IP3KA_MOUSE
ID IP3KA_MOUSE Reviewed; 459 AA.
AC Q8R071; A2AQ20;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Inositol-trisphosphate 3-kinase A;
DE EC=2.7.1.127 {ECO:0000250|UniProtKB:P23677};
DE AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase A;
DE Short=IP3 3-kinase A;
DE Short=IP3K A;
DE Short=InsP 3-kinase A;
GN Name=Itpka {ECO:0000312|MGI:MGI:1333822};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Testis;
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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-35; ARG-55 AND ARG-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 {ECO:0000250|UniProtKB:P23677}.
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:P23677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000250|UniProtKB:P23677};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
CC {ECO:0000250|UniProtKB:P23677}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P23677}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AL844536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027291; AAH27291.1; -; mRNA.
DR CCDS; CCDS16607.1; -.
DR RefSeq; NP_666237.1; NM_146125.2.
DR AlphaFoldDB; Q8R071; -.
DR SMR; Q8R071; -.
DR BioGRID; 230741; 5.
DR IntAct; Q8R071; 4.
DR MINT; Q8R071; -.
DR STRING; 10090.ENSMUSP00000028758; -.
DR iPTMnet; Q8R071; -.
DR PhosphoSitePlus; Q8R071; -.
DR SwissPalm; Q8R071; -.
DR MaxQB; Q8R071; -.
DR PaxDb; Q8R071; -.
DR PeptideAtlas; Q8R071; -.
DR PRIDE; Q8R071; -.
DR ProteomicsDB; 267148; -.
DR Antibodypedia; 23312; 203 antibodies from 28 providers.
DR DNASU; 228550; -.
DR Ensembl; ENSMUST00000028758; ENSMUSP00000028758; ENSMUSG00000027296.
DR GeneID; 228550; -.
DR KEGG; mmu:228550; -.
DR UCSC; uc008luf.1; mouse.
DR CTD; 3706; -.
DR MGI; MGI:1333822; Itpka.
DR VEuPathDB; HostDB:ENSMUSG00000027296; -.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000161350; -.
DR HOGENOM; CLU_017767_1_1_1; -.
DR InParanoid; Q8R071; -.
DR OMA; HIILESS; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; Q8R071; -.
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; 228550; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q8R071; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R071; protein.
DR Bgee; ENSMUSG00000027296; Expressed in CA1 field of hippocampus and 126 other tissues.
DR Genevisible; Q8R071; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; ISO:MGI.
DR GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
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 GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
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; Cytoskeleton; Kinase;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..459
FT /note="Inositol-trisphosphate 3-kinase A"
FT /id="PRO_0000066866"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..293
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 247..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310..317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 55
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 62
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23677"
SQ SEQUENCE 459 AA; 50935 MW; 3CDA79DD267A1A5D CRC64;
MTLPGRPTGM ARPRGAGPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA AGEPRARGAK
RRGGQVPNGL PRAAPAPVIP QLTVTSEEDV TPASPGPPDQ EGNWLPAAGS HLQQPRRLST
SSLSSTGSSS LLEDSEDDLL SDSESRSRGN VQLETSEDVG QKSHWQKIRT MVNLPVMSPF
RKRYSWVQLA GHTGSFKAAG TSGLILKRSS EPEHYCLVRL MADVLRGCVP AFHGIVERDG
ESYLQLQDLL DGFDGPCVLD CKMGVRTYLE EELTKARERP KLRKDMYKKM LAVDPEAPTE
EEHAQRAVTK PRYMQWREGI SSSTTLGFRI EGIKKADGSC STDFKTTRSR EQVTRVFEEF
MQGDAEVLRR YLNRLQQIRD TLEISDFFRR HEVIGSSLLF VHDHCHRAGV WLIDFGKTTP
LPDGQILDHR RPWEEGNRED GYLLGLDNLI GILASLAER
