P4KG5_ARATH
ID P4KG5_ARATH Reviewed; 630 AA.
AC Q9C671;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 5;
DE Short=AtPI4Kgamma5;
DE Short=PI-4Kgamma5;
DE Short=PI4K gamma 5;
DE EC=2.7.1.67;
GN Name=PI4KG5; Synonyms=PI4KGAMMA5; OrderedLocusNames=At1g26270;
GN ORFNames=F28B23.7;
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=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 [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 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 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).
RN [6]
RP INTERACTION WITH AHK2.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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 -!- SUBUNIT: Interacts with AHK2. {ECO:0000269|PubMed:18642946}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AC079829; AAG50675.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30670.1; -; Genomic_DNA.
DR EMBL; AY035014; AAK59519.1; -; mRNA.
DR EMBL; AY058170; AAL25584.1; -; mRNA.
DR EMBL; AY075684; AAL77691.1; -; mRNA.
DR PIR; A86389; A86389.
DR RefSeq; NP_564242.1; NM_102391.3.
DR AlphaFoldDB; Q9C671; -.
DR SMR; Q9C671; -.
DR BioGRID; 24405; 1.
DR IntAct; Q9C671; 1.
DR STRING; 3702.AT1G26270.1; -.
DR iPTMnet; Q9C671; -.
DR PaxDb; Q9C671; -.
DR PRIDE; Q9C671; -.
DR ProteomicsDB; 251346; -.
DR EnsemblPlants; AT1G26270.1; AT1G26270.1; AT1G26270.
DR GeneID; 839168; -.
DR Gramene; AT1G26270.1; AT1G26270.1; AT1G26270.
DR KEGG; ath:AT1G26270; -.
DR Araport; AT1G26270; -.
DR TAIR; locus:2028798; AT1G26270.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_027241_1_1_1; -.
DR InParanoid; Q9C671; -.
DR OMA; VCFVRLS; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q9C671; -.
DR PRO; PR:Q9C671; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C671; baseline and differential.
DR Genevisible; Q9C671; 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:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..630
FT /note="Phosphatidylinositol 4-kinase gamma 5"
FT /id="PRO_0000398600"
FT DOMAIN 41..98
FT /note="Ubiquitin-like; degenerate"
FT DOMAIN 162..459
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 168..174
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 312..320
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 339..365
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 500..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 279..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 630 AA; 70259 MW; 48EA8ED4D169670A CRC64;
MSRKLDSPIK TQMAVALVKS PLNGEFREFN KVGMKTPVGR RRVFVQTETG CVLGLELDRS
DNAHTVKRKL QVALNFPIEE SSLTFGDLVL KNDLTAVRSD SPLLLTRNNF HRSSSTPCLS
PMRADLQQRR DESSPIEILG NSVSFSFVRQ MAKDITKAVK KGIDPVAVNS GLGGAYYFKN
SRGESVAIVK PTDEEPYAPN NPKGFVGKAL GQPGLKRSVR VGETGYREVA AYLLDKEHFA
NVPPTALVKI THSIFNVNDG VKASKPMEKM LVSKIASLQQ FIPHDYDASE HGTSNFPVSA
VHRIGILDIR ILNTDRHSGN LLVKKLDGDG MFGQVELVPI DHGLCLPETL EDPYFEWIHW
PQASIPFSED ELKYIANLDP LGDCEMLRRE LPMVREASLR VLVLCTIFLK EAAANGLCLA
EIGEMMTREV RPGDEEPSEI EVVCLEAMSL IGEKDAESPR SDLGNDIEFQ FDIDCEEVTD
CTKKLALPLG LTFGNARGQL SKVEETTEDG EEEEEEDREE EENDRADLEK MPTIKLSMSL
KSTLLGEKSQ KYQKHPGARV ESAYASSAHR SADEQIPSST SFVKLSDMSE EEWTIFLEKY
QELLYPAIEK RKSITLGQKQ RQRLGTSCQF
