ID VIP2_XENLA Reviewed; 1131 AA. AC Q5XHF8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 {ECO:0000250|UniProtKB:O43314}; DE EC=2.7.4.24 {ECO:0000250|UniProtKB:O43314}; 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 {ECO:0000250|UniProtKB:O43314}; Synonyms=hisppd1, vip2; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Oocyte; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-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. CC {ECO:0000250|UniProtKB:O43314}. 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:O43314}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; CC Evidence={ECO:0000250|UniProtKB:O43314}; 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:O43314}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; CC Evidence={ECO:0000250|UniProtKB:O43314}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:O43314}. 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:O43314}. 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; BC084099; AAH84099.1; -; mRNA. DR RefSeq; NP_001088187.1; NM_001094718.1. DR AlphaFoldDB; Q5XHF8; -. DR SMR; Q5XHF8; -. DR DNASU; 495012; -. DR AGR; Xenbase:XB-GENE-1000382; -. DR Xenbase; XB-GENE-1000382; ppip5k2.L. DR OrthoDB; 5476261at2759; -. DR Proteomes; UP000186698; Genome assembly. DR Bgee; 495012; Expressed in egg cell and 19 other cell types or tissues. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. 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: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:SF10; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 2; 1. DR Pfam; PF00328; His_Phos_2; 1. DR Pfam; PF18086; PPIP5K2_N; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..1131 FT /note="Inositol hexakisphosphate and diphosphoinositol- FT pentakisphosphate kinase 2" FT /id="PRO_0000315695" FT REGION 21..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 385..456 FT /note="Polyphosphoinositide-binding domain" FT /evidence="ECO:0000250|UniProtKB:O43314" FT REGION 912..951 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..35 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..52 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 932..951 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 67..68 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 148 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 201 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 227..228 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 227 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 251..254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 260..262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 276 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 278 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 323 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 335..337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O43314" FT BINDING 340..343 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O43314" SQ SEQUENCE 1131 AA; 128720 MW; 4ADD5D46EC308E46 CRC64; MSVSATENDV PRFFVGCEES DELLDQSKPE NLDNLYEHTE DEEDEEDDEY DSPPERQIVV GICAMAKKSK SKPMKEILER LSLFKYITVV IFEEEVILNE TVENWPLCDC LISFHSKGFL LDKAVAYAKL RNPFVINDLN LQYQIQDRRE VYRILTNEGI MLPRYAVLNR DPNKPEECNL IEGEDHVEVN GEIFQKPFVE KPVSAEDHNV YIYYPTSAGG GSQRLFRKIG SRSSVYSPES SVRKTGSYIY EEFMPTDGTD VKVYTVGPDY AHAEARKSPA LDGKVERDSE GKEVRYPVIL NAREKLIAWK VCLAFKQTVC GFDLLRASGQ SYVCDVNGFS FVKNSMKYYD DCAKILGNII MRELAPVFHI PWSIPLEAED IPIVPTTSGT KMELRCVIAV IRHGDRTPKQ KMKMEVRHQR FFDLFEKYHG YKTGKIKLKK PKQLQEVLDI ARQLLVELGQ NNDSEIEESK AKLEQLKTVL EMYGHFSGIN RKVQLTYLPH GCPKTSSEEE DCRREEPSLL LVLKWGGELT PAGRVQAEEL GRAFRCMYPG GQGDYAGFPG CGLLRLHSTY RHDLKIYASD EGRVQMTAAA FAKGLLALEG ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHEI LQRDRDFSSE DFEKLSPTGS VSQIKSMHFI KNPVKTCDKV YSLIQSLTSQ IRQRMEDPKF ADIQLYHSET LELMLRRWSK LEKDFKTKNG RYDISKIPDI YDCIKYDVQH NCSLKLENTM ELYRLSKALA DIVIPQEYGI SRPEKLEIAK GYCTPLVRKI RSDLQRTQDD DTVNKLHPLY SRGVMSPERH VRTRLYFTSE SHVHSLLSIL RFGALCDETK DEQWKRAMDY LNVVSELNYM TQIVIMLYED PNKDVSSEER FHVELHFSPG AKGCEEDKNL PSGFGYRPAS QENESSKKHT HANDSDEDLG VCRRDEPDRA LVMFKPMVSD PIHIHRKSPL PRSRKIGSVE VLSDNNSHLR TARLLEQKHI GLGFELYSMV PSICPLETLH NSLSLKQVDE FLSAVAAPSS DYQMDTPTAS PSTPGFYTYV GGRKISLNTY TPTKILPPLF PVSTDVEMSD SVFQSCSSTS MVPGLAGSAD NTERNHQAQD D //