ID VIP1_PONAB Reviewed; 1409 AA. AC Q5RDF1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 22-FEB-2023, entry version 83. DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 {ECO:0000250|UniProtKB:Q6PFW1}; DE EC=2.7.4.24 {ECO:0000250|UniProtKB:Q6PFW1}; DE AltName: Full=Diphosphoinositol pentakisphosphate kinase 1; DE AltName: Full=Histidine acid phosphatase domain-containing protein 2A; DE AltName: Full=InsP6 and PP-IP5 kinase 1; DE AltName: Full=VIP1 homolog; GN Name=PPIP5K1 {ECO:0000250|UniProtKB:Q6PFW1}; Synonyms=HISPPD2A, VIP1; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 the CC IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate CC group-containing inositol pyrophosphates diphosphoinositol CC pentakisphosphate, PP-InsP5, and bis-diphosphoinositol CC tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also CC respectively called InsP7 and InsP8, regulate a variety of cellular CC processes, including apoptosis, vesicle trafficking, cytoskeletal CC dynamics, exocytosis, insulin signaling and neutrophil activation. CC Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to CC produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce CC (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, CC produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when CC cells are exposed to hyperosmotic stress. CC {ECO:0000250|UniProtKB:Q6PFW1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-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}. Cell membrane CC {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane CC upon activation of the PtdIns 3-kinase pathway. CC {ECO:0000250|UniProtKB:Q6PFW1}. CC -!- DOMAIN: The C-terminal acid phosphatase-like domain binds CC PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase CC domain of histidine acid phosphatases, it has no phosphatase activity. CC {ECO:0000250|UniProtKB:Q6PFW1}. CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR857961; CAH90206.1; -; mRNA. DR AlphaFoldDB; Q5RDF1; -. DR SMR; Q5RDF1; -. DR STRING; 9601.ENSPPYP00000007270; -. DR eggNOG; KOG1057; Eukaryota. DR InParanoid; Q5RDF1; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; IEA:InterPro. 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; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07061; HP_HAP_like; 1. DR Gene3D; 3.40.50.11950; -; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1. DR InterPro; IPR033379; Acid_Pase_AS. 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; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1. DR PANTHER; PTHR12750:SF11; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 1; 1. DR Pfam; PF00328; His_Phos_2; 1. DR Pfam; PF18086; PPIP5K2_N; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..1409 FT /note="Inositol hexakisphosphate and diphosphoinositol- FT pentakisphosphate kinase 1" FT /id="PRO_0000315690" FT REGION 382..453 FT /note="Polyphosphoinositide-binding domain" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" FT REGION 891..996 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1110..1183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 964..996 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1110..1180 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 64..65 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 224..225 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 224 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 248..251 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 257..259 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 275 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 332..334 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 337..340 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT MOD_RES 920 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" FT MOD_RES 963 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" FT MOD_RES 1013 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" FT MOD_RES 1049 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" FT MOD_RES 1121 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2ARP1" FT MOD_RES 1128 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFW1" SQ SEQUENCE 1409 AA; 156514 MW; EDFDB8AF4D0BED96 CRC64; MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESIVR KTGSYIYEEF MPTDGTDVKV YAVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM EKLVARKVCV AFRQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY GHFSGINRKV QSTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DELAPTRSTS LLNSMTVIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGAAEL LRLSKALADV VIPQEYGISR EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLESH VHSLLSVFRY GGLLDETQDA QWQRALDYLS AISELNYMTQ IVIMLYEDNT QDPLSEERFH VELHFSPGVK GVEEEGSAPA GCGFRPASSE NEEMKTNEGS MENLCPGKAS DEPDRALQTS PQPPEGPGLP RRSPLIRNRK AGSMEVLSET SSSRPGGYRL FSSSRPPTEM KQSGLGSQCT GLFSTTVLGG SFSAPNLQDY ARSHGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGF EGCSMVPTIY PLETLHNALS LHQVSEFLSR VCQRHTDAQA QASAALFDSM HSSQASDNPF SPPRTLHSPP LQLQQRSEKP PWYSSGPSST VSSAGPSSPT TVDGNSQFGF SDQPSLNSHV AEEHQGLGLL LETPGSGAQE LSIEGEQELF EPNQSPQVPP VETSQPYEEV SQPCQEVPDI SQPCQDISEA LSQPCQEVPD ISQQCQENHD NGNHTCQEVP HISQPCQKSS QLCQKVSEEV CQLCLENSEE VSQPCQGVSV EVGKLVHKFH VGVGSLVQET LVEVGSPAEE IPEEVIQPYQ GFSVEVGRLA QEASAINLLS QGIPEIDKPS QEFPEEIDLQ AQEVPEEIN //