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 29-MAY-2013, entry version 86.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase;
DE EC=2.7.4.21;
DE EC=2.7.4.24;
DE AltName: Full=InsP6 and PP-IP5 kinase;
GN ORFNames=F46F11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP 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
RT investigating biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with
CC the IP6K kinases to synthesize the diphosphate group-containing
CC inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-
CC InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4.
CC PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and
CC InsP8, may regulate a variety of cellular processes, including
CC apoptosis, vesicle trafficking, cytoskeletal dynamics, and
CC exocytosis. Phosphorylates inositol hexakisphosphate (InsP6) at
CC positions 1 or 3 to produce PP-InsP5 which is in turn
CC phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
CC phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from
CC InsP6, to produce (PP)2-InsP4 (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
CC 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4,5,6-
CC pentakisphosphate = ADP + 1D-myo-inositol diphosphate
CC tetrakisphosphate (isomeric configuration unknown).
CC -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate
CC pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate
CC tetrakisphosphate (isomeric configuration unknown).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily.
CC -!- CAUTION: Although related to histidine acid phosphatases, it lacks
CC the conserved active sites, suggesting that it has no phosphatase
CC activity.
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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.
DR RefSeq; NP_740856.1; NM_171837.6.
DR UniGene; Cel.5361; -.
DR ProteinModelPortal; P91309; -.
DR SMR; P91309; 16-326.
DR PaxDb; P91309; -.
DR PRIDE; P91309; -.
DR EnsemblMetazoa; F46F11.1a.1; F46F11.1a.1; F46F11.1.
DR EnsemblMetazoa; F46F11.1a.2; F46F11.1a.2; F46F11.1.
DR GeneID; 172221; -.
DR KEGG; cel:CELE_F46F11.1; -.
DR UCSC; F46F11.1b; c. elegans.
DR CTD; 172221; -.
DR WormBase; F46F11.1a; CE41904; WBGene00018508; -.
DR WormBase; F46F11.1b; CE30534; WBGene00018508; -.
DR eggNOG; NOG245915; -.
DR GeneTree; ENSGT00390000009048; -.
DR HOGENOM; HOG000177917; -.
DR InParanoid; P91309; -.
DR KO; K13024; -.
DR OMA; LTDCQQK; -.
DR NextBio; 874563; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR000560; His_Pase_superF_clade-2.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF08443; RimK; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1 1323 Inositol hexakisphosphate and
FT diphosphoinositol-pentakisphosphate
FT kinase.
FT /FTId=PRO_0000315696.
FT NP_BIND 212 215 ATP (By similarity).
FT NP_BIND 221 223 ATP (By similarity).
FT NP_BIND 296 298 ATP (By similarity).
FT REGION 26 27 Substrate binding (By similarity).
FT REGION 188 189 Substrate binding (By similarity).
FT REGION 301 304 Substrate binding (By similarity).
FT BINDING 109 109 ATP (By similarity).
FT BINDING 162 162 ATP (By similarity).
FT BINDING 169 169 ATP (By similarity).
FT BINDING 188 188 ATP (By similarity).
FT BINDING 223 223 Substrate (By similarity).
FT BINDING 237 237 Substrate (By similarity).
FT BINDING 284 284 ATP (By similarity).
FT VAR_SEQ 1044 1159 MADDGKTAKRQRSVTGAEKSMEEGDKPHGEWKGNGVAKSGS
FT QISVGSNEMESNNESMETVGGGKGQWVKDLLDQTKRAMAMN
FT SIREVEPPIVIPTPVPSTTTAVVEDEASERQSRS -> SQR
FT GSFHVTEPIQIDEKT (in isoform b).
FT /FTId=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
//
