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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog)

 VIP1_PONAB              Reviewed;        1409 AA.
Q5RDF1;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
28-FEB-2018, entry version 67.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1;
EC=2.7.4.21;
EC=2.7.4.24;
AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
AltName: Full=InsP6 and PP-IP5 kinase 1;
AltName: Full=VIP1 homolog;
Name=PPIP5K1; Synonyms=HISPPD2A, VIP1;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the
diphosphate group-containing inositol pyrophosphates
diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and
(PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a
variety of cellular processes, including apoptosis, vesicle
trafficking, cytoskeletal dynamics, exocytosis, insulin signaling
and neutrophil activation. Phosphorylates inositol
hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5
which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4.
Alternatively, phosphorylates at position 1 or 3 PP-InsP5,
produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated
when cells are exposed to hyperosmotic stress.
{ECO:0000250|UniProtKB:Q6PFW1}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane
{ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma
membrane upon activation of the PtdIns 3-kinase pathway.
{ECO:0000250|UniProtKB:Q6PFW1}.
-!- DOMAIN: The C-terminal acid phosphatase-like domain binds
PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the
phosphatase domain of histidine acid phosphatases, it has no
phosphatase activity. {ECO:0000250|UniProtKB:Q6PFW1}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
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EMBL; CR857961; CAH90206.1; -; mRNA.
UniGene; Pab.17834; -.
ProteinModelPortal; Q5RDF1; -.
SMR; Q5RDF1; -.
STRING; 9601.ENSPPYP00000007270; -.
PRIDE; Q5RDF1; -.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
HOGENOM; HOG000177917; -.
HOVERGEN; HBG108657; -.
InParanoid; Q5RDF1; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
CDD; cd07061; HP_HAP_like; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR037446; His_Pase_VIP1.
InterPro; IPR029033; His_PPase_superfam.
PANTHER; PTHR12750; PTHR12750; 1.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 3.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 1409 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 1.
/FTId=PRO_0000315690.
NP_BIND 248 251 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 257 259 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 332 334 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 64 65 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 224 225 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 337 340 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 382 453 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:Q6PFW1}.
BINDING 145 145 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 198 198 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 205 205 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 224 224 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 259 259 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 273 273 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 275 275 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 320 320 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 963 963 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1013 1013 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1049 1049 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1121 1121 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARP1}.
MOD_RES 1128 1128 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
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


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