ID   VIP1_CAEEL              Reviewed;        1323 AA.
AC   P91309; Q8T3B4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 3.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000250|UniProtKB:Q6PFW1};
DE   AltName: Full=InsP6 and PP-IP5 kinase;
GN   ORFNames=F46F11.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
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).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases to synthesize the diphosphate group-containing inositol
CC       pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC       diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC       InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC       of cellular processes, including apoptosis, vesicle trafficking,
CC       cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC       hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in
CC       turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
CC       phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to
CC       produce (PP)2-InsP4. {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC         inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC         ChEBI:CHEBI:456216; EC=2.7.4.24;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC         + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC         + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=P91309-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=P91309-2; Sequence=VSP_030639;
CC   -!- DOMAIN: The N-terminal kinase domain produces inositol polyphosphates.
CC       The C-terminal acid phosphatase-like domain binds inositol
CC       polyphosphates and negatively regulates their accumulation. The C-
CC       terminal domain reduces the amount of inositol pyrophosphates in a
CC       dose-dependent manner in vitro. {ECO:0000250|UniProtKB:O74429}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although related to histidine acid phosphatases, it lacks the
CC       conserved active sites, suggesting that it has no phosphatase activity.
CC       {ECO:0000305}.
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DR   EMBL; FO081396; CCD71324.1; -; Genomic_DNA.
DR   EMBL; FO081396; CCD71335.1; -; Genomic_DNA.
DR   RefSeq; NP_740855.2; NM_170868.4. [P91309-1]
DR   RefSeq; NP_740856.1; NM_171837.6. [P91309-2]
DR   AlphaFoldDB; P91309; -.
DR   SMR; P91309; -.
DR   BioGRID; 37679; 5.
DR   STRING; 6239.F46F11.1a.1; -.
DR   EPD; P91309; -.
DR   PaxDb; 6239-F46F11-1a; -.
DR   PeptideAtlas; P91309; -.
DR   EnsemblMetazoa; F46F11.1a.1; F46F11.1a.1; WBGene00018508. [P91309-1]
DR   EnsemblMetazoa; F46F11.1b.1; F46F11.1b.1; WBGene00018508. [P91309-2]
DR   GeneID; 172221; -.
DR   KEGG; cel:CELE_F46F11.1; -.
DR   UCSC; F46F11.1b; c. elegans. [P91309-1]
DR   AGR; WB:WBGene00018508; -.
DR   WormBase; F46F11.1a; CE41904; WBGene00018508; -. [P91309-1]
DR   WormBase; F46F11.1b; CE30534; WBGene00018508; -. [P91309-2]
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   InParanoid; P91309; -.
DR   OMA; AQIWACS; -.
DR   OrthoDB; 5476261at2759; -.
DR   PhylomeDB; P91309; -.
DR   Reactome; R-CEL-1855167; Synthesis of pyrophosphates in the cytosol.
DR   PRO; PR:P91309; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00018508; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.11950; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR037446; His_Pase_VIP1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR040557; VIP1_N.
DR   PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1323
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase"
FT                   /id="PRO_0000315696"
FT   REGION          355..426
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   REGION          933..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..1014
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1075
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         212..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         296..298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         301..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   VAR_SEQ         1044..1159
FT                   /note="MADDGKTAKRQRSVTGAEKSMEEGDKPHGEWKGNGVAKSGSQISVGSNEMES
FT                   NNESMETVGGGKGQWVKDLLDQTKRAMAMNSIREVEPPIVIPTPVPSTTTAVVEDEASE
FT                   RQSRS -> SQRGSFHVTEPIQIDEKT (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030639"
SQ   SEQUENCE   1323 AA;  150120 MW;  B9D3A901879C8B0F CRC64;
     MAHKGTESKE QIWPYKITIG ICAMNRKATS KPMRAIMKKI IDFYGQWVDS FIFPEQVIIN
     EPVENWPLCH CLVSFHSTEF PLEKAIAYVK LRNPYVINNL DRQYDLLDRR TVFKILSDNG
     IEHPRHGYVI RGRPNEPDTE LVEHPDHIEV NGEVFNKPFV EKPISSEDHN VYIYYPSSVG
     GGSQRLFRKI NNRSSWYSPK SEVRKEGSYI YEEFIPADGT DVKVYAVGPF YAHAEARKAP
     GLDGKVERDS DGKEVRYPVI LSNKEKQIAK KIVLAFGQTV CGFDLLRANG KSYVCDVNGF
     SFVKTSTKYY EDTAKILGNQ IVRHYAKSKN WRVPSDMPQP PILDLGLGDD PPMITTPSGK
     LAELRCVVAV IRHGDRTPKQ KMKLIVTDQR FFALFEKYDG YKKHEIKMKK PNQLMEVLEL
     ARALVIEKQR DRHQILEKLR EGTGEEEIHK SEHDLEVCEE EMKKWEQMRT VLEMYGHFSG
     INRKVQMKYL KERETKTSDE ELRREGPALL LILKWGGELT TAGNMQAEAL GRLFRTLYPG
     IRRTDGKSSP EDTQGLGFLR LHSTYRHDLK IYASDEGRVQ TTAAAFAKGL LALEGELTPI
     LMQMVKSANT DGLLDDDCQA RLYQTELKRY LHKALQADRD FTPQDYLELN PNGLRAITAA
     MEFIKNPRKM CHEIAGYVEK MCGVIVEYSQ TRPTGSTLYL QESMDLAQRR WNKELREFRR
     KNKHGEVEFD ISKIPDIYDN IKYDMEHNPD LCINNEVEFE RMYVCVKNMA DIVVPQEYGI
     KTENKMVIAQ RVCTPLLRKI RNDLHRCLEN KESEETQTRL DPRASQGIAT PFRHVRTRLY
     FTSESHIHTL MNLIRYGNLC SVDDKKWQRA MNFLSGVTEF NYMTQVVLMV YEDSRKENDE
     ADTGPRFHIE ILFSPGLYPC FLTEKERIYE TRFNLSTNPK PATSSRSSGR ESRDTNDSAS
     SSTEGRRPSI EKVVTVVTPT QLSTPSVTND DLSISSNAES TAAESTGLVN TTTKTHNDSE
     DDLNDVESVN LVALDELNNT TKAMADDGKT AKRQRSVTGA EKSMEEGDKP HGEWKGNGVA
     KSGSQISVGS NEMESNNESM ETVGGGKGQW VKDLLDQTKR AMAMNSIREV EPPIVIPTPV
     PSTTTAVVED EASERQSRSR RYFPYRFKHH TAQLLTGMSG GGVHMQNRLI STDVLTGKFG
     DHDNKKNSRK DFGAGTAVLS TAVIARSSSA PRLMTYESED FSVGEIKRFW PPLRSLETLH
     DSINLSQFDG FLERLIKGAL TPLPSPPKTP LPSALSCDAI NKTPTQDEVE KVIGKLAPTS
     STD
//