VIP1_CAEEL
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 03-AUG-2022, entry version 135.
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-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; 4.
DR STRING; 6239.F46F11.1a; -.
DR EPD; P91309; -.
DR PaxDb; P91309; -.
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 CTD; 172221; -.
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; IQERWCC; -.
DR OrthoDB; 138859at2759; -.
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 tissues.
DR GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
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; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
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; PTHR12750; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF53254; SSF53254; 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
