P4KB2_ARATH
ID P4KB2_ARATH Reviewed; 1116 AA.
AC Q0WPX9; Q9FY80;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphatidylinositol 4-kinase beta 2;
DE Short=PI4-kinase beta 2;
DE Short=PtdIns-4-kinase beta 2;
DE EC=2.7.1.67;
DE AltName: Full=Phosphatidylinositol 4-OH kinase beta2;
DE Short=AtPI4Kbeta2;
DE Short=PI-4Kbeta2;
GN Name=PI4KB2; Synonyms=PI4KBETA2; OrderedLocusNames=At5g09350;
GN ORFNames=T5E8.150;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16567499; DOI=10.1083/jcb.200508116;
RA Preuss M.L., Schmitz A.J., Thole J.M., Bonner H.K.S., Otegui M.S.,
RA Nielsen E.;
RT "A role for the RabA4b effector protein PI-4Kbeta1 in polarized expansion
RT of root hair cells in Arabidopsis thaliana.";
RL J. Cell Biol. 172:991-998(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19208902; DOI=10.1105/tpc.108.060277;
RA Szumlanski A.L., Nielsen E.;
RT "The Rab GTPase RabA4d regulates pollen tube tip growth in Arabidopsis
RT thaliana.";
RL Plant Cell 21:526-544(2009).
RN [7]
RP FUNCTION.
RX PubMed=21134079; DOI=10.1111/j.1600-0854.2010.01146.x;
RA Kang B.H., Nielsen E., Preuss M.L., Mastronarde D., Staehelin L.A.;
RT "Electron tomography of RabA4b- and PI-4Kbeta1-labeled trans Golgi network
RT compartments in Arabidopsis.";
RL Traffic 12:313-329(2011).
RN [8]
RP FUNCTION.
RX PubMed=22318862; DOI=10.1093/pcp/pcs011;
RA Delage E., Ruelland E., Guillas I., Zachowski A., Puyaubert J.;
RT "Arabidopsis type-III phosphatidylinositol 4-kinases beta1 and beta2 are
RT upstream of the phospholipase C pathway triggered by cold exposure.";
RL Plant Cell Physiol. 53:565-576(2012).
RN [9]
RP REVIEW.
RX PubMed=22899063; DOI=10.4161/psb.21305;
RA Delage E., Ruelland E., Zachowski A., Puyaubert J.;
RT "Eat in or take away? How phosphatidylinositol 4-kinases feed the
RT phospholipase C pathway with substrate.";
RL Plant Signal. Behav. 7:1197-1199(2012).
CC -!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed
CC step in the production of the second messenger inositol-1,4,5-
CC trisphosphate (By similarity). Necessary for proper organization of the
CC trans-Golgi network (TGN) and post-Golgi secretion in root hairs.
CC Together with PI4KB1, required during polarized root hair expansion and
CC pollen tube elongation. Functions redundantly with PI4KB1 upstream of
CC the cold response phosphoinositide-dependent phospholipase C (PI-PLC)
CC pathway. {ECO:0000250, ECO:0000269|PubMed:16567499,
CC ECO:0000269|PubMed:19208902, ECO:0000269|PubMed:21134079,
CC ECO:0000269|PubMed:22318862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9FMJ0}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9FMJ0}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9FMJ0}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q9FMJ0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9FMJ0}. Note=Associated to tip-localized
CC membranes in growing root hairs. {ECO:0000250|UniProtKB:Q9FMJ0}.
CC -!- DOMAIN: The PPC (Plant PI4K Charged) region is involved in membrane
CC targeting and phospholipid binding. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: When associated with PI4KB1 disruption: aberrant
CC root hair morphologies, and short and wavy pollen tubes.
CC {ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:19208902}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391712; CAC05461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91380.1; -; Genomic_DNA.
DR EMBL; AK228931; BAF00820.1; -; mRNA.
DR RefSeq; NP_196497.1; NM_120971.3.
DR AlphaFoldDB; Q0WPX9; -.
DR SMR; Q0WPX9; -.
DR STRING; 3702.AT5G09350.1; -.
DR iPTMnet; Q0WPX9; -.
DR PaxDb; Q0WPX9; -.
DR PRIDE; Q0WPX9; -.
DR ProteomicsDB; 251326; -.
DR EnsemblPlants; AT5G09350.1; AT5G09350.1; AT5G09350.
DR GeneID; 830794; -.
DR Gramene; AT5G09350.1; AT5G09350.1; AT5G09350.
