P4KG8_ARATH
ID P4KG8_ARATH Reviewed; 533 AA.
AC Q0WMZ6; Q9LXY0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 8;
DE Short=AtPI4Kgamma8;
DE Short=PI-4Kgamma8;
DE Short=PI4K gamma 8;
DE EC=2.7.1.67;
GN Name=PI4KG8; Synonyms=PI4KGAMMA8; OrderedLocusNames=At3g56600;
GN ORFNames=T5P19_250;
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=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 [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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 [5]
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 [6]
RP GENE FAMILY.
RX PubMed=17880284; DOI=10.1042/bj20070959;
RA Galvao R.M., Kota U., Soderblom E.J., Goshe M.B., Boss W.F.;
RT "Characterization of a new family of protein kinases from Arabidopsis
RT containing phosphoinositide 3/4-kinase and ubiquitin-like domains.";
RL Biochem. J. 409:117-127(2008).
CC -!- FUNCTION: The phosphorylation of phosphatidylinositol (PI) to PI4P is
CC the first committed step in the generation of phosphatidylinositol 4,5-
CC bisphosphate (PIP2), a precursor of the second messenger inositol
CC 1,4,5-trisphosphate (InsP3). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE79542.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF01504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL163972; CAB88063.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79542.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79543.2; -; Genomic_DNA.
DR EMBL; DQ446770; ABE66021.1; -; mRNA.
DR EMBL; AK229660; BAF01504.1; ALT_INIT; mRNA.
DR PIR; T49061; T49061.
DR RefSeq; NP_001319769.1; NM_001339803.1.
DR RefSeq; NP_001327285.1; NM_001339804.1.
DR RefSeq; NP_191219.2; NM_115519.3.
DR AlphaFoldDB; Q0WMZ6; -.
DR SMR; Q0WMZ6; -.
DR STRING; 3702.AT3G56600.1; -.
DR PaxDb; Q0WMZ6; -.
DR PRIDE; Q0WMZ6; -.
DR ProteomicsDB; 251361; -.
DR EnsemblPlants; AT3G56600.2; AT3G56600.2; AT3G56600.
DR GeneID; 824827; -.
DR Gramene; AT3G56600.2; AT3G56600.2; AT3G56600.
DR KEGG; ath:AT3G56600; -.
DR Araport; AT3G56600; -.
DR TAIR; locus:2102604; AT3G56600.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_027241_1_1_1; -.
DR InParanoid; Q0WMZ6; -.
DR OMA; RIFILCT; -.
DR OrthoDB; 1273723at2759; -.
DR PRO; PR:Q0WMZ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WMZ6; baseline and differential.
DR Genevisible; Q0WMZ6; AT.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR044571; P4KG1-8.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR45800; PTHR45800; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..533
FT /note="Phosphatidylinositol 4-kinase gamma 8"
FT /id="PRO_0000423365"
FT DOMAIN 101..397
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 107..113
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 243..251
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 276..302
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT BINDING 108..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 210..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
SQ SEQUENCE 533 AA; 58376 MW; 87FAAED73C9BF1B8 CRC64;
MAVALDPLTD RFSQFSRSSQ RCRLQSLTNL DFNFLGFNTK QTNLSASSHS LNNRSVSTPC
FSISGSNLDG SATPHIEILG GQRVPTVRSL VAEVTIAIVS GAQPLLLPSG LGGAYLLQTE
KGNNIAVAKP VDEEPLAFNN PKGSGGLTLG QPGMKRSIRV GESGIRELAA YLLDHQGFSS
VPPTALVRIS HVPFHDRGSD HAAYKVASLQ RFVGHDFDAG ELGPGSFTVV SVHRIGILDV
RVLNLDRHAG NMLVKKIHDQ DETTCSNGVG AAELVPIDHG LCLPECLDDP YFEWLNWPQA
SVPFTDIELQ YISNLDPFKD AELLRTELDS IQESSLRVLI VCTIFLKEAA AAGLSLAEIG
EKMTRDICRG EESSSVLEIL CNKAKASAVS GSDDDDDYSS EWNEVEAELE CGIFQFDDEV
ECKELPDMLQ VPIFTRVPSI AANLSALMRC PPNQWISTYD TNIEEERRDR SIVRSKSHPI
CVNYDEKEGV YFGDMSGDEW EMFLHSFQML LPEALEGSTS KGPKPRFGSS CKF
