ID   IP6K3_MOUSE             Reviewed;         396 AA.
AC   Q8BWD2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Inositol hexakisphosphate kinase 3;
DE            Short=InsP6 kinase 3;
DE            EC=2.7.4.21;
DE   AltName: Full=Inositol hexaphosphate kinase 3;
GN   Name=Ip6k3; Synonyms=Ihpk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=11502751; DOI=10.1074/jbc.m106842200;
RA   Saiardi A., Nagata E., Luo H.R., Snowman A.M., Snyder S.H.;
RT   "Identification and characterization of a novel inositol hexakisphosphate
RT   kinase.";
RL   J. Biol. Chem. 276:39179-39185(2001).
CC   -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC       diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts
CC       1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity).
CC       {ECO:0000250}.
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; EC=2.7.4.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
CC         + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC         + ADP; Xref=Rhea:RHEA:37467, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:74946, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.21;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in cerebellum, brain cortex,
CC       kidney, thymus and lung. Detected at lower levels in hippocampus,
CC       testis, heart and olfactory bulb. {ECO:0000269|PubMed:11502751}.
CC   -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC       {ECO:0000305}.
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DR   EMBL; AK052857; BAC35176.1; -; mRNA.
DR   CCDS; CCDS28562.1; -.
DR   RefSeq; NP_766615.1; NM_173027.2.
DR   AlphaFoldDB; Q8BWD2; -.
DR   SMR; Q8BWD2; -.
DR   STRING; 10090.ENSMUSP00000025046; -.
DR   PhosphoSitePlus; Q8BWD2; -.
DR   PaxDb; 10090-ENSMUSP00000025046; -.
DR   Antibodypedia; 45687; 171 antibodies from 29 providers.
DR   DNASU; 271424; -.
DR   Ensembl; ENSMUST00000025046.4; ENSMUSP00000025046.3; ENSMUSG00000024210.4.
DR   GeneID; 271424; -.
DR   KEGG; mmu:271424; -.
DR   UCSC; uc008bfl.1; mouse.
DR   AGR; MGI:3045325; -.
DR   CTD; 117283; -.
DR   MGI; MGI:3045325; Ip6k3.
DR   VEuPathDB; HostDB:ENSMUSG00000024210; -.
DR   eggNOG; KOG1620; Eukaryota.
DR   GeneTree; ENSGT00940000160887; -.
DR   HOGENOM; CLU_014862_0_0_1; -.
DR   InParanoid; Q8BWD2; -.
DR   OMA; VYQADTG; -.
DR   OrthoDB; 20436at2759; -.
DR   PhylomeDB; Q8BWD2; -.
DR   TreeFam; TF314066; -.
DR   BRENDA; 2.7.4.21; 3474.
DR   Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR   BioGRID-ORCS; 271424; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q8BWD2; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8BWD2; Protein.
DR   Bgee; ENSMUSG00000024210; Expressed in hindlimb stylopod muscle and 34 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; ISO:MGI.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; ISO:MGI.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.470.160; Inositol polyphosphate kinase; 1.
DR   InterPro; IPR005522; IPK.
DR   InterPro; IPR038286; IPK_sf.
DR   PANTHER; PTHR12400:SF40; INOSITOL HEXAKISPHOSPHATE KINASE 3; 1.
DR   PANTHER; PTHR12400; INOSITOL POLYPHOSPHATE KINASE; 1.
DR   Pfam; PF03770; IPK; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   Genevisible; Q8BWD2; MM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..396
FT                   /note="Inositol hexakisphosphate kinase 3"
FT                   /id="PRO_0000066882"
FT   BINDING         206..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  44418 MW;  DB98CB79B4B36EE0 CRC64;
     MVVRHSSDKG KIGVGVPLEP FLHQVGGHLS VLQYDAYTVC KPLVSQEQKF YESLPLAMKC
     FTPKYKGTIT VRLRRDSRGH LGLVANPLKE NLEPFQVSPE SRAVALWQTL QQTTGSESSP
     CPLTQLARSL KESAAKVLLR SDCHLSTQAS PLVESEDGSQ VERKGFNPWG LHCHQAHLTR
     LCSQYPEDKR HRFLLLENVV SQYKQPCILD LKMGTRQHGD DASEEKKARH MKKCAQSTSA
     CLGVRICGMQ VYQTDQKSFL CKDKYYGRKL SVEGFRQALS QFLHDGTRLR AELLEPILRR
     LQALLTVIRS QSSYRFYSSS VLIIYDGEPP QTTQGSTSGG VTSGDPAKVD VRMIDFAHTT
     FKGSWNEHTT YEGPDPGYIF GLENLIGILR DIQEGE
//