IP3KC_RAT
ID IP3KC_RAT Reviewed; 678 AA.
AC Q80ZG2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Inositol-trisphosphate 3-kinase C;
DE EC=2.7.1.127 {ECO:0000269|PubMed:12649294};
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; Synonyms=Ip3kc;
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], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF 318-LEU--VAL-321 AND
RP 318-LEU--ILE-326, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=Wistar; TISSUE=Circumvallate papilla;
RX PubMed=12649294; DOI=10.1074/jbc.m211059200;
RA Nalaskowski M.M., Bertsch U., Fanick W., Stockebrand M.C., Schmale H.,
RA Mayr G.W.;
RT "Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized
RT for basal cellular inositol trisphosphate phosphorylation and shuttles
RT actively between nucleus and cytoplasm.";
RL J. Biol. Chem. 278:19765-19776(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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
CC (PubMed:12649294). Can phosphorylate inositol 2,4,5-triphosphate to
CC inositol 2,4,5,6-tetraphosphate. {ECO:0000269|PubMed:12649294}.
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:0000269|PubMed:12649294};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000269|PubMed:12649294};
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. {ECO:0000269|PubMed:12649294}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for Ins(1,4,5)P3 {ECO:0000269|PubMed:12649294};
CC KM=1.5 uM for Ins(2,4,5)P3 {ECO:0000269|PubMed:12649294};
CC KM=33 uM for ATP {ECO:0000269|PubMed:12649294};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12649294}. Cytoplasm
CC {ECO:0000269|PubMed:12649294}. Note=Shuttles actively between nucleus
CC and cytoplasm with both nuclear import and nuclear export activity.
CC -!- TISSUE SPECIFICITY: Highly expressed in tongue epithelium, taste
CC papilla, heart, brain and testis. Weakly expressed in lung, liver and
CC kidney. {ECO:0000269|PubMed:12649294}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AY160770; AAO20335.1; -; mRNA.
DR EMBL; AJ440782; CAD29464.1; -; mRNA.
DR RefSeq; NP_835195.1; NM_178094.3.
DR AlphaFoldDB; Q80ZG2; -.
DR SMR; Q80ZG2; -.
DR STRING; 10116.ENSRNOP00000018696; -.
DR BindingDB; Q80ZG2; -.
DR ChEMBL; CHEMBL2667; -.
DR CarbonylDB; Q80ZG2; -.
DR iPTMnet; Q80ZG2; -.
DR PhosphoSitePlus; Q80ZG2; -.
DR jPOST; Q80ZG2; -.
DR PaxDb; Q80ZG2; -.
DR PRIDE; Q80ZG2; -.
DR Ensembl; ENSRNOT00000100648; ENSRNOP00000084385; ENSRNOG00000013945.
DR GeneID; 308451; -.
DR KEGG; rno:308451; -.
DR UCSC; RGD:631336; rat.
DR CTD; 80271; -.
DR RGD; 631336; Itpkc.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000160033; -.
DR HOGENOM; CLU_017767_5_0_1; -.
DR InParanoid; Q80ZG2; -.
DR OMA; WADNLWT; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; Q80ZG2; -.
DR TreeFam; TF318394; -.
DR BRENDA; 2.7.1.127; 5301.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SABIO-RK; Q80ZG2; -.
DR PRO; PR:Q80ZG2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013945; Expressed in esophagus and 20 other tissues.
DR Genevisible; Q80ZG2; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IDA:RGD.
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_0000234072"
FT REGION 25..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..381
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 COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..274
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:0000250|UniProtKB:Q7TS72"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DU7"
FT MUTAGEN 318..326
FT /note="Missing: No export in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:12649294"
FT MUTAGEN 318..321
FT /note="LCPV->ACPA: No export in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:12649294"
SQ SEQUENCE 678 AA; 74463 MW; 5EDEA14255DACD2B CRC64;
MRRCPCRGSL SEAEAGALPA EARMGLEALR GGRRRQPGLQ RPGPGAGGPT GRPEGGGPRA
WIEGFSLHSE AERTDFGPAP CPDGPQAEPC GDEHEECEAA GLGVASEKPS QNKELDGSNL
QTHPKLSSPL AEMEMAGSWT DGFRTDLHRP DLQARPKRAS LCTQPGFDES WTELDRSELW
QTLPERDKPW VDHLRTHQDM SRLQNHPACP SPEPSAGTSC KELSADGSRT PHDTDGFWIE
SQTDGSLIGP STQTACRQPA NDGFSAQDTD GTLIQPGTDD GPWVDSVLEK SNGDDPLMEP
EPRDLVTNLC SHLECSSLCP VPRLIITSES PEPGAQPLGP QARIEGGTGG FSSASSFDES
EDDLVAGGGG TSDPEDRSGS KPWKKLKTVL KYSPFVVSFH KHYYPWVQLS GHAGNFQAGE
DGRILKRFCQ CEQRSLELLM GDPLRPFVPT YYGMVQRDGQ AFNQMEDLLA DFEGPSIMDC
KMGSRTYLEE ELVKARERPK PRKDMYEKMV AVDPGAPTPE EHAQGAVTKP RYMQWRETLS
STSTLGFRIE GIKKADGTCN TNFKKTQALE QVTKVLEDFV NGDVGILRKY VARLEDLRDT
LENSPFFKTH EVVGSSLLFV HDHTGLAKVW MIDFGKTVAL PDHQMLSHRL PWAEGNREDG
YLWGLDNLIC LLQGLAQS
