ITS3_SCHPO
ID ITS3_SCHPO Reviewed; 742 AA.
AC O13853;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase its3;
DE EC=2.7.1.68;
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase;
DE AltName: Full=Diphosphoinositide kinase;
DE AltName: Full=PIP5K;
DE AltName: Full=PtdIns(4)P-5-kinase;
GN Name=its3; ORFNames=SPAC19G12.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10950958; DOI=10.1074/jbc.m005575200;
RA Zhang Y., Sugiura R., Lu Y., Asami M., Maeda T., Itoh T., Takenawa T.,
RA Shuntoh H., Kuno T.;
RT "Phosphatidylinositol 4-phosphate 5-kinase Its3 and calcineurin Ppb1
RT coordinately regulate cytokinesis in fission yeast.";
RL J. Biol. Chem. 275:35600-35606(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 238-445, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9873063; DOI=10.1074/jbc.274.2.1147;
RA Vancurova I., Choi J.H., Lin H., Kuret J., Vancura A.;
RT "Regulation of phosphatidylinositol 4-phosphate 5-kinase from
RT Schizosaccharomyces pombe by casein kinase I.";
RL J. Biol. Chem. 274:1147-1155(1999).
CC -!- FUNCTION: Involved, together with the calcineurin ppb1, in cytokinesis.
CC {ECO:0000269|PubMed:10950958}.
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 -!- SUBCELLULAR LOCATION: Nucleus. Membrane; Peripheral membrane protein.
CC Note=The active form of the enzyme is membrane-associated and
CC concentrates at the septum in dividing cells.
CC -!- PTM: Phosphorylated by casein kinase I. Phosphorylation inactivates the
CC enzyme. {ECO:0000269|PubMed:9873063}.
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DR EMBL; CU329670; CAB10125.1; -; Genomic_DNA.
DR EMBL; AB027961; BAA87265.1; -; Genomic_DNA.
DR PIR; T38001; T38001.
DR RefSeq; NP_594429.1; NM_001019858.2.
DR AlphaFoldDB; O13853; -.
DR SMR; O13853; -.
DR BioGRID; 278704; 19.
DR STRING; 4896.SPAC19G12.14.1; -.
DR iPTMnet; O13853; -.
DR MaxQB; O13853; -.
DR PaxDb; O13853; -.
DR PRIDE; O13853; -.
DR EnsemblFungi; SPAC19G12.14.1; SPAC19G12.14.1:pep; SPAC19G12.14.
DR GeneID; 2542231; -.
DR KEGG; spo:SPAC19G12.14; -.
DR PomBase; SPAC19G12.14; its3.
DR VEuPathDB; FungiDB:SPAC19G12.14; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_1_1; -.
DR InParanoid; O13853; -.
DR OMA; HLWKGIN; -.
DR PhylomeDB; O13853; -.
DR Reactome; R-SPO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-SPO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-SPO-8847453; Synthesis of PIPs in the nucleus.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O13853; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0052811; F:1-phosphatidylinositol-3-phosphate 4-kinase activity; IMP:PomBase.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IGI:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IMP:PomBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; EXP:PomBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IMP:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.800.10; -; 1.
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; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..742
FT /note="Phosphatidylinositol 4-phosphate 5-kinase its3"
FT /id="PRO_0000185484"
FT DOMAIN 264..662
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 83748 MW; F0A3A8C668318970 CRC64;
MKIDSNGIVN PHSITNEIPS YDEKQAVDLN GNAFAPNGTF QKKDLISHKN DFERTMRHDV
LHTNPKIEVR SETHIYEPND SLFKENQDFP SNPTAHSPSS SSNDSVITAT GVPDGILRDS
PIVSALEPPS SNSSSSPQLQ NLKHQLSSPQ PSRAPIDRSS SNPVTSSQQP PNDRSTLSSS
QKAKRPLKRS YSEKNSSNAE PSGSRSGDRG TNVSTSGSLL DGIPPDIGSA SWAEAVKQKR
VNMRRRREEL DDECVLVGTR VSEGHENYVT AYNMLTGIRV GVSRCQAKMD RELTPADFTA
RHKFTFDITG NELTPSAKYD FKFKDYAPWV FRHLRQLFHL DAADYLVSLT SKYILSELDS
PGKSGSFFYF SRDYRFIIKT IHHSEHKFLR EILYDYYEHV KNNPNTLISQ FYGLHRVKLP
FGRKIHFVVM NNLFPPHRDI HQTFDLKGST LGRELDENQP CQSPMCTMKD TNWIRRNMHL
QFGPLKRQIF LTQVKADIDM LSSLGIMDYS LLVGIHDLSR GNRDKIRNSI LSVYDPNVSQ
HRVPSINGNE SHSNVHVIRQ VVNSTGPVSL DQSCNLLPTD QFVERRNFMF YSDDGGFQAT
DENNEPGNFI FYIGIIDLLT KYSYVKRVEH LWKGINHSDS VISAVPPAEY ASRFYKFVES
SIKPTLLVLK PFPLKPQDGQ RVNKQQSVNA GNVRTNNKHG SLNNNTAPSS RNAKSTSAHK
SPKTEHRFPF PCRNVTTNTS SS
