P4KG3_ARATH
ID P4KG3_ARATH Reviewed; 574 AA.
AC Q9FNF8;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 3;
DE Short=AtPI4Kgamma3;
DE Short=PI-4Kgamma3;
DE Short=PI4K gamma 3;
DE EC=2.7.1.67;
GN Name=PI4KG3; Synonyms=PI4KGAMMA3; OrderedLocusNames=At5g24240;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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;
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 [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; AB006701; BAB10389.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93274.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68289.1; -; Genomic_DNA.
DR EMBL; AK226621; BAE98733.1; -; mRNA.
DR RefSeq; NP_001318634.1; NM_001343856.1.
DR RefSeq; NP_197812.1; NM_122330.2.
DR AlphaFoldDB; Q9FNF8; -.
DR SMR; Q9FNF8; -.
DR STRING; 3702.AT5G24240.1; -.
DR iPTMnet; Q9FNF8; -.
DR PaxDb; Q9FNF8; -.
DR PRIDE; Q9FNF8; -.
DR ProteomicsDB; 250923; -.
DR EnsemblPlants; AT5G24240.1; AT5G24240.1; AT5G24240.
DR EnsemblPlants; AT5G24240.2; AT5G24240.2; AT5G24240.
DR GeneID; 832491; -.
DR Gramene; AT5G24240.1; AT5G24240.1; AT5G24240.
DR Gramene; AT5G24240.2; AT5G24240.2; AT5G24240.
DR KEGG; ath:AT5G24240; -.
DR Araport; AT5G24240; -.
DR TAIR; locus:2169774; AT5G24240.
DR eggNOG; KOG0001; Eukaryota.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_023603_0_0_1; -.
DR InParanoid; Q9FNF8; -.
DR OMA; RNDSQIR; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q9FNF8; -.
DR PRO; PR:Q9FNF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNF8; baseline and differential.
DR Genevisible; Q9FNF8; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA: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:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:1902074; P:response to salt; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044571; P4KG1-8.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45800; PTHR45800; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00240; ubiquitin; 2.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..574
FT /note="Phosphatidylinositol 4-kinase gamma 3"
FT /id="PRO_0000423361"
FT DOMAIN 32..109
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 110..188
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 257..555
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 263..269
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 414..422
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 438..464
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT BINDING 264..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 381..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
SQ SEQUENCE 574 AA; 64035 MW; 8F0169D5E4CE3EB3 CRC64;
MSVASVALSP ALEELVNFPG IIGRFGFNLD DPILVFLTIA GSVIPKRVME SDSIASVKLR
IQSIKGFFVK KQKLLYDGRE VSRNDSQIRD YGLADGKLLH LVIRLSDLQA ISVRTVDGKE
FELVVERSRN VGYVKQQIAS KEKELGIPRD HELTLDGEEL DDQRLITDLC QNGDNVIHLL
ISKSAKVRAK PVGKDFEVFI EDVNHKHNVD GRRGKNISSE AKPKEFFVEP FIVNPEIKLP
ILLKELISST LEGLEKGNGP IRSSDGSGGA YFMQDPSGHK YVSVFKPIDE EPMAVNNPHG
QPVSVDGEGL KKGTQVGEGA IREVAAYILD YPMTGPRTFP HDQTGFAGVP PTTMVKCLHK
DFNHPNGYSF SPENTKIGSL QMFVSNVGSC EDMGYRVFPV DQVHKISVLD IRLANADRHA
GNILVSRDGK DGQMVLTPID HGYCFPNKFE DCTFEWLYWP QAKEPYSSET LEYIKSLDPE
KDIELLRFHG WEIPPSCTRV LRISTMLLKK GSAKGLTPFT IGSIMCRETL KEESVIEQII
HDAEAIVPTE TTEDEFISTV SAIMDNRLDQ YAWN
