P4KG4_ARATH
ID P4KG4_ARATH Reviewed; 566 AA.
AC Q9ZPY9; B9DGU3; B9DHV3;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 4 {ECO:0000303|PubMed:17880284};
DE Short=AtPI4Kgamma4 {ECO:0000303|PubMed:17880284};
DE Short=PI-4Kgamma4 {ECO:0000303|PubMed:17880284};
DE Short=PI4K gamma 4 {ECO:0000303|PubMed:17880284};
DE EC=2.7.1.67 {ECO:0000269|PubMed:17880284};
DE AltName: Full=Ubiquitin-like domain kinase gamma 4 {ECO:0000303|PubMed:17880284};
DE Short=UbDK gamma 4 {ECO:0000303|PubMed:17880284};
GN Name=PI4KG4 {ECO:0000303|PubMed:17880284};
GN Synonyms=PI4KGAMMA4 {ECO:0000303|PubMed:17880284},
GN UBDKGAMMA4 {ECO:0000303|PubMed:17880284};
GN OrderedLocusNames=At2g46500 {ECO:0000312|Araport:AT2G46500};
GN ORFNames=F11C10.19 {ECO:0000312|EMBL:AAM15268.1},
GN F13A10.3 {ECO:0000312|EMBL:AAD20161.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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, INTERACTION WITH RPN10; UFD1 AND CDC48,
RP AUTOPHOSPHORYLATION, GENE FAMILY, AND MUTAGENESIS OF LYS-284.
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) (By similarity). Undergoes
CC autophosphorylation and phosphorylates serine/threonine residues of
CC protein substrates (PubMed:17880284). Phosphorylates RPN10 and UFD1 in
CC vitro (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 -!- SUBUNIT: Interacts with RPN10, UFD1 and CDC48 in vitro.
CC {ECO:0000269|PubMed:17880284}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23323832};
CC Peripheral membrane protein {ECO:0000269|PubMed:23323832}; Cytoplasmic
CC side {ECO:0000269|PubMed:23323832}.
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=Q9ZPY9-1; Sequence=Displayed;
CC -!- INDUCTION: By salt. {ECO:0000269|PubMed:23323832}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AC006418; AAD20161.1; -; Genomic_DNA.
DR EMBL; AC006526; AAM15268.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10708.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10709.1; -; Genomic_DNA.
DR EMBL; AF419566; AAL31898.1; -; mRNA.
DR EMBL; BT002694; AAO11610.1; -; mRNA.
DR EMBL; AK317284; BAH19960.1; -; mRNA.
DR EMBL; AK317659; BAH20320.1; -; mRNA.
DR PIR; F84903; F84903.
DR RefSeq; NP_566076.1; NM_130214.3. [Q9ZPY9-1]
DR RefSeq; NP_973700.1; NM_201971.3. [Q9ZPY9-1]
DR AlphaFoldDB; Q9ZPY9; -.
DR SMR; Q9ZPY9; -.
DR BioGRID; 4595; 5.
DR IntAct; Q9ZPY9; 1.
DR STRING; 3702.AT2G46500.1; -.
DR PaxDb; Q9ZPY9; -.
DR PRIDE; Q9ZPY9; -.
DR EnsemblPlants; AT2G46500.1; AT2G46500.1; AT2G46500. [Q9ZPY9-1]
DR EnsemblPlants; AT2G46500.2; AT2G46500.2; AT2G46500. [Q9ZPY9-1]
DR GeneID; 819260; -.
DR Gramene; AT2G46500.1; AT2G46500.1; AT2G46500. [Q9ZPY9-1]
DR Gramene; AT2G46500.2; AT2G46500.2; AT2G46500. [Q9ZPY9-1]
DR KEGG; ath:AT2G46500; -.
DR Araport; AT2G46500; -.
DR TAIR; locus:2039064; AT2G46500.
DR eggNOG; KOG0001; Eukaryota.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_023603_0_0_1; -.
DR InParanoid; Q9ZPY9; -.
DR OMA; IVAPQLN; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q9ZPY9; -.
DR PRO; PR:Q9ZPY9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPY9; baseline and differential.
DR Genevisible; Q9ZPY9; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
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 InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR45800; PTHR45800; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00240; ubiquitin; 2.
DR PRINTS; PR00348; UBIQUITIN.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..566
FT /note="Phosphatidylinositol 4-kinase gamma 4"
FT /id="PRO_0000423362"
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 255..547
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..267
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 407..415
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 430..456
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT BINDING 262..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 374..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT MUTAGEN 284
FT /note="K->A: Abolishes protein kinase activity."
FT /evidence="ECO:0000269|PubMed:17880284"
FT CONFLICT 170
FT /note="D -> G (in Ref. 4; BAH19960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 62625 MW; 84117C3F0914B685 CRC64;
MSSAGVALSP VRSEPLIMPL VRANSCLDSY PDDTIMIYLT LPGSVIPMRV LESDSIESVK
LRIQSYRGFV VRNQKLVFGG RELARSNSNM RDYGVSEGNI LHLVLKLSDL QVLDVKTTCG
KHCRFHVERG RNIGYVKKQI SKKRGDFVDP DEQEILYEGE KLEDQSLIND ICRNDDSVLH
LLVRRSAKVR VKPVEKNFEL SIVAPQAKDK KGREAKSIVP PKKLSLEPVV VNSKAKVPLV
VKDMIQSASD GLKSGNSPVR SSEGTGGAYF MQGPSGNKFV GVFKPIDEEP MAENNPQGLP
LSPNGEGLKK GTKVGEGALR EVAAYILDHP KSGNKSMFGE EIGFAGVPPT AMIECLHPGF
NHPKGIKTKI GSLQMFTEND GSCEDMGPLS FPVEEVHKIS VLDIRLANAD RHGGNILMTK
DESGKLVLVP IDHGYCLPES FEDCTFEWLY WPQARKPYSA ETQEYIRSLD AEEDIDLLKF
HGWKMPAETA QTLRISTMLL KKGVERGLTA FEIGTIMCRE TLSKKSLVEE MVEEAQEAVL
PGTSEAAFLE ALSDVMDYHL DHSQEH
