VIP2_XENLA
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 03-AUG-2022, entry version 78.
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-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}.
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DR EMBL; BC084099; AAH84099.1; -; mRNA.
DR RefSeq; NP_001088187.1; NM_001094718.1.
DR AlphaFoldDB; Q5XHF8; -.
DR SMR; Q5XHF8; -.
DR DNASU; 495012; -.
DR GeneID; 495012; -.
DR CTD; 495012; -.
DR Xenbase; XB-GENE-1000382; ppip5k2.L.
DR OrthoDB; 93740at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 495012; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
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; 3.40.50.1240; -; 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; PTHR12750; 2.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF53254; SSF53254; 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
