IP3KB_RAT
ID IP3KB_RAT Reviewed; 934 AA.
AC P42335; Q91XW1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Inositol-trisphosphate 3-kinase B {ECO:0000305};
DE EC=2.7.1.127 {ECO:0000250|UniProtKB:P27987};
DE AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase B;
DE Short=IP3 3-kinase B;
DE Short=IP3K B;
DE Short=InsP 3-kinase B;
GN Name=Itpkb {ECO:0000312|RGD:2932};
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].
RC TISSUE=Brain;
RA Bertsch U., Suesse S., Frerk S., Fanick W.;
RT "Cloning of the complete protein coding regions for inositol 1,4,5-
RT trisphosphate 3-kinase B-isoforms from rat and human.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-934.
RC TISSUE=Liver;
RX PubMed=8312366; DOI=10.1016/0167-4889(94)90139-2;
RA Thomas S., Brake B., Luzio J.P., Stanley K., Banting G.;
RT "Isolation and sequence of a full length cDNA encoding a novel rat inositol
RT 1,4,5-trisphosphate 3-kinase.";
RL Biochim. Biophys. Acta 1220:219-222(1994).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-48; SER-209 AND
RP SER-274, AND 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 {ECO:0000250|UniProtKB:P27987}.
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:P27987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000250|UniProtKB:P27987};
CC -!- ACTIVITY REGULATION: IP3K is activated by calcium and calmodulin. Form
CC B is much more sensitive to calcium/calmodulin than form A.
CC {ECO:0000250|UniProtKB:P27987}.
CC -!- SUBUNIT: Interacts with DMTN. {ECO:0000250|UniProtKB:P27987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P27987}. Cytoplasm
CC {ECO:0000250|UniProtKB:P27987}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P27987}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52298.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ242781; CAC40660.1; -; mRNA.
DR EMBL; X74227; CAA52298.1; ALT_FRAME; mRNA.
DR PIR; S41053; S41053.
DR RefSeq; NP_062185.2; NM_019312.2.
DR RefSeq; XP_017454406.1; XM_017598917.1.
DR RefSeq; XP_017454407.1; XM_017598918.1.
DR PDB; 2AQX; X-ray; 2.50 A; A/B=642-930.
DR PDBsum; 2AQX; -.
DR AlphaFoldDB; P42335; -.
DR SMR; P42335; -.
DR STRING; 10116.ENSRNOP00000004032; -.
DR iPTMnet; P42335; -.
DR PhosphoSitePlus; P42335; -.
DR PaxDb; P42335; -.
DR PRIDE; P42335; -.
DR Ensembl; ENSRNOT00000004032; ENSRNOP00000004032; ENSRNOG00000002969.
DR GeneID; 54260; -.
DR KEGG; rno:54260; -.
DR UCSC; RGD:2932; rat.
DR CTD; 3707; -.
DR RGD; 2932; Itpkb.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000156764; -.
DR HOGENOM; CLU_017767_4_0_1; -.
DR InParanoid; P42335; -.
DR OMA; RTKSWGD; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; P42335; -.
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; P42335; -.
DR EvolutionaryTrace; P42335; -.
DR PRO; PR:P42335; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002969; Expressed in lung and 18 other tissues.
DR Genevisible; P42335; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISO:RGD.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0002262; P:myeloid cell homeostasis; ISO:RGD.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:RGD.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; ISO:RGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISO:RGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0045059; P:positive thymic T cell selection; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR GO; GO:0045061; P:thymic T cell selection; ISO:RGD.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 2.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..934
FT /note="Inositol-trisphosphate 3-kinase B"
FT /id="PRO_0000066869"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..764
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 718..720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 754
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 781..788
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 885
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 888
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27987"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 63..68
FT /note="LSLEEP -> ATKVPW (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 934 AA; 101819 MW; C844B79747E1A117 CRC64;
MAVYCYALNS LVIMNSTNEL KSGSPLPSGS ETPQPSGRAA LSPGSVFSPG RGASFLFPPA
ESLSLEEPGS AGGWRSGRRR LNSSSGSGGG SSSSNSSSSS GVGSPSWAGR LRGDAQQVVA
TRILSPPGPE EAQRKLRILQ RELQNVQVNQ KVGMFEAQIQ AQTSAIQAPR SPRLGRARSP
SPCPFRSSSQ PPERVLAPCS PSEERRTKSW GEQCTETPDA NSRRRSRLST HPSKDKEGVA
PLLGPASPTR LGTQSPSTSV RMERGSPASP RCGSPTPMEI DKRTAPSLEH FGTSLTLATK
VAASAASAGP HPGHDSVLME ADCELGAMRP WEAHLERRGQ FLGRETGSAP EPIRTHIREP
PGRVERVHSV GGQGSWTPEV IKRPEEGTVD AQSSELSENP RWSRLPGDPG SVGPEKGGSR
IPGIRGPQQT LDSMREGSSA LGLLGGSQAA QPGSMDVETG ISCGRMLEPL PPGEVTTNLK
EPQCLPGDRM GMQPESSIVW PSAVEEAPLI WTCDTGIQLK GTWRSQDGDA HPSCQEKSPD
QKDKACSPSN IPAIPAVIIT DMGAQEDGGL EEIQGSPRGP LPLRKLSSSS ASSTGFSSSY
EDSEEDISSD PERTLDPNSA FLHTLDQQKP RVSKSWRKIK NMVQWSPFVM SFKKKYPWIQ
LAGHAGSFKA AANGRILKKH CESEQRCLDR LMADVLRPFV PAYHGDVVKD GERYNQMDDL
LADFDSPCVM DCKMGIRTYL EEELTKARKK PSLRKDMYQK MVEVDPEAPT EEEKAQRAVT
KPRYMQWRET ISSTATLGFR IEGIKKEDGS VNRDFKKTKT REQVTEAFRE FTKGNQNILI
AYRDRLKAIR ETLEVSPFFK CHEVIGSSLL FIHDKKEQAK VWMIDFGKTT PLPEGQTLQH
DVPWQEGNRE DGYLSGLNNL IDILTEMSQG SPLT
