P4KG7_ARATH
ID P4KG7_ARATH Reviewed; 650 AA.
AC Q9SI52; Q0WMJ0; Q940C9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 7 {ECO:0000303|PubMed:17880284};
DE Short=AtPI4Kgamma7 {ECO:0000303|PubMed:17880284};
DE Short=PI-4Kgamma7 {ECO:0000303|PubMed:17880284};
DE Short=PI4K gamma 7 {ECO:0000303|PubMed:17880284};
DE EC=2.7.1.67 {ECO:0000269|PubMed:17880284};
DE AltName: Full=Ubiquitin-like domain kinase gamma 7 {ECO:0000303|PubMed:17880284};
DE Short=UbDK gamma 7 {ECO:0000303|PubMed:17880284};
GN Name=PI4KG7 {ECO:0000303|PubMed:17880284};
GN Synonyms=PI4KGAMMA7 {ECO:0000303|PubMed:17880284},
GN UBDKGAMMA7 {ECO:0000303|PubMed:17880284};
GN OrderedLocusNames=At2g03890 {ECO:0000312|Araport:AT2G03890};
GN ORFNames=T18C20.9 {ECO:0000312|EMBL:AAD24822.2};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 460-650.
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 FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND 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) (By similarity). Undergoes
CC autophosphorylation and phosphorylates serine/threonine residues of
CC protein substrates (PubMed:17880284). {ECO:0000250|UniProtKB:Q9BTU6,
CC ECO:0000269|PubMed:17880284}.
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:17880284};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000269|PubMed:17880284};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SI52-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007196; AAD24822.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05763.1; -; Genomic_DNA.
DR EMBL; AY056101; AAL06989.1; -; mRNA.
DR EMBL; BT002696; AAO11612.1; -; mRNA.
DR EMBL; AK229831; BAF01661.1; -; mRNA.
DR PIR; D84453; D84453.
DR RefSeq; NP_565307.1; NM_126434.4. [Q9SI52-1]
DR AlphaFoldDB; Q9SI52; -.
DR SMR; Q9SI52; -.
DR BioGRID; 316; 1.
DR STRING; 3702.AT2G03890.1; -.
DR iPTMnet; Q9SI52; -.
DR PaxDb; Q9SI52; -.
DR PRIDE; Q9SI52; -.
DR ProteomicsDB; 251407; -. [Q9SI52-1]
DR EnsemblPlants; AT2G03890.1; AT2G03890.1; AT2G03890. [Q9SI52-1]
DR GeneID; 814915; -.
DR Gramene; AT2G03890.1; AT2G03890.1; AT2G03890. [Q9SI52-1]
DR KEGG; ath:AT2G03890; -.
DR Araport; AT2G03890; -.
DR TAIR; locus:2056799; AT2G03890.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_027241_1_1_1; -.
DR InParanoid; Q9SI52; -.
DR OMA; CVSSANM; -.
DR PhylomeDB; Q9SI52; -.
DR PRO; PR:Q9SI52; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI52; baseline and differential.
DR Genevisible; Q9SI52; AT.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR044571; P4KG1-8.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45800; PTHR45800; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..650
FT /note="Phosphatidylinositol 4-kinase gamma 7"
FT /id="PRO_0000423364"
FT DOMAIN 46..103
FT /note="Ubiquitin-like; degenerate"
FT DOMAIN 166..463
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 172..178
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 316..324
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 343..369
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 508..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 283..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C671"
SQ SEQUENCE 650 AA; 72762 MW; 037C8D85B70EED9F CRC64;
MSRNLDSPVQ TQMAVAVFKT PLTGASKMEG KQHHKHQHLQ RQSSGRRVFV QTETGCVLGM
ELDRSDNVHT VKRRLQIALN FPTEESSLTY GDMVLTNDLS AVRNDSPLLL KRNFMHRSSS
TPCLSPTGRD LQQKDRSGPI EILGHSDCFS IVKHMVKDIV KAMKMGVEPL PVHSGLGGAY
YFRNKRGESV AIVKPTDEEP FAPNNPKGFV GKALGQPGLK SSVRVGETGF REVAAYLLDY
GRFANVPPTA LVKITHSVFN VNDGVKGNKP REKKLVSKIA SFQKFVAHDF DASDHGTSSF
PVTSVHRIGI LDIRIFNTDR HGGNLLVKKL DGVGMFGQVE LIPIDHGLCL PETLEDPYFE
WIHWPQASLP FSDEEVDYIQ SLDPVKDCDM LRRELPMIRE ACLRVLVLCT IFLKEASAYG
LCLAEIGEMM TREFRPGEEE PSELEVVCIE AKRSVTERDV FSPRSDVVGE AEFQFDLDCD
DLESVYSSKI QLTDDYFTKN PFSNGRSSLG KLEESIKEEE EDEEEEEDKT ENTVPMIIMK
DSFFSSAAFH DKAPSLSKLS TSMKNTHLSD TTRKNPKPLT RGKSENTSSG HKSANEQLPV
SASFVKVADM KEDEWVLFLE RFQELLGPAF AKRKTATLSK RQRLGTSCQF