DR KEGG; ath:AT5G09350; -.
DR Araport; AT5G09350; -.
DR TAIR; locus:2184782; AT5G09350.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_4_1_1; -.
DR InParanoid; Q0WPX9; -.
DR OMA; GMYRVLN; -.
DR OrthoDB; 1147978at2759; -.
DR PhylomeDB; Q0WPX9; -.
DR BioCyc; ARA:AT5G09350-MON; -.
DR PRO; PR:Q0WPX9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WPX9; baseline and differential.
DR Genevisible; Q0WPX9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IGI:TAIR.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Developmental protein; Golgi apparatus;
KW Kinase; Membrane; Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..1116
FT /note="Phosphatidylinositol 4-kinase beta 2"
FT /id="PRO_0000398595"
FT DOMAIN 1..143
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT REPEAT 210..229
FT /note="1"
FT REPEAT 242..261
FT /note="2"
FT REPEAT 264..283
FT /note="3"
FT REPEAT 286..304
FT /note="4"
FT REPEAT 307..326
FT /note="5"
FT REPEAT 329..348
FT /note="6"
FT REPEAT 351..370
FT /note="7"
FT REPEAT 378..396
FT /note="8"
FT REPEAT 418..436
FT /note="9"
FT REPEAT 452..470
FT /note="10"
FT REPEAT 488..507
FT /note="11"
FT DOMAIN 830..1101
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 210..507
FT /note="11 X 20 AA approximate repeats (PPC)"
FT REGION 394..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..842
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 964..972
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 983..1007
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMJ0"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMJ0"
SQ SEQUENCE 1116 AA; 126242 MW; C1116F2E5ED4D936 CRC64;
MQMAQFLSLV RGDSIESPRE ITSPSNLISE SGSNGWLIRF FDSSFFCEWI AVSYLYKHQH
SGVRDYLCNR MYTLPLSGIE SYLFQICYLM VHKPSPSLDK FVIDICAKSL KIALKVHWFL
LAELEDSDDN EGISRIQEKC QIAATLVGEW SPLMRPHNEP STPGSKVLNK FLSSKQKLFS
LTLSPPTQKS LLFSPTSGSN LQDDGSQLSA DDNKIFKRLI PSPKVRDALL FRKSADKEDE
ECEKDGFFKR LLRDSRGEDD EQRSNSEGFF KRLLKDNKSE EEEISNNSEG FFKRLRSSKG
DEEELTSSSD GFFKRLLRDN KGDEEELGAN SEGFFKKLLR DSKNEDEEPN ANTEGFFKKL
FHESKNEDDK VSNAVDDEEK DGFLKKLFKE KFDEKRNGNE RNETDETVYT DETSGEDNGR
EGFFKKLFKE KFEDKPNIGK ADDGNESEDD ESSEFSLFRR LFRRHPEDVK TTLPSENCSN
GGFVESSPGT ENFFRKLFRD RDRSVEDSEL FGSKKYKEKC PGSPKPQNNT PSKKPPLPNN
TAAQFRKGSY HESLEFVHAL CETSYDLVDI FPIEDRKTAL RESIAEINSH LAQAETTGGI
CFPMGRGVYR VVNIPEDEYV LLNSREKVPY MICVEVLKAE TPCGAKTTST SLKLSKGGIP
LANGDAFLHK PPPWAYPLST AQEVYRNSAD RMSLSTVEAI DQAMTHKSEV KLVNACLSVE
THSNSNTKSV SSGVTGVLRT GLESDLEWVR LVLTADPGLR MESITDPKTP RRKEHRRVSS
IVAYEEVRAA AAKGEAPPGL PLKGAGQDSS DAQPMANGGM LKAGDALSGE FWEGKRLRIR
KDSIYGNLPG WDLRSIIVKS GDDCRQEHLA VQLISHFFDI FQEAGLPLWL RPYEVLVTSS
YTALIETIPD TASIHSIKSR YPNITSLRDF FDAKFKENSP SFKLAQRNFV ESMAGYSLVC
YLLQIKDRHN GNLLMDEEGH IIHIDFGFML SNSPGGVNFE SAPFKLTREL LEVMDSDAEG
LPSEFFDYFK VLCIQGFLTC RKHAERIILL VEMLQDSGFP CFKGGPRTIQ NLRKRFHLSL
TEEQCVSLVL SLISSSLDAW RTRQYDYYQR VLNGIR
