PI5K7_ARATH
ID PI5K7_ARATH Reviewed; 754 AA.
AC Q9SUI2; O04095;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 7;
DE Short=AtPIP5K7;
DE EC=2.7.1.68;
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 7;
DE AltName: Full=Diphosphoinositide kinase 7;
DE Short=AtP5K2;
DE AltName: Full=PtdIns(4)P-5-kinase 7;
GN Name=PIP5K7; Synonyms=P5K2; OrderedLocusNames=At1g10900;
GN ORFNames=T19D16.18;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RA Elge S., Mueller-Roeber B.;
RT "Molecular aspects of AtP5K2 in stomatal guard cells a phosphatidyinositol-
RT 4-phosphate 5-kinase.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65487.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ009782; CAB53377.1; -; mRNA.
DR EMBL; U95973; AAB65487.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28661.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60004.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60005.1; -; Genomic_DNA.
DR EMBL; AY062718; AAL32796.1; -; mRNA.
DR EMBL; BT010342; AAQ56785.1; -; mRNA.
DR PIR; G86242; G86242.
DR RefSeq; NP_001322318.1; NM_001331939.1.
DR RefSeq; NP_001322319.1; NM_001331940.1.
DR RefSeq; NP_172559.2; NM_100965.5.
DR AlphaFoldDB; Q9SUI2; -.
DR SMR; Q9SUI2; -.
DR STRING; 3702.AT1G10900.1; -.
DR iPTMnet; Q9SUI2; -.
DR PaxDb; Q9SUI2; -.
DR PRIDE; Q9SUI2; -.
DR ProteomicsDB; 235019; -.
DR EnsemblPlants; AT1G10900.1; AT1G10900.1; AT1G10900.
DR EnsemblPlants; AT1G10900.2; AT1G10900.2; AT1G10900.
DR EnsemblPlants; AT1G10900.3; AT1G10900.3; AT1G10900.
DR GeneID; 837633; -.
DR Gramene; AT1G10900.1; AT1G10900.1; AT1G10900.
DR Gramene; AT1G10900.2; AT1G10900.2; AT1G10900.
DR Gramene; AT1G10900.3; AT1G10900.3; AT1G10900.
DR KEGG; ath:AT1G10900; -.
DR Araport; AT1G10900; -.
DR TAIR; locus:2197454; AT1G10900.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; Q9SUI2; -.
DR OMA; KHGMGTM; -.
DR OrthoDB; 271548at2759; -.
DR PhylomeDB; Q9SUI2; -.
DR BioCyc; ARA:AT1G10900-MON; -.
DR PRO; PR:Q9SUI2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SUI2; baseline and differential.
DR Genevisible; Q9SUI2; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF02493; MORN; 8.
DR Pfam; PF01504; PIP5K; 1.
DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1.
DR SMART; SM00698; MORN; 8.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..754
FT /note="Phosphatidylinositol 4-phosphate 5-kinase 7"
FT /id="PRO_0000185479"
FT REPEAT 16..38
FT /note="MORN 1"
FT REPEAT 39..61
FT /note="MORN 2"
FT REPEAT 62..84
FT /note="MORN 3"
FT REPEAT 85..107
FT /note="MORN 4"
FT REPEAT 108..130
FT /note="MORN 5"
FT REPEAT 131..153
FT /note="MORN 6"
FT REPEAT 154..176
FT /note="MORN 7"
FT REPEAT 177..198
FT /note="MORN 8"
FT DOMAIN 329..750
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 710..731
FT /note="Activation loop"
FT /evidence="ECO:0000250"
SQ SEQUENCE 754 AA; 85955 MW; D2310E6AABBA4F00 CRC64;
MDMRSGDREF PNGDFYSGEV KGIIPNGKGK YAWSDGTIYE GDWDEGKISG KGKLIWSSGA
KYEGDFSGGY LHGFGTMTSP DESVYSGAWR MNVRHGLGRK EYCNSDLYDG LWKEGLQDGR
GSYSWTNGNR YIGNWKKGKM CERGVMRWEN GDLYDGFWLN GFRHGSGVYK FADGCLYYGT
WSRGLKDGKG VFYPAGTKQP SLKKWCRSLE YDDTGKFVLS RSASVNVEEL RSLNTVTQSL
SVKTSAGETT CDPPRDFTCH GPVSKSARFS GSGQSEGQDK NRIVYEREYM QGVLIRETIM
SSVDRSHKIK PPNRPREVRA RSLMTFLRGE HNYYLMLNLQ LGIRYTVGKI TPVPRREVRA
SDFGKNARTK MFFPRDGSNF TPPHKSVDFS WKDYCPMVFR NLRQMFKLDA AEYMMSICGD
DGLTEISSPG KSGSIFYLSH DDRFVIKTLK KSELQVLLRM LPKYYEHVGD HENTLITKFF
GVHRITLKWG KKVRFVVMGN MFCTELKIHR RYDLKGSTQG RFTEKIKIQE KTTLKDLDLA
YEFHMDKLLR EALFKQIYLD CSFLESLNII DYSLLLGLHF RAPGQLNDIL EPPNAMSDQE
SVSSVDVGLT QEHSIPPKGL LLVTHEPNSV NTAPGPHIRG STLRAFSVGE QEVDLILPGT
ARLRVQLGVN MPAQAHHKLI EDKEESATIE LFEVYDVVVY MGIIDILQEY NTKKKVEHTC
KSLQYDPMTI SVTEPSTYSK RFVNFLHKVF PEER
