IPPK_MOUSE
ID IPPK_MOUSE Reviewed; 489 AA.
AC Q6P1C1; Q3V3Z0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE EC=2.7.1.158;
DE AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE Short=InsP5 2-kinase;
GN Name=Ippk;
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=Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15939868; DOI=10.1073/pnas.0503656102;
RA Verbsky J., Lavine K., Majerus P.W.;
RT "Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2-kinase
RT gene, associated lethality, and tissue distribution of 2-kinase
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8448-8453(2005).
CC -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many
CC processes such as mRNA export, non-homologous end-joining, endocytosis,
CC ion channel regulation. It also protects cells from TNF-alpha-induced
CC apoptosis. {ECO:0000269|PubMed:15939868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In brain, it is expressed throughout the
CC hippocampus (CA1, CA2, CA3 and dentate gyrus), inner layers of the
CC cerebral cortex, and Purkinje cells of the cerebellum. In heart, it is
CC expressed in cardiomyocytes but not in interstitial cells, blood
CC vessels, or valves. Also expressed in testis.
CC {ECO:0000269|PubMed:15939868}.
CC -!- DEVELOPMENTAL STAGE: In 9 dpc embryos it is expressed in regions
CC corresponding to the neural tube, notochord and somites. Through the
CC neural tube, it is expressed in the ventricular zone and in migrating
CC neuroblasts. Also expressed in the notochord and specific regions of
CC the somite. Strongly expressed in the myotome (future skeletal muscle)
CC of the somite. In addition to the neural tube, it is also expressed in
CC the ventricular zone and migrating neuroblasts throughout the embryonic
CC brain. Prominent expression is detected in the yolk sac and embryonic
CC heart. Within the yolk sac, it is expressed in both the epithelial and
CC endothelial layers (blood vessels) but absent from the blood islands.
CC In the heart, it is detected in both the atrial and ventricular
CC chambers. In the ventricular myocardium it is present in both the
CC endocardium and myocardium. Also expressed in the cardinal vein, aorta,
CC digestive tract, and pharyngeal arches.
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2.
CC -!- DISRUPTION PHENOTYPE: Death during ermbryogenesis before 8.5 dpc,
CC suggesting that InsP6 is required for yolk sac function and
CC development. {ECO:0000269|PubMed:15939868}.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
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DR EMBL; AK029085; BAE20447.1; -; mRNA.
DR EMBL; AK160092; BAE35623.1; -; mRNA.
DR EMBL; AK167467; BAE39551.1; -; mRNA.
DR EMBL; BC062167; AAH62167.1; -; mRNA.
DR EMBL; BC065157; AAH65157.1; -; mRNA.
DR CCDS; CCDS26500.1; -.
DR RefSeq; NP_951011.1; NM_199056.3.
DR PDB; 5MW8; X-ray; 2.40 A; A=1-468.
DR PDB; 5MWL; X-ray; 3.20 A; A/B=1-468.
DR PDB; 5MWM; X-ray; 2.60 A; A=1-468.
DR PDBsum; 5MW8; -.
DR PDBsum; 5MWL; -.
DR PDBsum; 5MWM; -.
DR AlphaFoldDB; Q6P1C1; -.
DR SMR; Q6P1C1; -.
DR BioGRID; 217663; 6.
DR STRING; 10090.ENSMUSP00000021817; -.
DR iPTMnet; Q6P1C1; -.
DR PhosphoSitePlus; Q6P1C1; -.
DR EPD; Q6P1C1; -.
DR PaxDb; Q6P1C1; -.
DR PRIDE; Q6P1C1; -.
DR ProteomicsDB; 269499; -.
DR Antibodypedia; 13762; 116 antibodies from 25 providers.
DR DNASU; 75678; -.
DR Ensembl; ENSMUST00000220447; ENSMUSP00000152331; ENSMUSG00000021385.
DR GeneID; 75678; -.
DR KEGG; mmu:75678; -.
DR UCSC; uc007qjj.2; mouse.
DR CTD; 64768; -.
DR MGI; MGI:1922928; Ippk.
DR VEuPathDB; HostDB:ENSMUSG00000021385; -.
DR eggNOG; KOG4749; Eukaryota.
DR GeneTree; ENSGT00390000010053; -.
DR HOGENOM; CLU_033188_1_0_1; -.
DR InParanoid; Q6P1C1; -.
DR OMA; NCVHCGE; -.
DR PhylomeDB; Q6P1C1; -.
DR TreeFam; TF106142; -.
DR BRENDA; 2.7.1.158; 3474.
DR Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-MMU-1855191; Synthesis of IPs in the nucleus.
DR BioGRID-ORCS; 75678; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Ippk; mouse.
DR PRO; PR:Q6P1C1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6P1C1; protein.
DR Bgee; ENSMUSG00000021385; Expressed in primary oocyte and 241 other tissues.
DR ExpressionAtlas; Q6P1C1; baseline and differential.
DR Genevisible; Q6P1C1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; ISS:HGNC-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0052746; P:inositol phosphorylation; ISS:BHF-UCL.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR Gene3D; 3.30.200.110; -; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; PTHR14456; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..489
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110530"
FT MOTIF 136..140
FT /note="EXKPK motif"
FT CONFLICT 83
FT /note="E -> Q (in Ref. 1; BAE20447)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 18..37
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:5MWL"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5MWL"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5MWL"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 333..349
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:5MW8"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:5MW8"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5MW8"
FT HELIX 446..463
FT /evidence="ECO:0007829|PDB:5MW8"
SQ SEQUENCE 489 AA; 55928 MW; 441839EA3F425D5A CRC64;
MEEGKMDENE WSYHGEGNKS LVVAHAQRCV VLRFLKFPPN KKKTSEEILQ HLQNIVDFGK
NVMKDFLGEN YVHCGEVVQL PLEFVKQLCL KIQCERPESR CDKDLDTFSG YAMCLPNLTR
LQTFHFAEHR PILCVEIKPK CGFIPFSNDV THEMKHKVCR YCMHQHLKVA TGKWKKISKY
CPLDLYSGNK QRMHFALRSL LQETQNNLRI FKNGELIYGC GDARSPVADL KELAHHLKPF
FFPSNGLASG PHCTKAVIRE LVHVITRVLL SSSEKARAGA LRLGLQGPRV CEASPFSRSL
HNQGKNTSEH SGLPKGCLLY KTLQVQMLDQ LDIEGLYPLY KRVEQYLEEF PEERKTLQID
GPYDEVFYQK LLDLSTEDDG TVAFALTKVQ QYRVAMTAKD CSIMIALSPC LQGTSSDQRP
VIPSSRSRLA FSVSVLDLDL KPYESIPHQY KLDSKIVNYY SKTVHAKDDT VRSTRFKEHE
DCTLVLHKV
