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Database: UniProt
Entry: Q5REW0
LinkDB: Q5REW0
Original site: Q5REW0 
ID   VIP2_PONAB              Reviewed;        1244 AA.
AC   Q5REW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   11-JUN-2014, entry version 47.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2;
DE            EC=2.7.4.21;
DE            EC=2.7.4.24;
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 2;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 1;
DE   AltName: Full=InsP6 and PP-IP5 kinase 2;
DE   AltName: Full=VIP1 homolog 2;
GN   Name=PPIP5K2; Synonyms=HISPPD1, VIP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with
CC       the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the
CC       diphosphate group-containing inositol pyrophosphates
CC       diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC       diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and
CC       (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a
CC       variety of cellular processes, including apoptosis, vesicle
CC       trafficking, cytoskeletal dynamics, exocytosis, insulin signaling
CC       and neutrophil activation. Phosphorylates inositol
CC       hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5
CC       which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4.
CC       Alternatively, phosphorylates at position 1 or 3 PP-InsP5,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By
CC       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   -!- DOMAIN: The polyphosphoinositide-binding domain mediates binding
CC       of PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the
CC       phosphatase domain of histidine acid phosphatases, it has no
CC       phosphatase activity (By similarity).
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily.
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DR   EMBL; CR857406; CAH89697.1; -; mRNA.
DR   ProteinModelPortal; Q5REW0; -.
DR   HOVERGEN; HBG108657; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
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   Gene3D; 3.40.50.1240; -; 3.
DR   InterPro; IPR000560; His_Pase_superF_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 3.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1   1244       Inositol hexakisphosphate and
FT                                diphosphoinositol-pentakisphosphate
FT                                kinase 2.
FT                                /FTId=PRO_0000315694.
FT   NP_BIND     237    240       ATP (By similarity).
FT   NP_BIND     246    248       ATP (By similarity).
FT   NP_BIND     321    323       ATP (By similarity).
FT   REGION       53     54       Substrate binding (By similarity).
FT   REGION      213    214       Substrate binding (By similarity).
FT   REGION      326    329       Substrate binding (By similarity).
FT   REGION      371    442       Polyphosphoinositide-binding domain (By
FT                                similarity).
FT   BINDING     134    134       ATP (By similarity).
FT   BINDING     187    187       ATP (By similarity).
FT   BINDING     194    194       ATP (By similarity).
FT   BINDING     213    213       ATP (By similarity).
FT   BINDING     248    248       Substrate (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     264    264       ATP (By similarity).
FT   BINDING     309    309       ATP (By similarity).
FT   MOD_RES      38     38       Phosphoserine (By similarity).
FT   MOD_RES    1007   1007       Phosphoserine (By similarity).
FT   MOD_RES    1017   1017       Phosphoserine (By similarity).
FT   MOD_RES    1173   1173       Phosphoserine (By similarity).
SQ   SEQUENCE   1244 AA;  140390 MW;  CBB0901E63D33824 CRC64;
     MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM
     KEILERVSLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF
     VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF
     QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM
     PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA
     FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI
     PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG
     KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFFSGINRKV
     QLTYLPHGCP KTSSEEEDSR REEPSLLLVL KWGGELTPAG RVQAEELGRA FRCMYPGGQG
     DYAGFPGCGL LRLHSTYRHD LKIYASDEGR VQMTAAAFAK GLLALEGELT PILVQMVKSA
     NMNGLLDSDS DSLSSCQQRV KARLHEILQK DRDFTAEDYE ELTPSGSVSL IKSMHLIKNP
     VKTCDKVYSL IQSLTSQIRH RMEDPKSSDI QLYHSETLEL MLRRWSKLEK DFKAKNGRYD
     ISKIPDIYDC IKYDVQHNGS LKLENTMELY RLSKALADIV IPQEYGITKA EKLEIAKGYC
     TPLVRKIRSD LQRTQDDGTV NKLHPVYSRG VLSPERHVRT RLYFTSESHV HSLLSILRYG
     ALCNESKDEQ WKRAMDYLNV VNELNYMTQI VIMLYEDPNK DLSSEERFHV ELHFSPGAKG
     CEEDKNLPSG YGYRPASREN EGRRPSKIDN DDEPHTSKRD EVDRAVILFK PMVSEPIHIH
     RKSPLPRSRK MATNDEESPL SVSSPEGTGT WLHYTSGVGT GRRRRRSGEQ ITSSPVSPKS
     LAFTSSIFGS WQQVVSENAN YLRTPRTLVE QKQNPTVGSH CAGLFSTSVL GGSSSAPNLQ
     DYARTHRKKL TSSGCIDDAT RGSAVKRFSI SFARHPTNGF ELYSMVPSIC PLETLHNALS
     LKQVDEFLAS IASPSSDVPR KTAEISSTAL HSSPIMRKKV SLNTYTPAKI LPTPPATLKS
     TKASSKPATS GPSSAVVPNT SSRKKNITSK TETHEHKKNT GKKK
//
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