P4KA1_ARATH
ID P4KA1_ARATH Reviewed; 2028 AA.
AC Q9SXA1; O81129;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Phosphatidylinositol 4-kinase alpha 1 {ECO:0000303|PubMed:12805633};
DE Short=PI4-kinase alpha 1ao;
DE Short=PtdIns-4-kinase alpha 1 {ECO:0000303|PubMed:12805633};
DE EC=2.7.1.67 {ECO:0000269|PubMed:12805633};
DE AltName: Full=Phosphatidylinositol 4-OH kinase alpha1 {ECO:0000305};
DE Short=AtPI4Kalpha1 {ECO:0000303|PubMed:12805633};
DE Short=PI-4Kalpha1 {ECO:0000305};
GN Name=PI4KA1 {ECO:0000305};
GN Synonyms=PI4KALPHA {ECO:0000303|PubMed:9712908},
GN PI4KALPHA1 {ECO:0000303|PubMed:12805633};
GN OrderedLocusNames=At1g49340 {ECO:0000312|Araport:AT1G49340};
GN ORFNames=F13F21.23 {ECO:0000312|EMBL:AAD43164.1};
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], FUNCTION, TISSUE SPECIFICITY, AND PH DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=9712908; DOI=10.1074/jbc.273.35.22761;
RA Stevenson J.M., Perera I.Y., Boss W.F.;
RT "A phosphatidylinositol 4-kinase pleckstrin homology domain that binds
RT phosphatidylinositol 4-monophosphate.";
RL J. Biol. Chem. 273:22761-22767(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PH DOMAIN,
RP AND INTERACTION WITH ACTIN FILAMENTS.
RX PubMed=12805633; DOI=10.1104/pp.103.021758;
RA Stevenson-Paulik J., Love J., Boss W.F.;
RT "Differential regulation of two Arabidopsis type III phosphatidylinositol
RT 4-kinase isoforms. A regulatory role for the pleckstrin homology domain.";
RL Plant Physiol. 132:1053-1064(2003).
RN [6]
RP DISRUPTION PHENOTYPE, AND 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 [7]
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 (Probable). Can bind to phosphatidylinositol 4-
CC monophosphate (PI-4-P or PtdIns4P), phosphatidylinositol 4,5-
CC bisphosphate (PI-4,5-P2 or PtdIns4,5P2), and phosphatidic acid (PtdOH),
CC but not to 3-phosphoinositides (PubMed:9712908). May function upstream
CC of the cold response phosphoinositide-dependent phospholipase C (PI-
CC PLC) pathway (PubMed:22318862). {ECO:0000269|PubMed:22318862,
CC ECO:0000269|PubMed:9712908, ECO:0000305|PubMed:9712908}.
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; Evidence={ECO:0000269|PubMed:12805633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000269|PubMed:12805633};
CC -!- ACTIVITY REGULATION: Repressed by PtdIns4P, adenosine and wortmannin,
CC but stimulated by other negatively charged lipids such as PtdIns3P,
CC PtdOH, and phosphatidyl-serine (PtdSer). {ECO:0000269|PubMed:12805633}.
CC -!- SUBUNIT: Interacts in vitro with actin filaments via its PH domain.
CC {ECO:0000269|PubMed:12805633}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12805633};
CC Peripheral membrane protein {ECO:0000269|PubMed:12805633}; Cytoplasmic
CC side {ECO:0000269|PubMed:12805633}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12805633}.
CC -!- TISSUE SPECIFICITY: Present in leaves and inflorescences.
CC {ECO:0000269|PubMed:9712908}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:22318862}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF035936; AAC32803.2; -; mRNA.
DR EMBL; AC007504; AAD43164.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32419.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32420.1; -; Genomic_DNA.
DR PIR; F96529; F96529.
DR PIR; T52022; T52022.
DR RefSeq; NP_175359.2; NM_103824.4.
DR RefSeq; NP_850960.1; NM_180629.2.
DR AlphaFoldDB; Q9SXA1; -.
DR SMR; Q9SXA1; -.
DR STRING; 3702.AT1G49340.2; -.
DR iPTMnet; Q9SXA1; -.
DR PaxDb; Q9SXA1; -.
DR PRIDE; Q9SXA1; -.
DR ProteomicsDB; 251360; -.
DR EnsemblPlants; AT1G49340.1; AT1G49340.1; AT1G49340.
DR EnsemblPlants; AT1G49340.2; AT1G49340.2; AT1G49340.
DR GeneID; 841357; -.
DR Gramene; AT1G49340.1; AT1G49340.1; AT1G49340.
DR Gramene; AT1G49340.2; AT1G49340.2; AT1G49340.
DR KEGG; ath:AT1G49340; -.
DR Araport; AT1G49340; -.
DR TAIR; locus:2010202; AT1G49340.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_2_1_1; -.
DR InParanoid; Q9SXA1; -.
DR OMA; MSQRDEN; -.
DR OrthoDB; 1147978at2759; -.
DR PhylomeDB; Q9SXA1; -.
DR BioCyc; ARA:AT1G49340-MON; -.
DR PRO; PR:Q9SXA1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXA1; baseline and differential.
DR Genevisible; Q9SXA1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0098857; C:membrane microdomain; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0001727; F:lipid kinase activity; IDA:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
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:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0048831; P:regulation of shoot system development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP: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; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Membrane; Reference proteome; Transferase.
