ITPK1_CHICK
ID ITPK1_CHICK Reviewed; 407 AA.
AC Q5F480;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase;
DE EC=2.7.1.134 {ECO:0000250|UniProtKB:Q13572};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase;
DE Short=Inositol-triphosphate 5/6-kinase;
DE Short=Ins(1,3,4)P(3) 5/6-kinase;
DE EC=2.7.1.159 {ECO:0000250|UniProtKB:Q13572};
GN Name=ITPK1; ORFNames=RCJMB04_2g4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate
CC such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4
CC at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to
CC have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of
CC plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
CC is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
CC Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6)
CC pathway. Also acts as an inositol polyphosphate phosphatase that
CC dephosphorylates Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and
CC Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that
CC interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and
CC Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as
CC the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-
CC induced apoptosis by interfering with the activation of TNFRSF1A-
CC associated death domain. Plays an important role in MLKL-mediated
CC necroptosis. Produces highly phosphorylated inositol phosphates such as
CC inositolhexakisphosphate (InsP6) which bind to MLKL mediating the
CC release of an N-terminal auto-inhibitory region leading to its
CC activation. Essential for activated phospho-MLKL to oligomerize and
CC localize to the cell membrane during necroptosis.
CC {ECO:0000250|UniProtKB:Q13572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC EC=2.7.1.134; Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12453;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12454;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13254;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13255;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20941;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20942;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4,6-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:70287,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660,
CC ChEBI:CHEBI:189099, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70288;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70289;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 1D-myo-inositol
CC 1,3,4-trisphosphate = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + 1D-
CC myo-inositol 3,4,5,6-tetrakisphosphate; Xref=Rhea:RHEA:70263,
CC ChEBI:CHEBI:57539, ChEBI:CHEBI:57660, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58414; Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70264;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70265;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 1D-myo-inositol
CC 1,3,4-trisphosphate = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-
CC myo-inositol 3,4,5,6-tetrakisphosphate; Xref=Rhea:RHEA:70271,
CC ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70272;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70273;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:Q13572};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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DR EMBL; AJ851420; CAH65054.1; -; mRNA.
DR RefSeq; NP_001012606.1; NM_001012588.1.
DR AlphaFoldDB; Q5F480; -.
DR SMR; Q5F480; -.
DR STRING; 9031.ENSGALP00000036796; -.
DR PaxDb; Q5F480; -.
DR Ensembl; ENSGALT00000048796; ENSGALP00000044263; ENSGALG00000034898.
DR GeneID; 423421; -.
DR KEGG; gga:423421; -.
DR CTD; 3705; -.
DR VEuPathDB; HostDB:geneid_423421; -.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR GeneTree; ENSGT00390000001278; -.
DR HOGENOM; CLU_041857_1_1_1; -.
DR InParanoid; Q5F480; -.
DR OMA; CKPLIAY; -.
DR OrthoDB; 1116241at2759; -.
DR PhylomeDB; Q5F480; -.
DR TreeFam; TF329288; -.
DR Reactome; R-GGA-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-GGA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q5F480; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000034898; Expressed in colon and 13 other tissues.
DR ExpressionAtlas; Q5F480; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IBA:GO_Central.
DR GO; GO:0000825; F:inositol tetrakisphosphate 6-kinase activity; ISS:UniProtKB.
DR GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR InterPro; IPR041429; ITPK1_N.
DR PANTHER; PTHR14217; PTHR14217; 1.
DR Pfam; PF05770; Ins134_P3_kin; 1.
DR Pfam; PF17927; Ins134_P3_kin_N; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Isomerase; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..407
FT /note="Inositol-tetrakisphosphate 1-kinase"
FT /id="PRO_0000220835"
FT DOMAIN 117..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 18
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250"
FT BINDING 188..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 199
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 45316 MW; 284E13DF28E16122 CRC64;
MQTFLKGKRV GYWLSEKKIR KLNFQAFAEL CRKRGVEVVQ LDLTKPIEDQ GPLDVIIHKL
TDVILEADQN DSQSLELVQR FQEYIDAHPE TIILDPLPAI RTLLDRSKSY ELIRQIEAYM
QDERICSPPF MELTSACGED TLQLIEKNGL AFPFICKTRV AHGTNSHEMA IIFNQEGLKA
VRPPCVIQSF INHNAVLYKV FVVGESYTVV KRPSLKNFSA GISDRESIFF NSHNVSKPES
SSVLTALDKI EGVFERPDDD VIREISKALR QALGVSLFGI DIIINNQTGQ HAVIDINAFP
GYEGVSEFFT DLLNHIAAVL QGQAPEVTQL NRSKLLAEQT GGIMDERICC ASTGCISVMG
KDSSWIVESE TNSSVKLQHQ RLGCNSAVSP SFQQHCVATL ATKASSQ
