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Database: UniProt
Entry: P91309
LinkDB: P91309
Original site: P91309 
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   16-APR-2014, entry version 92.
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-diphosphate 2,3,4,5,6-
CC       pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
CC       2,3,4,6-tetrakisphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-
CC       pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
CC       2,3,4,6-tetrakisphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
CC       1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
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, 515-592.
DR   STRING; 6239.F46F11.1a; -.
DR   PaxDb; P91309; -.
DR   PRIDE; P91309; -.
DR   EnsemblMetazoa; F46F11.1a.1; F46F11.1a.1; F46F11.1. [P91309-1]
DR   EnsemblMetazoa; F46F11.1a.2; F46F11.1a.2; F46F11.1. [P91309-1]
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; -.
DR   WormBase; F46F11.1b; CE30534; WBGene00018508; -.
DR   eggNOG; NOG245915; -.
DR   HOGENOM; HOG000177917; -.
DR   InParanoid; P91309; -.
DR   KO; K13024; -.
DR   OMA; GICCMMK; -.
DR   PhylomeDB; P91309; -.
DR   NextBio; 874563; -.
DR   PRO; PR:P91309; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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: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:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
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.
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
//
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