IP6K2_RABIT
ID IP6K2_RABIT Reviewed; 425 AA.
AC Q95221;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Inositol hexakisphosphate kinase 2;
DE Short=InsP6 kinase 2;
DE EC=2.7.4.- {ECO:0000269|PubMed:10567691};
DE AltName: Full=P(i)-uptake stimulator {ECO:0000303|PubMed:10567691};
DE Short=PiUS {ECO:0000303|PubMed:10567691};
GN Name=IP6K2; Synonyms=IHPK2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand; TISSUE=Small intestine;
RX PubMed=9070460; DOI=10.1007/s002329900183;
RA Norbis F., Boll M., Stange G., Markovich D., Verrey F., Biber J., Murer H.;
RT "Identification of a cDNA/protein leading to an increased Pi-uptake in
RT Xenopus laevis oocytes.";
RL J. Membr. Biol. 156:19-24(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10567691; DOI=10.1016/s0014-5793(99)01462-3;
RA Schell M.J., Letcher A.J., Brearley C.A., Biber J., Murer H., Irvine R.F.;
RT "PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase.";
RL FEBS Lett. 461:169-172(1999).
CC -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
CC {ECO:0000269|PubMed:10567691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10567691};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000269|PubMed:10567691}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHH9}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, intestine, liver and heart.
CC {ECO:0000269|PubMed:9070460}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was first identified because of its ability to stimulate
CC Na(+)-dependent phosphate cotransport. {ECO:0000269|PubMed:9070460}.
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DR EMBL; U74297; AAB49289.1; -; mRNA.
DR RefSeq; NP_001075846.1; NM_001082377.1.
DR AlphaFoldDB; Q95221; -.
DR SMR; Q95221; -.
DR STRING; 9986.ENSOCUP00000018629; -.
DR Ensembl; ENSOCUT00000012420; ENSOCUP00000010692; ENSOCUG00000012420.
DR GeneID; 100009233; -.
DR KEGG; ocu:100009233; -.
DR CTD; 51447; -.
DR eggNOG; KOG1620; Eukaryota.
DR GeneTree; ENSGT00940000156310; -.
DR HOGENOM; CLU_014862_0_0_1; -.
DR InParanoid; Q95221; -.
DR OMA; CEPKSKV; -.
DR OrthoDB; 902814at2759; -.
DR UniPathway; UPA00949; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000012420; Expressed in embryo and 17 other tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097243; F:flavonoid binding; ISS:UniProtKB.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:1905396; P:cellular response to flavonoid; ISS:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0043647; P:inositol phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
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; Kinase; Lipid metabolism; Nucleotide-binding; Nucleus;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..425
FT /note="Inositol hexakisphosphate kinase 2"
FT /id="PRO_0000066879"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 215..223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 235..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
SQ SEQUENCE 425 AA; 48967 MW; 4FC714618FEFD7B5 CRC64;
MSPAFRAMDV EPRTKGILLE PFVHQVGGHS CVLRFNETTL CKPLIPREHQ FYETLPAEMR
KFTPQYKGVV SVCFEEDEDR NLCLIAYPLK GDHGTVDLVD NSDCEPKSKV LRWTTKKHHV
LESEKTPKEW VRQHRKEEKM KSHKLEEEFE WLKKSEVLYY SVEKKGNVSS QLKHYNPWSM
KCHQQQLQRM KENAKHRNQY KFILLENLTS RYEVPCVLDL KMGTRQHGDD ASEEKAANQI
RKCQQSTSAV IGVRVCGMQV YQAGSGQLMF MNKYHGRKLS VQGFKEALFQ FFHNGRYLRR
ELLGPVLKKL AELKAVLERQ ESYRFYSSSL LVIYDGKEWP EVALDSDAED LEDLSEESAD
ESAGAYAYKP IGASSVDVRM IDFAHTTCRL YGEDSVVHEG QDAGYIFGLQ SLIDIVTEIS
EDSGE
