PI5K3_ARATH
ID PI5K3_ARATH Reviewed; 705 AA.
AC O48709;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 3 {ECO:0000303|PubMed:12226484};
DE Short=AtPIP5K3 {ECO:0000303|PubMed:12226484};
DE EC=2.7.1.68 {ECO:0000250|UniProtKB:Q99755};
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 3 {ECO:0000303|PubMed:12226484};
DE AltName: Full=Diphosphoinositide kinase 3 {ECO:0000303|PubMed:12226484};
DE AltName: Full=PtdIns(4)P-5-kinase 3 {ECO:0000303|PubMed:12226484};
GN Name=PIP5K3 {ECO:0000303|PubMed:12226484};
GN OrderedLocusNames=At2g26420 {ECO:0000312|Araport:AT2G26420};
GN ORFNames=T9J22.9 {ECO:0000312|EMBL:AAC14492.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
CC -!- FUNCTION: With DRP1A and DRP2B, required for the precise coordination
CC of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair
CC positioning during planar polarity formation in root hair-forming
CC cells, probably by mediating the correct basal-to-planar polarity
CC switching of D6PK into the polar, lipid-enriched domain.
CC {ECO:0000269|PubMed:27251533}.
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 Evidence={ECO:0000250|UniProtKB:Q99755};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27251533}.
CC Note=Accumulates in a sterol-enriched, polar membrane domain during
CC root hair initiation. {ECO:0000269|PubMed:27251533}.
CC -!- DISRUPTION PHENOTYPE: Basal shift of ARAC3/ROP6 and ARAC4/ROP2
CC positioning and broad lateral localization of D6PK in root hair-forming
CC cells leading to basal shift of root hair positions.
CC {ECO:0000269|PubMed:27251533}.
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DR EMBL; AC002505; AAC14492.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07835.1; -; Genomic_DNA.
DR PIR; T00975; T00975.
DR RefSeq; NP_001318292.1; NM_001336067.1.
DR AlphaFoldDB; O48709; -.
DR SMR; O48709; -.
DR BioGRID; 2534; 1.
DR STRING; 3702.AT2G26420.1; -.
DR PaxDb; O48709; -.
DR PRIDE; O48709; -.
DR EnsemblPlants; AT2G26420.1; AT2G26420.1; AT2G26420.
DR GeneID; 817182; -.
DR Gramene; AT2G26420.1; AT2G26420.1; AT2G26420.
DR KEGG; ath:AT2G26420; -.
DR Araport; AT2G26420; -.
DR TAIR; locus:2066246; AT2G26420.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; O48709; -.
DR OMA; IMEEWKS; -.
DR PhylomeDB; O48709; -.
DR BioCyc; ARA:AT2G26420-MON; -.
DR BRENDA; 2.7.1.68; 399.
DR PRO; PR:O48709; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48709; baseline and differential.
DR Genevisible; O48709; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
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; 7.
DR Pfam; PF01504; PIP5K; 1.
DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1.
DR SMART; SM00698; MORN; 7.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 4: Predicted;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..705
FT /note="Phosphatidylinositol 4-phosphate 5-kinase 3"
FT /id="PRO_0000185475"
FT REPEAT 58..80
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 81..103
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT REPEAT 104..126
FT /note="MORN 3"
FT /evidence="ECO:0000255"
FT REPEAT 127..149
FT /note="MORN 4"
FT /evidence="ECO:0000255"
FT REPEAT 150..172
FT /note="MORN 5"
FT /evidence="ECO:0000255"
FT REPEAT 173..195
FT /note="MORN 6"
FT /evidence="ECO:0000255"
FT REPEAT 196..218
FT /note="MORN 7"
FT /evidence="ECO:0000255"
FT DOMAIN 321..701
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 661..682
FT /note="Activation loop"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 80134 MW; 851E86AE18AAF157 CRC64;
MQETVFLFTE ENLNKEQSLG VKYKQSSRRV VPMTSCEVSD TAAEIRIVEK VLKNGDLYNG
GLSAGVPHGT GKYLWSDGCM YEGEWTRGKA SGKGRFSWPS GATYEGQFKD GRMDGEGTFI
GIDGDTYRGH WLWGRKHGYG EKRYANGDGY QGNWKANLQD GNGRYVWSDG NEYVGEWKNG
VISGKGKMTW ANGNRYDGLW ENGAPVGKGV LSWGEEKTSY NGWGRKSKKK DEEIVQNHKL
SSVETLSANT NFPRICISEL EDTGVCDHVE ASPYTSESDT SGCGEQEWAR SPLLLESGGA
MSVQQSPRWL DEGDVKKPGH TVTAGHKNYD LMLNLQLGIR YSVGKHASLL RELRHSDFDP
KDKQWTRFPP EGSKSTPPHL SAEFKWKDYC PIVFRHLRDL FAIDQADYML AICGNESLRE
FASPGKSGSA FYLTQDERYM IKTMKKSEIK VLLKMLPNYY EHVSKYKNSL VTKFFGVHCV
KPVGGQKTRF IVMGNLFCSE YRIHKRFDLK GSSHGRTIDK DEGEIDETTT LKDLDLKYVF
RLETSWFQAF INQIDLDCEF LEAERIMDYS LLIGLHFRES GMRDDISLGI GRRDQEDKLM
RGNGPLMRLG ESTPAKAEQV SRFEEETWEE DAIDNSNPKG TRKEAVEVIL YFGVIDILQD
YDITKKLEHA YKSLHADPAS ISAVDPKLYS RRFRDFINKI FIEDK
