IP3KH_CAEEL
ID IP3KH_CAEEL Reviewed; 494 AA.
AC Q95Q62; H2KZ42; H2KZ43; H2KZ45; H2KZ46; H2KZ47; O45049; O45050; O45051;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Inositol-trisphosphate 3-kinase homolog {ECO:0000305};
DE EC=2.7.1.127 {ECO:0000269|PubMed:9491893};
DE AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase homolog {ECO:0000303|PubMed:9491893};
DE Short=IP3 3-kinase {ECO:0000305};
DE Short=IP3K {ECO:0000305};
DE Short=InsP 3-kinase {ECO:0000305};
DE AltName: Full=let-23 fertility effector 2 {ECO:0000303|PubMed:9491893};
GN Name=lfe-2 {ECO:0000312|WormBase:C46H11.4a};
GN ORFNames=C46H11.4 {ECO:0000312|WormBase:C46H11.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC38960.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=9491893; DOI=10.1016/s0092-8674(00)80945-9;
RA Clandinin T.R., DeModena J.A., Sternberg P.W.;
RT "Inositol trisphosphate mediates a RAS-independent response to LET-23
RT receptor tyrosine kinase activation in C. elegans.";
RL Cell 92:523-533(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=16186564; DOI=10.1085/jgp.200509355;
RA Espelt M.V., Estevez A.Y., Yin X., Strange K.;
RT "Oscillatory Ca2+ signaling in the isolated Caenorhabditis elegans
RT intestine: role of the inositol-1,4,5-trisphosphate receptor and
RT phospholipases C beta and gamma.";
RL J. Gen. Physiol. 126:379-392(2005).
RN [4] {ECO:0000305}
RP ALTERNATIVE SPLICING (ISOFORMS C; D; E AND F).
RX PubMed=18084645; DOI=10.6026/97320630002017;
RA Kashyap L., Tabish M., Ganesh G., Dubey D.;
RT "Computational and molecular characterization of multiple isoforms of lfe-2
RT gene in nematode C. elegans.";
RL Bioinformation 2:17-21(2007).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=23671426; DOI=10.1371/journal.pgen.1003510;
RA Kovacevic I., Orozco J.M., Cram E.J.;
RT "Filamin and phospholipase C-epsilon are required for calcium signaling in
RT the Caenorhabditis elegans spermatheca.";
RL PLoS Genet. 9:E1003510-E1003510(2013).
CC -!- FUNCTION: Probably by regulating inositol 1,4,5-trisphosphate levels,
CC negatively regulates posterior body wall muscle contractions required
CC for defecation and let-23 signaling pathway that controls spermathecal
CC dilation and ovulation (PubMed:9491893, PubMed:16186564). May also
CC regulate ovulation downstream of actin cross-linker fln-1
CC (PubMed:23671426). {ECO:0000269|PubMed:16186564,
CC ECO:0000269|PubMed:23671426, ECO:0000269|PubMed:9491893}.
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:9491893};
CC -!- ACTIVITY REGULATION: Unlike mammalian IP3K, may not be regulated by
CC calmodulin. {ECO:0000303|PubMed:9491893}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=a {ECO:0000312|WormBase:C46H11.4a};
CC IsoId=Q95Q62-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C46H11.4b};
CC IsoId=Q95Q62-2; Sequence=VSP_058582;
CC Name=c {ECO:0000312|WormBase:C46H11.4c};
CC IsoId=Q95Q62-3; Sequence=VSP_058583;
CC Name=d {ECO:0000312|WormBase:C46H11.4d};
CC IsoId=Q95Q62-4; Sequence=VSP_058584;
CC Name=e {ECO:0000312|WormBase:C46H11.4e};
CC IsoId=Q95Q62-5; Sequence=VSP_058586;
CC Name=f {ECO:0000312|WormBase:C46H11.4f};
CC IsoId=Q95Q62-6; Sequence=VSP_058585;
CC -!- TISSUE SPECIFICITY: Expressed in spermatheca.
CC {ECO:0000269|PubMed:9491893}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AF045611; AAC38960.1; -; mRNA.
DR EMBL; AF045612; AAC38961.1; -; mRNA.
DR EMBL; AF045613; AAC38962.1; -; mRNA.
