P4KG4_ORYSJ
ID P4KG4_ORYSJ Reviewed; 565 AA.
AC Q6K881;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphatidylinositol 4-kinase gamma 4 {ECO:0000305};
DE Short=PI-4Kgamma4 {ECO:0000305};
DE Short=PI4K gamma 4 {ECO:0000305};
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:Q9BTU6};
DE AltName: Full=Ubiquitin-like domain kinase gamma 4 {ECO:0000303|PubMed:28254780};
DE Short=OsUbDKgamma4 {ECO:0000303|PubMed:28254780};
DE Short=UbDKgamma4 {ECO:0000303|PubMed:28254780};
GN Name=PI4KG4 {ECO:0000305};
GN OrderedLocusNames=Os02g0290500 {ECO:0000312|EMBL:BAF08505.1},
GN LOC_Os02g18840 {ECO:0000305};
GN ORFNames=OJ1086_G08.5 {ECO:0000312|EMBL:BAD21748.1},
GN OJ1756_H07.61 {ECO:0000312|EMBL:BAD21741.1},
GN OsJ_06315 {ECO:0000312|EMBL:EAZ22642.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, INTERACTION WITH FTIP1 AND RPN10, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28254780; DOI=10.1105/tpc.16.00728;
RA Song S., Chen Y., Liu L., Wang Y., Bao S., Zhou X., Teo Z.W., Mao C.,
RA Gan Y., Yu H.;
RT "OsFTIP1-mediated regulation of florigen transport in rice is negatively
RT regulated by the ubiquitin-like domain kinase OsUbDKgamma4.";
RL Plant Cell 29:491-507(2017).
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). Involved in the control of
CC flowering under long day conditions by promoting degradation of FTIP1
CC (PubMed:28254780). Recruits FTIP1 for degradation by the 26S proteasome
CC in leaves, which affects RFT1 transport to the shoot apical meristem
CC (SAM) (PubMed:28254780). {ECO:0000250|UniProtKB:Q9BTU6,
CC ECO:0000269|PubMed:28254780}.
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:0000250|UniProtKB:Q9BTU6};
CC -!- SUBUNIT: Interacts with FTIP1 and RPN10. {ECO:0000269|PubMed:28254780}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28254780}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:28254780}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the phloem including
CC companion cells. {ECO:0000269|PubMed:28254780}.
CC -!- DISRUPTION PHENOTYPE: Early flowering phenotype under long day
CC conditions. {ECO:0000269|PubMed:28254780}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AP004168; BAD21741.1; -; Genomic_DNA.
DR EMBL; AP004212; BAD21748.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08505.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS78188.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ22642.1; -; Genomic_DNA.
DR EMBL; AK065628; BAG89595.1; -; mRNA.
DR RefSeq; XP_015622865.1; XM_015767379.1.
DR AlphaFoldDB; Q6K881; -.
DR SMR; Q6K881; -.
DR STRING; 4530.OS02T0290500-01; -.
DR PaxDb; Q6K881; -.
DR PRIDE; Q6K881; -.
DR EnsemblPlants; Os02t0290500-01; Os02t0290500-01; Os02g0290500.
DR GeneID; 4329058; -.
DR Gramene; Os02t0290500-01; Os02t0290500-01; Os02g0290500.
DR KEGG; osa:4329058; -.
DR eggNOG; KOG0001; Eukaryota.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_023603_0_0_1; -.
DR InParanoid; Q6K881; -.
DR OMA; HMGKGSK; -.
DR OrthoDB; 1273723at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6K881; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0048579; P:negative regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Flowering; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Transferase.
FT CHAIN 1..565
FT /note="Phosphatidylinositol 4-kinase gamma 4"
FT /id="PRO_0000445342"
FT DOMAIN 32..104
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 109..187
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 257..542
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 291..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..410
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 425..451
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 369..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
SQ SEQUENCE 565 AA; 61806 MW; 62C22BFE8535F3EF CRC64;
MSSAGIATLS PLLDQFCFAP HGEPRLQQLD SIVIFLAMPG VAPMPMRVLH SDSVASVKLR
IQQFKGFVTT KQRLVFSGHE LSLNNSHVRD YGLTDGNVLH LVVRLADLRA ISIETANGKK
FQFQVESCCN VGYLKDKLSA ESGQQLGSLK DQRLVFDGEE LEDNQLIADI SKKGAAVIHL
FIRRPAKVQT QQGDKETVVT VVTPKDNDNL QTDALNLAKP AKGKPAPVEP IIANGKVKLS
PAVMEMIYST ISGIENGYLP VMSTEGSGGV YFMKDSSGES NVAVFKPIDE EPMAKNNPRG
LPLSTDGEGL KRGTRVGEGA LREVAAYILD HPVYGCKSCD VPGFSGVPPT ALVRCFHMGK
GSNKVGSLQL FVDNNGSCED MGPRAFPVKE VQKIAILDIR LANADRHAGN ILVCQDGEDH
LKLIPIDHGY CLPEKFEDCT FEWLYWPQAR EPFGPETAAY IGSLDADKDI ALLKFHGWAL
SPQCARVLRI STMLLKKGAE RGLTPYDIGS ILCRQTVKKE SEIEAIIEEA EDAILPGTSE
ETFLETISEI MDFHLDKLAV KLKKF
