VIP2_PONAB
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 03-AUG-2022, entry version 80.
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 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. Required for
CC normal hearing. {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}.
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; CR857406; CAH89697.1; -; mRNA.
DR AlphaFoldDB; Q5REW0; -.
DR SMR; Q5REW0; -.
DR STRING; 9601.ENSPPYP00000017519; -.
DR PRIDE; Q5REW0; -.
DR eggNOG; KOG1057; Eukaryota.
DR InParanoid; Q5REW0; -.
DR Proteomes; UP000001595; Unplaced.
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; 1.
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; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1244
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase 2"
FT /id="PRO_0000315694"
FT REGION 371..442
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT REGION 899..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 237..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 246..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 321..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 326..329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
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