DR EMBL; BX284601; CCD66218.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66219.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66220.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66228.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66229.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66230.1; -; Genomic_DNA.
DR PIR; T42444; T42444.
DR PIR; T42512; T42512.
DR PIR; T42513; T42513.
DR RefSeq; NP_001021047.1; NM_001025876.3. [Q95Q62-1]
DR RefSeq; NP_001021048.1; NM_001025877.5. [Q95Q62-2]
DR RefSeq; NP_001021049.1; NM_001025878.5. [Q95Q62-3]
DR RefSeq; NP_001249776.1; NM_001262847.1.
DR RefSeq; NP_001249778.1; NM_001262849.1. [Q95Q62-5]
DR RefSeq; NP_001249779.1; NM_001262850.1.
DR AlphaFoldDB; Q95Q62; -.
DR SMR; Q95Q62; -.
DR IntAct; Q95Q62; 1.
DR MINT; Q95Q62; -.
DR STRING; 6239.C46H11.4a; -.
DR EPD; Q95Q62; -.
DR PaxDb; Q95Q62; -.
DR EnsemblMetazoa; C46H11.4a.1; C46H11.4a.1; WBGene00002979. [Q95Q62-1]
DR EnsemblMetazoa; C46H11.4b.1; C46H11.4b.1; WBGene00002979. [Q95Q62-2]
DR EnsemblMetazoa; C46H11.4c.1; C46H11.4c.1; WBGene00002979. [Q95Q62-3]
DR EnsemblMetazoa; C46H11.4e.1; C46H11.4e.1; WBGene00002979. [Q95Q62-5]
DR EnsemblMetazoa; C46H11.4f.1; C46H11.4f.1; WBGene00002979.
DR EnsemblMetazoa; C46H11.4f.2; C46H11.4f.2; WBGene00002979.
DR GeneID; 172128; -.
DR KEGG; cel:CELE_C46H11.4; -.
DR UCSC; C46H11.4c; c. elegans. [Q95Q62-1]
DR CTD; 172128; -.
DR WormBase; C46H11.4a; CE27862; WBGene00002979; lfe-2. [Q95Q62-1]
DR WormBase; C46H11.4b; CE27863; WBGene00002979; lfe-2. [Q95Q62-2]
DR WormBase; C46H11.4c; CE27864; WBGene00002979; lfe-2. [Q95Q62-3]
DR WormBase; C46H11.4d; CE43466; WBGene00002979; lfe-2. [Q95Q62-4]
DR WormBase; C46H11.4e; CE43449; WBGene00002979; lfe-2. [Q95Q62-5]
DR WormBase; C46H11.4f; CE52138; WBGene00002979; lfe-2. [Q95Q62-6]
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000173539; -.
DR HOGENOM; CLU_552348_0_0_1; -.
DR InParanoid; Q95Q62; -.
DR OMA; FGFNDPH; -.
DR OrthoDB; 966687at2759; -.
DR PhylomeDB; Q95Q62; -.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:Q95Q62; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002979; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IGI:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..494
FT /note="Inositol-trisphosphate 3-kinase homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437981"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 260..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 322..329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P23677"
FT VAR_SEQ 1..173
FT /note="MHTQPQSYQAPEQTHMRIENRRIEAGKGGTNLLLIIESRVDTLSINLPTLYS
FT LLFTTNITILMSAPQHRQLRRAAHITKIASIDLCSLEEEDHEDLVLEESGHHPSDIQNE
