P4KG2_ARATH
ID P4KG2_ARATH Reviewed; 550 AA.
AC Q9SGW8; Q6NLD9; Q6NPL1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 2;
DE Short=AtPI4Kgamma2;
DE Short=PI-4Kgamma2;
DE Short=PI4K gamma 2;
DE EC=2.7.1.67;
GN Name=PI4KG2; Synonyms=PI4KGAMMA2; OrderedLocusNames=At1g64460/At1g64470;
GN ORFNames=F1N19.4/F1N19.30;
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] OF 1-235.
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-550.
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) 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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23323832; DOI=10.1042/bj20121639;
RA McLoughlin F., Arisz S.A., Dekker H.L., Kramer G., de Koster C.G.,
RA Haring M.A., Munnik T., Testerink C.;
RT "Identification of novel candidate phosphatidic acid-binding proteins
RT involved in the salt-stress response of Arabidopsis thaliana roots.";
RL Biochem. J. 450:573-581(2013).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23323832};
CC Peripheral membrane protein {ECO:0000269|PubMed:23323832}; Cytoplasmic
CC side {ECO:0000269|PubMed:23323832}.
CC -!- INDUCTION: By salt. {ECO:0000269|PubMed:23323832}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19692.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF19692.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAS76698.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAS88785.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC009519; AAF19692.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT012211; AAS76698.1; ALT_FRAME; mRNA.
DR EMBL; BT012395; AAS88785.1; ALT_FRAME; mRNA.
DR EMBL; BT010909; AAR24687.1; -; mRNA.
DR AlphaFoldDB; Q9SGW8; -.
DR SMR; Q9SGW8; -.
DR BioGRID; 27975; 1.
DR IntAct; Q9SGW8; 1.
DR STRING; 3702.AT1G64460.1; -.
DR PaxDb; Q9SGW8; -.
DR PeptideAtlas; Q9SGW8; -.
DR PRIDE; Q9SGW8; -.
DR ProteomicsDB; 250812; -.
DR Araport; AT1G64460; -.
DR TAIR; locus:2019419; AT1G64460.
DR TAIR; locus:2019459; AT1G64470.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_059282_0_0_1; -.
DR OrthoDB; 1273723at2759; -.
DR PRO; PR:Q9SGW8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGW8; baseline and differential.
DR Genevisible; Q9SGW8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; 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:0034051; P:negative regulation of plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050821; P:protein stabilization; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
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 PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..550
FT /note="Phosphatidylinositol 4-kinase gamma 2"
FT /id="PRO_0000423360"
FT DOMAIN 34..111
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 112..190
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 234..532
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..246
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 392..400
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 415..441
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT BINDING 241..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 359..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
SQ SEQUENCE 550 AA; 60447 MW; 48DED024E29EEB1A CRC64;
MSVADVALSP IHRGSAFAVG GFGQSTTTHY SVKSVLVFLS VSGSTMPMLI LESDSIAEVK
LRIQTCNGFR VRRQKLVFSG RELARNASRV KDYGVTGGSV LHLVLKLYDP LLVTVITTCG
KVFQFHVDRR RNVGYLKKRI SKEGKGFPEV DDQEILFKGE KLDDNRIIDG ICKDGNSVIH
LLVKKSVEDT VKREEDTATG KDSLLEPVVL NPDVKLPEVL EDMIDRTVDG LNKGSPPVRS
AEGTGGTYLM QDSSGLNYVS VFKPMDEEPM AVNNPQQLPV SSDGQGLKRG TRVGEGATRE
VAAYLLDHPK SGLRSVSKEV MGFAGVPPTA MVRSSHKVYN YPNGFSSCAT KDAKVGSLQM
FMKNNGSCED IGPGAFPVEE VHKICVFDIR MANADRHAGN ILTGKSEEGK TLLIPIDHGY
CLPENFEDCT FEWLYWPQAK LPFSADTIDY INSLDSEQDI ALLQLHGWNV PEAVSRTLRI
STMLLKKGVE RNLTPYQIGS VMCRETVNKD SAIEEIVREA HNSVLPASSE ATFLEAVSVA
MDRRLDELTK
