IP3KC_MOUSE
ID IP3KC_MOUSE Reviewed; 678 AA.
AC Q7TS72; Q3U384;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Inositol-trisphosphate 3-kinase C;
DE EC=2.7.1.127;
DE AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase C;
DE Short=IP3 3-kinase C;
DE Short=IP3K C;
DE Short=InsP 3-kinase C;
GN Name=Itpkc;
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=NOD;
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 TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-
CC trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate
CC and participates to the regulation of calcium homeostasis (By
CC similarity). Can phosphorylate inositol 2,4,5-triphosphate to inositol
CC 2,4,5,6-tetraphosphate (By similarity). {ECO:0000250|UniProtKB:Q80ZG2,
CC ECO:0000250|UniProtKB:Q96DU7}.
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:0000250|UniProtKB:Q96DU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000250|UniProtKB:Q96DU7};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin. Inhibited by high
CC concentrations of the substrate Ins(1,2,4)P3, and allosterically
CC activated by the product Ins(1,3,4,5)P4.
CC {ECO:0000250|UniProtKB:Q96DU7}.
CC -!- INTERACTION:
CC Q7TS72; O54824: Il16; NbExp=3; IntAct=EBI-648015, EBI-641708;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DU7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96DU7}. Note=Shuttles actively between nucleus
CC and cytoplasm with both nuclear import and nuclear export activity.
CC {ECO:0000250|UniProtKB:Q80ZG2}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AK154888; BAE32904.1; -; mRNA.
DR EMBL; BC053450; AAH53450.1; -; mRNA.
DR CCDS; CCDS21015.1; -.
DR RefSeq; NP_853624.1; NM_181593.2.
DR AlphaFoldDB; Q7TS72; -.
DR SMR; Q7TS72; -.
DR IntAct; Q7TS72; 1.
DR STRING; 10090.ENSMUSP00000003850; -.
DR iPTMnet; Q7TS72; -.
DR PhosphoSitePlus; Q7TS72; -.
DR EPD; Q7TS72; -.
DR MaxQB; Q7TS72; -.
DR PaxDb; Q7TS72; -.
DR PeptideAtlas; Q7TS72; -.
DR PRIDE; Q7TS72; -.
DR ProteomicsDB; 268983; -.
DR Antibodypedia; 30626; 190 antibodies from 31 providers.
DR DNASU; 233011; -.
DR Ensembl; ENSMUST00000003850; ENSMUSP00000003850; ENSMUSG00000003752.
DR GeneID; 233011; -.
DR KEGG; mmu:233011; -.
DR UCSC; uc009fvk.1; mouse.
DR CTD; 80271; -.
DR MGI; MGI:2442554; Itpkc.
DR VEuPathDB; HostDB:ENSMUSG00000003752; -.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000160033; -.
DR HOGENOM; CLU_017767_5_0_1; -.
DR InParanoid; Q7TS72; -.
DR OMA; WADNLWT; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; Q7TS72; -.
DR TreeFam; TF318394; -.
DR BRENDA; 2.7.1.127; 3474.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR BioGRID-ORCS; 233011; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Itpkc; mouse.
DR PRO; PR:Q7TS72; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TS72; protein.
DR Bgee; ENSMUSG00000003752; Expressed in lip and 191 other tissues.
DR Genevisible; Q7TS72; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0008440; F:inositol-1,4,5-trisphosphate 3-kinase activity; IDA:MGI.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
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; Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..678
FT /note="Inositol-trisphosphate 3-kinase C"
FT /id="PRO_0000234071"
FT REGION 26..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..512
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT MOTIF 318..326
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 171..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 466..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 502..508
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 529..536
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96DU7"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DU7"
FT CONFLICT 458
FT /note="D -> N (in Ref. 1; BAE32904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 678 AA; 74493 MW; 0D3705B3D682B6ED CRC64;
MRRCPCRGSL SEAEAGALPA EARMGLEALR GGRRRQPGLQ RPGPGAGGPT GRPEGGGPRA
WIEESSLHSE AERTDLEPAP CPNGPQAESC GDGHAECEAA GLVVASEKPR QNKELDGSNL
QTHPRRNSPL VEMEMAGSWT DGFRTDLHRS DLQSRPKRAS LCTQPGFDES WTELDRSDMW
QTLPERDNKP RVDNLRTHHG VSKLQTHPVC LSPESSADNS GKELSADASR TPHDTDGFWI
ESQTDDSLKG PSTQTACRQP GSDGFSSKDT ESALTQPGTD GLRDDSVLGE SNGNDPLDLS
EPGELVTNLC SHLECSSLCP VPRLIITPET PEPEAQPVGP QSRIEGGTGG FSSASSFDES
EDDLVAGGGG TSDPEDRAGS KPWKKLKTVL KYSPFVVSFH KHYYPWVQLS GHAGNFQAGE
DGRILKRFCQ CEQRSLELLM GDPLRPFVPA YYGMVQRDGQ AFNQMEDLLA DFEGPSIMDC
KMGSRTYLEE ELVKARERPK PRKDMYEKMV AVDPGAPTPE EHAQGAITKP RYMQWRETLS
STSTLGFRIE GIKKADGTCN TNFKKTQALE QVTKVLEDFV NGDLGILRKY VARLEDLRET
LENSPFFKTH EVVGSSLLFV HDHTGLAKVW MIDFGKTVAL PDHQMLSHRL PWTEGNREDG
YLWGLDNLIC LLQGLAQS