FT KPNRPPYSTLIRKRSGKVFRFVRPKLADLWHSRYHEASFDLGRRLGIGRRTQSCCEDVC
FT DEE -> MTTLFEKLAELMLMDTDKYSPQKSRLFKRMAANIISCFPYPTTRPASPQCLP
FT KPSPESCEHRAFCDAFGKLVQ (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058582"
FT VAR_SEQ 1..173
FT /note="MHTQPQSYQAPEQTHMRIENRRIEAGKGGTNLLLIIESRVDTLSINLPTLYS
FT LLFTTNITILMSAPQHRQLRRAAHITKIASIDLCSLEEEDHEDLVLEESGHHPSDIQNE
FT KPNRPPYSTLIRKRSGKVFRFVRPKLADLWHSRYHEASFDLGRRLGIGRRTQSCCEDVC
FT DEE -> MLEAIYAKIMGVGTSRHDKRQGCWSWGGSSNSEEKRMKRPKKLPSKLRLKIS
FT GNQRRRRDDTFVVWEEIPTPSVCDHRDTMNSEASSSPPSAPTQERLMQIISCFPYPTTR
FT PASPQCLPKPSPESCEHRAFCDAFGKLVQ (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058583"
FT VAR_SEQ 1..173
FT /note="MHTQPQSYQAPEQTHMRIENRRIEAGKGGTNLLLIIESRVDTLSINLPTLYS
FT LLFTTNITILMSAPQHRQLRRAAHITKIASIDLCSLEEEDHEDLVLEESGHHPSDIQNE
FT KPNRPPYSTLIRKRSGKVFRFVRPKLADLWHSRYHEASFDLGRRLGIGRRTQSCCEDVC
FT DEE -> MCLMSNVECKEVVNCNSSNSEEKRMKRPKKLPSKLRLKISGNQRRRRDDTFV
FT VWEEIPTPSVCDHRDTMNSEASSSPPSAPTQERLMQIISCFPYPTTRPASPQCLPKPSP
FT ESCEHRAFCDAFGKLVQ (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058584"
FT VAR_SEQ 1..173
FT /note="MHTQPQSYQAPEQTHMRIENRRIEAGKGGTNLLLIIESRVDTLSINLPTLYS
FT LLFTTNITILMSAPQHRQLRRAAHITKIASIDLCSLEEEDHEDLVLEESGHHPSDIQNE
FT KPNRPPYSTLIRKRSGKVFRFVRPKLADLWHSRYHEASFDLGRRLGIGRRTQSCCEDVC
FT DEE -> MNYAHSASEKKSENKTLKKKGHIARSSNSEEKRMKRPKKLPSKLRLKISGNQ
FT RRRRDDTFVVWEEIPTPSVCDHRDTMNSEASSSPPSAPTQERLMQIISCFPYPTTRPAS
FT PQCLPKPSPESCEHRAFCDAFGKLVQ (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_058585"
FT VAR_SEQ 2..173
FT /note="HTQPQSYQAPEQTHMRIENRRIEAGKGGTNLLLIIESRVDTLSINLPTLYSL
FT LFTTNITILMSAPQHRQLRRAAHITKIASIDLCSLEEEDHEDLVLEESGHHPSDIQNEK
FT PNRPPYSTLIRKRSGKVFRFVRPKLADLWHSRYHEASFDLGRRLGIGRRTQSCCEDVCD
FT EE -> SLSNRVRAHLVRSLLYIYTFIMGVGTSRHDKRQGCWSWGGSSNSEEKRMKRPK
FT KLPSKLRLKISGNQRRRRDDTFVVWEEIPTPSVCDHRDTMNSEASSSPPSAPTQERLMQ
FT IISCFPYPTTRPASPQCLPKPSPESCEHRAFCDAFGKLVQ (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058586"
FT CONFLICT 488
FT /note="R -> T (in Ref. 1; AAC38960/AAC38961/AAC38962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56840 MW; 8F1EBEC9F0359A29 CRC64;
MHTQPQSYQA PEQTHMRIEN RRIEAGKGGT NLLLIIESRV DTLSINLPTL YSLLFTTNIT
ILMSAPQHRQ LRRAAHITKI ASIDLCSLEE EDHEDLVLEE SGHHPSDIQN EKPNRPPYST
LIRKRSGKVF RFVRPKLADL WHSRYHEASF DLGRRLGIGR RTQSCCEDVC DEEVSVETMA
ITALPMDVWL KERLKKWVQL SGHEGSIVPA TPHTLYKKQC ANCGEGRAYK NISKDPALDG
FTPKYYDELE KNEEHFIEIE DLLQQFHDPT KTAIMDIKIG TRTFLESEVS NTKKRADLYE
KMVAIDNDEP TEEERKCGAI TKLRYMQFRE RESSTAQLGF RIEAAKRLEG ALEKNFKKVR
TVEDVTTTFM DFFGTQRSRV RQQLIERLKS MRKAIEHSSF FNSHEVVGSS ILIVFDTEKV
GCWMIDFAKS SPVPNGRTLN HRTTWIPGNN EDGYLIGIDN LVKILEELPE YGEHPDDQLM
VTEEVIARMK NTKS
