ID   IP6K2_RAT               Reviewed;         425 AA.
AC   Q9R0U1; Q5XIU6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Inositol hexakisphosphate kinase 2;
DE            Short=InsP6 kinase 2;
DE            EC=2.7.4.- {ECO:0000250|UniProtKB:Q9UHH9};
DE   AltName: Full=P(i)-uptake stimulator {ECO:0000303|PubMed:10527952};
DE            Short=PiUS {ECO:0000303|PubMed:10527952};
GN   Name=Ip6k2; Synonyms=Ihpk2, Pius;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Small intestine;
RX   PubMed=10527952; DOI=10.1042/bj3430705;
RA   Katai K., Miyamoto K., Kishida S., Segawa H., Nii T., Tanaka H., Tani Y.,
RA   Arai H., Tatsumi S., Morita K., Taketani Y., Takeda E.;
RT   "Regulation of intestinal Na+-dependent phosphate co-transporters by a low-
RT   phosphate diet and 1,25-dihydroxyvitamin D3.";
RL   Biochem. J. 343:705-712(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC       diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
CC       {ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC         inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC         ChEBI:CHEBI:456216;
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC       {ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHH9}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in small intestine.
CC       {ECO:0000269|PubMed:10527952}.
CC   -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was first identified because of its ability to stimulate
CC       Na(+)-dependent phosphate cotransport. {ECO:0000269|PubMed:10527952}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA87611.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR   EMBL; AB015723; BAA87611.1; ALT_SEQ; mRNA.
DR   EMBL; BC083574; AAH83574.1; -; mRNA.
DR   RefSeq; NP_067692.2; NM_021660.2.
DR   RefSeq; XP_008764786.1; XM_008766564.2.
DR   AlphaFoldDB; Q9R0U1; -.
DR   SMR; Q9R0U1; -.
DR   STRING; 10116.ENSRNOP00000027584; -.
DR   PhosphoSitePlus; Q9R0U1; -.
DR   PaxDb; 10116-ENSRNOP00000027584; -.
DR   Ensembl; ENSRNOT00000077078.2; ENSRNOP00000071056.1; ENSRNOG00000020361.8.
DR   GeneID; 59268; -.
DR   KEGG; rno:59268; -.
DR   UCSC; RGD:620529; rat.
DR   AGR; RGD:620529; -.
DR   CTD; 51447; -.
DR   RGD; 620529; Ip6k2.
DR   eggNOG; KOG1620; Eukaryota.
DR   GeneTree; ENSGT00940000156310; -.
DR   InParanoid; Q9R0U1; -.
DR   OrthoDB; 20436at2759; -.
DR   PhylomeDB; Q9R0U1; -.
DR   Reactome; R-RNO-1855191; Synthesis of IPs in the nucleus.
DR   UniPathway; UPA00949; -.
DR   PRO; PR:Q9R0U1; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000020361; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0097243; F:flavonoid binding; ISS:UniProtKB.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; ISO:RGD.
DR   GO; GO:1905396; P:cellular response to flavonoid; ISS:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; ISO:RGD.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR   GO; GO:0006817; P:phosphate ion transport; IDA:RGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISO:RGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   Gene3D; 3.30.470.160; Inositol polyphosphate kinase; 1.
DR   InterPro; IPR005522; IPK.
DR   InterPro; IPR038286; IPK_sf.
DR   PANTHER; PTHR12400:SF47; INOSITOL HEXAKISPHOSPHATE KINASE 2; 1.
DR   PANTHER; PTHR12400; INOSITOL POLYPHOSPHATE KINASE; 1.
DR   Pfam; PF03770; IPK; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   Genevisible; Q9R0U1; RN.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Lipid metabolism; Nucleotide-binding; Nucleus;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..425
FT                   /note="Inositol hexakisphosphate kinase 2"
FT                   /id="PRO_0000066880"
FT   BINDING         206..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         215..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         235..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFU5"
SQ   SEQUENCE   425 AA;  49164 MW;  6E44C1D3D6EA7FD8 CRC64;
     MSPAFRTMDV EPRTKGILLE PFVHQVGGHS CVLRFNETTL CKPLVPREHQ FYETLPAEMR
     RFTPQYKGVV SVRFEEDEDR NLCLIAYPLK GDHGPVDIVD NSDCEPKSKL LRWTNKKHHV
     LETEKSPKDW VRQHRKEEKM KSHKLEEEFE WLKKSEVLYY SVEKKGTVSS QLKHYNPWSM
     KCHQQQLQRM KENAKHRNQY KFILLENLTC RYEVPCVLDL KMGTRQHGDD ASEEKAANQI
     RKCQQSTSAV IGVRVCGMQV YQAGTGQLMF MNKYHGRKLS VQGFKEALFQ FFHNGRYLRR
     ELLGPVLKKL TELKAVLERQ ESYRFYSSSL LVIYDGKEWP EVTLDSDAED LEDLSEESAD
     ESAGAYAYKP LGASSVDVRM IDFAHTTCRL YGEDSVVHEG QDAGYIFGLQ SLIDIVTEIS
     EESGE
//