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 01-MAY-2013, entry version 41.
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 1,3,4,5,6-
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 -!- 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 UniGene; Pab.19436; -.
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: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; IPR000560; His_Pase_superF_clade-2.
DR Pfam; PF00328; His_Phos_2; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; FALSE_NEG.
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 217 217 Phosphoserine (By similarity).
FT MOD_RES 220 220 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).
FT MOD_RES 1181 1181 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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