PI5K8_ARATH
ID PI5K8_ARATH Reviewed; 769 AA.
AC Q8RY89; Q9C962;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 8;
DE Short=AtPIP5K8;
DE EC=2.7.1.68;
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 8;
DE AltName: Full=Diphosphoinositide kinase 8;
DE AltName: Full=PtdIns(4)P-5-kinase 8;
GN Name=PIP5K8; OrderedLocusNames=At1g60890; ORFNames=T7P1.4;
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].
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 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 [5]
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 -!- 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=Q8RY89-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51639.1; 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; AC018908; AAG51639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33744.1; -; Genomic_DNA.
DR EMBL; AY074507; AAL69491.1; -; mRNA.
DR EMBL; AY133824; AAM91758.1; -; mRNA.
DR PIR; D96634; D96634.
DR RefSeq; NP_176286.2; NM_104770.5. [Q8RY89-1]
DR AlphaFoldDB; Q8RY89; -.
DR SMR; Q8RY89; -.
DR BioGRID; 27605; 1.
DR STRING; 3702.AT1G60890.2; -.
DR iPTMnet; Q8RY89; -.
DR PaxDb; Q8RY89; -.
DR PRIDE; Q8RY89; -.
DR ProteomicsDB; 234956; -. [Q8RY89-1]
DR EnsemblPlants; AT1G60890.1; AT1G60890.1; AT1G60890. [Q8RY89-1]
DR GeneID; 842381; -.
DR Gramene; AT1G60890.1; AT1G60890.1; AT1G60890. [Q8RY89-1]
DR KEGG; ath:AT1G60890; -.
DR Araport; AT1G60890; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; Q8RY89; -.
DR OMA; CSINFYW; -.
DR PhylomeDB; Q8RY89; -.
DR BioCyc; ARA:AT1G60890-MON; -.
DR PRO; PR:Q8RY89; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY89; baseline and differential.
DR Genevisible; Q8RY89; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..769
FT /note="Phosphatidylinositol 4-phosphate 5-kinase 8"
FT /id="PRO_0000185480"
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 344..765
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 266..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..746
FT /note="Activation loop"
FT /evidence="ECO:0000250"
SQ SEQUENCE 769 AA; 87403 MW; 2E8A045211FB39A3 CRC64;
METRPAERVF SNGDVYSGQL KGTLPHGKGK YAWPDGIIYE GDWEEGKISG RGKLMWSSGA
KYEGDFSGGY LHGFGTLTSP DGSVYAGAWR MNVRHGLGRK EYCNSDVYDG SWREGLQDGS
GSYSWYNGNR FIGNWKKGKM SGRGVMSWAN GDLFNGFWLN GLRHGSGVYK YADGGFYFGT
WSRGLKDGSG VFYPAGSKHP SLKKWHRHFG YDDTGNFLLS HNSTINIDDL RTSKAVSRSL
SELTTTSGLT RTSERYPDDY WSTSDPPRDF MHHGPSSKSA RSVDSGQSEI RDKNPIVFER
EYMQGVLIKE RIMSSIDMSH RARPLNLTKE VTVSACVSFL GGKWNHYLML NLQLGIRYTV
GKITPVPPRE VRASDFSERA RIMMFFPRNG SQYTPPHKSI DFDWKDYCPM VFRNLREMFK
LDAADYMMSI CGDDGLREIS SPGKSGSIFY LSHDDRFVIK TLKRSELKVL LRMLPRYYEH
VGDYENTLIT KFFGVHRIKL KWGKKVRFVV MGNMFCTELK IHRRYDLKGS TQGRYTEKNK
IGEKTTLKDL DLAYEFHMDK LLREALFKQI ILDCSFLESL QILDYSLLLG LHFRAPDPLT
DILEPPNEMS DQESDSVGSV DVNLPREPSI PPKGLLMVTH EPNSVNTAPG PHIRGSTLRA
FSVGEKEVDL ILPGTARLRV QLGVNMPAQA HHKLGQDNEE SGTVELFEVY DVVVYMGIID
ILQEYNMKKK VEHTCKSMKY DPMTISAIEP TLYSKRFIDF LLKVFPEKA