FT CHAIN 1..2028
FT /note="Phosphatidylinositol 4-kinase alpha 1"
FT /id="PRO_0000398592"
FT DOMAIN 1483..1659
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1734..2012
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 184..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1660..1773
FT /note="Pleckstrin homology (PH) domain conferring
FT phosphoinositide binding specificity"
FT /evidence="ECO:0000305|PubMed:9712908"
FT REGION 1740..1746
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1876..1884
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1895..1920
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 186..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 463
FT /note="V -> E (in Ref. 1; AAC32803)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="E -> G (in Ref. 1; AAC32803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2028 AA; 224017 MW; 5264B0A885202F04 CRC64;
MEALTELCDI IAKNPKQFSE KLAWICGRCP QTEWLLAESP RVSRSHLNAV LAVARIISKN
PESIDNRAKS VVNEFLSAIP ASFRRSFWPH SFPSQLISSF YCDFLSYLSC AADLSPEFGT
EVARFTGEVV IAAIAPSSGD SDGDPAISKA FLVALSQHFP SILQSDGDKL ITMLLDQFVL
NRAPASPKEQ RQQNSANSET DTSSSQGSPI STNRYPSGKT EMASPGDEVA SHGSNLSSKS
SSSVVMNGGS IVWKSGVDQL SFGFSEGSGG ANPVFRQQVA SFEDESIESL EKQEIAFRLI
THILDKVKID SKLQDQVRFI AKRQLQSMSA FLKSRKRDWN EQGQVLKTRV NAKLSVYQAA
AKMKIKSLVS LETDGKTSKR LVLETLALLL DAADACLTSV WRKMKACEEL FDSLLSGIAK
IAVARGGQPL RVLLIRLKPL VLAVCALPDQ GAMLESIFKT SCVIIESAWA KDRAPVDNFI
MGLASSIRER NDYEEQVDRE KQVPAVQLNV IRLLADLNVA VKKPEVADMI LPLFIESLEE
GDASTPSFLR LQLLDAVSRI ATLGFDKSYR ETVVLMTRSY LSKLSSVGSV ESKTSAPEAT
TERVETLPAG FLTIASGLMD TKLRSDYRHR LLSLCSDVGL AAESKSGGSG VDFLGPLLPA
VAEICSDFDP TMDVEPSLLK LFRNLWFYIA LFGLAPPIVK TPTPPLKSTS NSVNSVGSMS
ATALQAVGGP YMWDNQWALA VQRIAQGTPP LVVSSVKWLE DELELNALHN PGSRRGNGNE
KVASTQRLAL STALGGRVDV AAMNTISGVK ATYLLAVAFL EIIRFISNGG ILNGESSVSA
SRSAFSCVFE YLKTPNLTPA VSQCLTAIVH RAFETAVSWL EDRISLTGKD ARNRELTTYA
HACFLIKSMS QRDEHVRDIS VNLLTQLRDK FPQVLWHSSC LDSLLFSVHD NTPSTVVNDP
AWTAAVRSLY QKVVREWIII SLSYAPCTSQ GLLQDKLCKA NTWQRAQTTT DVVSLLSEIK
IGTGKNELWS GIRTANIPAV MAAAAAASGA NLKVSEAFNL EVLGTGVVSA TVKCNHAGEI
AGMRRLYNSI GGFQSGSTPS GFGGGLQRLI SGAFSQAPQP EDDSFNEMLI ARFVRLLQQF
VNTAEKGGEV EKSQFRETCS QATALLLSNL GGESKTNVEG FSQLLRLLCW CPAYISTPDA
METGIFIWTW LVSAAPQLVS LVLAELVDAW IWTIDTKRGL FASDVRYSGP AAKLRPHLSP
GEPEDPPESD PVDQIVAHRL WLGFLIDRFE VVRHNSAEQL LLLGRMLQRS TDLEWCFTRH
PAAAGTFFSL MLLGLKFCSC QTQGNMQKFR SGLQLLEDRI YRTSLGWFAH QPEWYDVNIP
NFCHSEALSV SVFVHFLSNE LSESSQSDSK GKPRESGNLI DVTDQYHPVW GEMDNYTLGK
EKRKQLLLML CQHEADRLDV WAQPISSKDS PYSRLKISSE KWTEYAKTAF SVDPRIALSV
ASRFPANASV KSEVTQLVQT NIVDLRTIPE ALPYFVTPKN VEENSVLLQQ LPHWAACSIT
QALEFLTPAY KGHPRVMAYV LRVLESYPPE RVTFFMPQLV QSLRYDDGRL VEGYLLRATQ
RSDIFAHILI WHLQGEDVQE TPKDGSIDKN AAFQEILPQV RQHIIDGFSP NALDMFTREF
DFFDKVTSIS GVLFPLPKEE RRAGIRRELE KIEMQGDDLY LPTAPNKLVR GIRVDSGIPL
QSAAKVPIMI TFNVIDRDGD HSDVKPQACI FKVGDDCRQD VLALQVISLL RDIFQAAGLN
LYLFPYGVLP TGAERGIIEV VPNTRSRSQM GETTDGGLYE IFQQDYGPVG STTFETAREN
FLISSAGYAV ASLLLQPKDR HNGNLLFDDV GRLVHIDFGF ILETSPGGNM RFESAHFKLS
HEMTQLLDPS GVMKSKTWHQ FVSLCVKGYL AARRQMDGII STVQMMLESG LPCFSRGDPI
GNLRKRFHPE MSEREAAHFM IHVCTDAYNK WTTAGYDLIQ YLQQGIEK
