; Synthesis of PIPs at the Golgi membrane.
PRO; PR:Q9FMJ0; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9FMJ0; AT.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0035619; C:root hair tip; IDA:TAIR.
GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
GO; GO:0048768; P:root hair cell tip growth; IGI:TAIR.
Gene3D; 1.10.1070.11; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle;
Developmental protein; Golgi apparatus; Kinase; Membrane;
Phosphoprotein; Reference proteome; Repeat; Transferase.
CHAIN 1 1121 Phosphatidylinositol 4-kinase beta 1.
/FTId=PRO_0000398594.
DOMAIN 1 143 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
REPEAT 212 231 1. {ECO:0000269|PubMed:10026194}.
REPEAT 244 263 2. {ECO:0000269|PubMed:10026194}.
REPEAT 266 285 3. {ECO:0000269|PubMed:10026194}.
REPEAT 288 306 4. {ECO:0000269|PubMed:10026194}.
REPEAT 309 328 5. {ECO:0000269|PubMed:10026194}.
REPEAT 331 350 6. {ECO:0000269|PubMed:10026194}.
REPEAT 353 372 7. {ECO:0000269|PubMed:10026194}.
REPEAT 380 398 8. {ECO:0000269|PubMed:10026194}.
REPEAT 420 438 9. {ECO:0000269|PubMed:10026194}.
REPEAT 454 472 10. {ECO:0000269|PubMed:10026194}.
REPEAT 489 508 11. {ECO:0000269|PubMed:10026194}.
DOMAIN 859 1121 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
REGION 212 508 11 X 20 AA approximate repeats (PPC).
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MUTAGEN 864 864 K->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:20603382}.
CONFLICT 116 117 VH -> AS (in Ref. 1; CAB37928).
{ECO:0000305}.
SEQUENCE 1121 AA; 126375 MW; 686C994E431BBDB2 CRC64;
MPMGRFLSLV RGDSAESPRE ITSQSNIIGD TGSNGWLIRF FDSAFFCEWI AVSYLYKHPH
AGVRDYLCNR MYTLPLSGIE SYLFQICYMM VHKPSPSLDK FVIDICGKSL KIALKVHWFL
LAELEDADDN EGISRIQEKC QIAATLMGEW SPLMRPQNEV STPGSKNQVL NRLLSSKQKL
FSLKLSPPTQ KSLSFSPSPG TNVQDDGSQL PAEDNKIFKK LIPSPKVRDA LMFRKSADKD
DEESEKEGFF KRLLRDSKGE GDEPIPNSEG FFKRLLKDNK SEDEDITNSS EGFFKRLLSS
KGESEELTSS SDGLFKRLLR DNKGDEEELG ANSDSFFKRL LRESKNEDEE SNPNSEGFFK
KLFRDSKPED DKVPKEVDDE DKDGFLKKLF REKNDDKRHG SEKNEANGTV YADKKSGEED
EREGFFKKFF KEKSDDKKDI VKVDDGNESE GDESPEFSLF KRLFRIHPED AKPTSENENS
SNGLVESSPG TENFFRKLFR DRDQSVEDSE LFGSKKHKEK RPGSPKQRDD TPSGKPPLPN
NTASQFRKGA YHESLEFVQA LCETSYGLVD IFPIEDRKIG LRESLAEINF HLSEAEITGG
ICFPMGRGVF RVVHIPEDEC ILLNSREKAP YMISVEVLKA ETPSAKESSN SQKLSKGGIP
LANGDAFLQK PPPWAYPLWT TQEVYRNSAD RMSLSTAQAI DQAMTPKSEV KVKLVNVSLS
VEDRTSALES FGDPIDDVLG EAPRTGLNND LEWVRVVVTA DPGLRMESIP DPSVPRKKEH
RRVPSTVAME EVRAAAAKGE APPGLPLKGA GQDSSDAQPR ANGGMLKEGD ALSGELWEGK
RDRIRKASIY GKLPGWDLRS IIVKSGDDCR QEHLAVQLIS HFYDIFQEAG LPLWLRPYEV
LVTSSYTALI ETIPDTASIH SIKSRYPNIT SLRDFFVAKY KENSPSFKLA QRNFVESMAG
YSLVCYLLQV KDRHNGNLLL DEEGHIIHID FGFMLSNSPG GVNFESAPFK LTRELLEVMD
SDADGVPSEF FDYFKVLCIQ GFLTCRKHAE RIILLVEMLQ DSGFPCFKGG PRTIQNLRKR
FHLSLTEEQC VSLVLSLISS SLDAWRTRQY DYYQRVLNGI L


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