P4KG1_ARATH
ID P4KG1_ARATH Reviewed; 561 AA.
AC O22199; Q8RY38;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 1;
DE Short=AtPI4Kgamma1;
DE Short=PI-4Kgamma1;
DE Short=PI4K gamma 1;
DE EC=2.7.1.67;
GN Name=PI4KG1; Synonyms=PI4KGAMMA1; OrderedLocusNames=At2g40850;
GN ORFNames=T20B5.5;
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 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).
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}.
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DR EMBL; AC002409; AAB86445.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09890.1; -; Genomic_DNA.
DR EMBL; AY078924; AAL84930.1; -; mRNA.
DR PIR; T00749; T00749.
DR RefSeq; NP_181617.1; NM_129648.6.
DR AlphaFoldDB; O22199; -.
DR SMR; O22199; -.
DR STRING; 3702.AT2G40850.1; -.
DR PaxDb; O22199; -.
DR PRIDE; O22199; -.
DR ProteomicsDB; 251345; -.
DR EnsemblPlants; AT2G40850.1; AT2G40850.1; AT2G40850.
DR GeneID; 818683; -.
DR Gramene; AT2G40850.1; AT2G40850.1; AT2G40850.
DR KEGG; ath:AT2G40850; -.
DR Araport; AT2G40850; -.
DR TAIR; locus:2058485; AT2G40850.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_027241_1_1_1; -.
DR InParanoid; O22199; -.
DR OMA; EMMTRQF; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; O22199; -.
DR PRO; PR:O22199; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22199; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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..561
FT /note="Phosphatidylinositol 4-kinase gamma 1"
FT /id="PRO_0000423359"
FT DOMAIN 121..416
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 127..133
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 266..274
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 296..322
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 456..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 233..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT CONFLICT 232
FT /note="L -> S (in Ref. 3; AAL84930)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="R -> K (in Ref. 3; AAL84930)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="Missing (in Ref. 3; AAL84930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 61366 MW; 479937B6837E29DA CRC64;
MNCLATTIII TCKPTLISDM AVAIDPFSDK FPYFNRSSQR CRLQSLTNLD FNFLAQSFNH
TFEDDNIHRS VSSPCFSIAA SANMEEDLKA TTAPRIEILG GQRVPTVRAL VAEVTMAMVS
GAQPLLLPSG MGGAYLLQTG KGHNIAVAKP VDEEPLAFNN PKKSGNLMLG QPGMKHSIPV
GETGIRELAA YLLDYQGFSG VPPTALVSIS HVPFHVSDAF SFSSMPYKVA SLQRFVGHDF
DAGELGPGSF TATSVHRIGI LDVRLLNLDR HAGNMLVKRC DKKEAYNRLG TAELVPIDHG
LCLPECLDDP YFEWLNWPQA LVPFSDTELD YISNLDPFKD AELLRTELHS LPESAIRVLV
VCTVFLKQAA AAGLCLAEIG EKMTRDFSKG EESFSLLETL CTKAKASVFG KTSEDSDYSH
EGNEVNTELQ CGMFKFDGGD TPCEAEISEV FHVSKPPLVP RGPRANTIPN DVTASMSSSQ
NQRITHQEKS AKEKKRGGKQ ERCTVRSKSP PISPNHDESK GVSFVDMTTV EWDTFLQSFQ
TLLQDALSKG STPRLGCSCE I
