IP3KA_RAT
ID IP3KA_RAT Reviewed; 459 AA.
AC P17105;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 3.
DT 03-AUG-2022, entry version 151.
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|RGD:619950};
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].
RX PubMed=2176078; DOI=10.1042/bj2720107;
RA Takazawa K., Vandekerckhove J., Dumont J.E., Erneux C.;
RT "Cloning and expression in Escherichia coli of a rat brain cDNA encoding a
RT Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase.";
RL Biochem. J. 272:107-112(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=2157285; DOI=10.1126/science.2157285;
RA Choi K.Y., Kim H.K., Lee S.Y., Moon K.H., Sim S.S., Kim J.W., Chung H.K.,
RA Rhee S.G.;
RT "Molecular cloning and expression of a complementary DNA for inositol
RT 1,4,5-trisphosphate 3-kinase.";
RL Science 248:64-66(1990).
RN [3]
RP PROTEIN SEQUENCE OF 315-326, CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL
RP MODIFICATION.
RX PubMed=7646431; DOI=10.1042/bj3100109;
RA Communi D., Lecocq R., Vanweyenberg V., Erneux C.;
RT "Active site labelling of inositol 1,4,5-trisphosphate 3-kinase A by
RT phenylglyoxal.";
RL Biochem. J. 310:109-115(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 185-459 IN COMPLEX WITH ADP.
RX PubMed=15350215; DOI=10.1016/j.molcel.2004.08.005;
RA Miller G.J., Hurley J.H.;
RT "Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-
RT kinase.";
RL Mol. Cell 15:703-711(2004).
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:0000269|PubMed:7646431}.
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:7646431};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000269|PubMed:7646431};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41457.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X56917; CAA40248.1; -; mRNA.
DR EMBL; M29787; AAA41457.1; ALT_INIT; mRNA.
DR PIR; S13064; S13064.
DR RefSeq; NP_112307.2; NM_031045.2.
DR PDB; 1TZD; X-ray; 2.20 A; A/B=185-459.
DR PDBsum; 1TZD; -.
DR AlphaFoldDB; P17105; -.
DR SMR; P17105; -.
DR BioGRID; 249574; 3.
DR STRING; 10116.ENSRNOP00000007247; -.
DR BindingDB; P17105; -.
DR ChEMBL; CHEMBL3261; -.
DR iPTMnet; P17105; -.
DR PhosphoSitePlus; P17105; -.
DR PaxDb; P17105; -.
DR PRIDE; P17105; -.
DR Ensembl; ENSRNOT00000007247; ENSRNOP00000007247; ENSRNOG00000005284.
DR GeneID; 81677; -.
DR KEGG; rno:81677; -.
DR UCSC; RGD:619950; rat.
DR CTD; 3706; -.
DR RGD; 619950; Itpka.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000161350; -.
DR HOGENOM; CLU_017767_1_1_1; -.
DR InParanoid; P17105; -.
DR OMA; HIILESS; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; P17105; -.
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; P17105; -.
DR EvolutionaryTrace; P17105; -.
DR PRO; PR:P17105; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005284; Expressed in Ammon's horn and 17 other tissues.
DR Genevisible; P17105; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA: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; IDA:RGD.
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:RGD.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
DR GO; GO:0006020; P:inositol metabolic process; ISO:RGD.
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; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR DisProt; DP02461; -.
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 3D-structure; ATP-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Kinase; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..459
FT /note="Inositol-trisphosphate 3-kinase A"
FT /id="PRO_0000066867"
FT REGION 1..26
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 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 BINDING 247..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R071"
FT MOD_RES 55
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R071"
FT MOD_RES 62
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R071"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1TZD"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:1TZD"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 365..382
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:1TZD"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1TZD"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:1TZD"
SQ SEQUENCE 459 AA; 50871 MW; 8093DADC0FADC290 CRC64;
MTLPGHPTGM ARPRGAGPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA AGEPRARGAK
RRGGQVPNGL PRAAPAPVIP QLTVTSEEDV APASPGPPDR EGNWLPAAGS HLQQPRRLST
SSLSSTGSSS LLEDSEDDLL SDSESRSRGN VQLETSEDVG QKSHWQKIRT MVNLPVMSPF
KKRYSWVQLA GHTGSFKAAG TSGLILKRSS EPEHYCLVRL MADVLRGCVP AFHGVVERDG
ESYLQLQDLL DGFDGPCVLD CKMGVRTYLE EELTKARERP KLRKDMYKKM LAVDPEAPTE
EEHAQRAVTK PRYMQWREGI SSSTTLGFRI EGIKKADGSC STDFKTTRSR EQVTRVFEEF
MQGDAEVLKR YLNRLQQIRD TLEISDFFRR HEVIGSSLLF VHDHCHRAGV WLIDFGKTTP
LPDGQILDHR RPWEEGNRED GYLLGLDNLI GILANLAER
