ID   IPPK_DANRE              Reviewed;         483 AA.
AC   Q4JL91; Q1LXA9; Q58ES1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE            EC=2.7.1.158;
DE   AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE   AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE            Short=InsP5 2-kinase;
GN   Name=ippk; Synonyms=ipk1; ORFNames=si:dkey-42i9.3, zgc:110769;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15992547; DOI=10.1016/j.devcel.2005.05.002;
RA   Sarmah B., Latimer A.J., Appel B., Wente S.R.;
RT   "Inositol polyphosphates regulate zebrafish left-right asymmetry.";
RL   Dev. Cell 9:133-145(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC       Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many
CC       processes such as mRNA export, non-homologous end-joining, endocytosis
CC       and ion channel regulation. InsP6 also acts as a key regulator of left-
CC       right asymmetry in embryo, probably by regulating asymmetric Ca(2+)
CC       during left-right specification. {ECO:0000269|PubMed:15992547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC         inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC         ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC         Evidence={ECO:0000269|PubMed:15992547};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed both maternally and zygotically.
CC       Expressed in cleavage-stage embryos. Ubiquitously distributed
CC       throughout blastula stages of embryogenesis. At the onset of
CC       gastrulation, it is enriched in cells around the blastoderm margin. At
CC       shield stage, expression is detected in the deep involuted cells that
CC       contribute to mesendoderm. During mid and late gastrula stages, it is
CC       strongly expressed in axial mesendoderm. However, it is not present in
CC       the nascent tailbud at yolk plug closure (YPC) stage. Expression in
CC       axial mesendoderm is reduced at the 2 somite stage (SS). At 6 SS, it is
CC       expressed in cells surrounding Kupffer's vesicle, but apparently not
CC       within. By 10 SS, it is no longer detected as a specific signal above
CC       background. {ECO:0000269|PubMed:15992547}.
CC   -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC       kinases of both family 1 and 2.
CC   -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK11040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ075212; AAY79345.1; -; mRNA.
DR   EMBL; BX465868; CAK11040.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC091783; AAH91783.1; -; mRNA.
DR   RefSeq; NP_001014346.1; NM_001014324.1.
DR   AlphaFoldDB; Q4JL91; -.
DR   SMR; Q4JL91; -.
DR   STRING; 7955.ENSDARP00000113709; -.
DR   PaxDb; Q4JL91; -.
DR   Ensembl; ENSDART00000131217; ENSDARP00000113709; ENSDARG00000003446.
DR   GeneID; 541511; -.
DR   KEGG; dre:541511; -.
DR   CTD; 64768; -.
DR   ZFIN; ZDB-GENE-050327-41; ippk.
DR   eggNOG; KOG4749; Eukaryota.
DR   GeneTree; ENSGT00390000010053; -.
DR   HOGENOM; CLU_033188_1_0_1; -.
DR   InParanoid; Q4JL91; -.
DR   OMA; NCVHCGE; -.
DR   OrthoDB; 1195478at2759; -.
DR   PhylomeDB; Q4JL91; -.
DR   TreeFam; TF106142; -.
DR   Reactome; R-DRE-1855167; Synthesis of pyrophosphates in the cytosol.
DR   Reactome; R-DRE-1855191; Synthesis of IPs in the nucleus.
DR   PRO; PR:Q4JL91; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 22.
DR   Bgee; ENSDARG00000003446; Expressed in early embryo and 28 other tissues.
DR   GO; GO:0005813; C:centrosome; IDA:ZFIN.
DR   GO; GO:0036064; C:ciliary basal body; IDA:ZFIN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IDA:ZFIN.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR   GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR   GO; GO:0032402; P:melanosome transport; IMP:ZFIN.
DR   Gene3D; 3.30.200.110; -; 1.
DR   InterPro; IPR009286; Ins_P5_2-kin.
DR   InterPro; IPR043001; IP5_2-K_N_lobe.
DR   PANTHER; PTHR14456; PTHR14456; 1.
DR   Pfam; PF06090; Ins_P5_2-kin; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Developmental protein; Kinase; Nucleotide-binding;
KW   Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..483
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000110532"
FT   REGION          279..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           140..144
FT                   /note="EXKPK motif"
FT   COMPBIAS        282..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        83
FT                   /note="R -> G (in Ref. 3; AAH91783)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="K -> E (in Ref. 3; AAH91783)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="I -> S (in Ref. 1; AAY79345)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  56028 MW;  21242F5883A4CBEC CRC64;
     MELDKMDEND WKYHGEGNKS IVVSHLRHCQ VLRLLKVPSE DSAHTRQTAE QTLRHILNIM
     DYSKHVMKPL LGEKYVHSGE VVRLPLDFLR QMSLKVQQER PELRCDKVMD TFSGCGLCLP
     DLTQLPLHHL RDHRPPICVE IKPKCGFLPF SRHMTKECKW KVCRFCMHQH YKLANGKWKR
     LSRYCPLDLF SGSKQRMYVA LKNLLEEPQN NLKIFKGGEL IFSCKDDAKQ QPDLNNLIQH
     LRPYFPHTNG LYNGHQPGKV ILNEFIQVIC SALLSGGDSN RSGEPRKMHL SESKPHCEAS
     PFPRDLIRNG HHGLPKDSVL AKILQVQMLD NLDIEGIYPL YKRVEQYLEE FPKERIRLQI
     DGPYDESFMD TVKSCLNEDD GSVEYAIGKV HQYRVAMTAK DCSVMITFAP CEEDEEHKLN
     LEKPRFTYSV SILDLDTKPY EGIPHQYKLD SKIVNYYLRS TQAPPPSSLY KERQECTLLF
     HAV