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   27-MAR-2024, entry version 145.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9SUI2; -.
DR   iPTMnet; Q9SUI2; -.
DR   PaxDb; 3702-AT1G10900-1; -.
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; AT1G10900; -.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   InParanoid; Q9SUI2; -.
DR   OMA; MWTDGAL; -.
DR   OrthoDB; 340426at2759; -.
DR   PhylomeDB; Q9SUI2; -.
DR   BioCyc; ARA:AT1G10900-MONOMER; -.
DR   PRO; PR:Q9SUI2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SUI2; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd17302; PIPKc_AtPIP5K_like; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR   InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR   InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR   PANTHER; PTHR23086:SF104; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 7; 1.
DR   PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 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   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS51455; PIPK; 1.
DR   Genevisible; Q9SUI2; AT.
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
//