IPMK_SCHPO
ID IPMK_SCHPO Reviewed; 268 AA.
AC Q9US14;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Inositol polyphosphate multikinase {ECO:0000305};
DE Short=IPMK;
DE EC=2.7.1.127 {ECO:0000250|UniProtKB:P07250};
DE EC=2.7.1.151 {ECO:0000250|UniProtKB:P07250};
DE AltName: Full=Inositol polyphosphate kinase 2;
GN Name=arg82; ORFNames=SPAC607.04;
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] {ECO:0000312|EMBL:CAB63791.1}
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 [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9794810; DOI=10.1042/bj3350671;
RA Ongusaha P.P., Hughes P.J., Davey J., Michell R.H.;
RT "Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis from
RT Ins(1,4,5)P3 and osmotic regulation.";
RL Biochem. J. 335:671-679(1998).
RN [3]
RP FUNCTION.
RX PubMed=12828642; DOI=10.1046/j.1365-2958.2003.03562.x;
RA El Alami M., Messenguy F., Scherens B., Dubois E.;
RT "Arg82p is a bifunctional protein whose inositol polyphosphate kinase
RT activity is essential for nitrogen and PHO gene expression but not for
RT Mcm1p chaperoning in yeast.";
RL Mol. Microbiol. 49:457-468(2003).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Inositol phosphate kinase with both monophosphoinositol and
CC diphosphoinositol polyphosphate synthase activities. Able to
CC phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the
CC carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-
CC tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-
CC tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently
CC phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-
CC pentakisphosphate (Ins(1,3,4,5,6)P5). Also converts (Ins(1,3,4,5,6)P5)
CC to InsP6 (Probable). Has also a role in transcription regulation. The
CC catalytic activity is required for PHO gene repression by phosphate and
CC for NCR gene activation in response to nitrogen availability,
CC indicating a role for inositol pyrophosphates in these controls
CC (PubMed:12828642). Inositol polyphosphates may be involved in the
CC regulation of chromatin remodeling of transcription (By similarity).
CC {ECO:0000250|UniProtKB:P07250, ECO:0000269|PubMed:12828642,
CC ECO:0000305|PubMed:9794810}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol
CC 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151;
CC Evidence={ECO:0000305|PubMed:9794810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol
CC 1,4,5,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:17717,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9794810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17718;
CC Evidence={ECO:0000305|PubMed:9794810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127;
CC Evidence={ECO:0000305|PubMed:9794810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000305|PubMed:9794810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:11856, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57627, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:9794810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11857;
CC Evidence={ECO:0000305|PubMed:9794810};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000255}.
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DR EMBL; CU329670; CAB63791.1; -; Genomic_DNA.
DR PIR; T50224; T50224.
DR RefSeq; NP_593593.1; NM_001019024.2.
DR AlphaFoldDB; Q9US14; -.
DR SMR; Q9US14; -.
DR STRING; 4896.SPAC607.04.1; -.
DR MaxQB; Q9US14; -.
DR PaxDb; Q9US14; -.
DR EnsemblFungi; SPAC607.04.1; SPAC607.04.1:pep; SPAC607.04.
DR GeneID; 2543061; -.
DR KEGG; spo:SPAC607.04; -.
DR PomBase; SPAC607.04; arg82.
DR VEuPathDB; FungiDB:SPAC607.04; -.
DR eggNOG; KOG1620; Eukaryota.
DR HOGENOM; CLU_042569_1_1_1; -.
DR InParanoid; Q9US14; -.
DR OMA; SCDECNA; -.
DR PhylomeDB; Q9US14; -.
DR Reactome; R-SPO-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-SPO-1855191; Synthesis of IPs in the nucleus.
DR PRO; PR:Q9US14; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000824; F:inositol tetrakisphosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0051765; F:inositol tetrakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0008440; F:inositol-1,4,5-trisphosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0000823; F:inositol-1,4,5-trisphosphate 6-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; ISO:PomBase.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..268
FT /note="Inositol polyphosphate multikinase"
FT /id="PRO_0000318137"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07250"
FT BINDING 86..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07250"
FT BINDING 127..135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07250"
SQ SEQUENCE 268 AA; 30418 MW; 6352721D64EEC5B4 CRC64;
MKLKLFPFQA AGHGQVLVSE DDKILIKPCI KSEVDFYKTC NDNITLYNWI PKNFGEWMPS
SRDIEGINPI AESVAFSLTG KAIILENILY QMETPCVMDI KLGKQLWADD APLEKRKRLD
AVSRSTTSGS LGFRITGILS WDRTNNTYIK RSTAWGKTLT DSDVVEGLND FFVSCSLSQK
ARLVESFLNL LKLFEVDLSE SYIELKSSSI LFVYDYSSLN PTYHCESNVV LKLIDLAHSR
WTKNTIDHNT LIGVKNLIHC FAMLLKNE
