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Q5RDF1 (VIP1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

EC=2.7.4.21
EC=2.7.4.24
Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 1
Histidine acid phosphatase domain-containing protein 2A
InsP6 and PP-IP5 kinase 1
VIP1 homolog
Gene names
Name:PPIP5K1
Synonyms:HISPPD2A, VIP1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1409 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.

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.

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.

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.

Subcellular location

Cytoplasmcytosol By similarity. Cell membrane By similarity. Note: Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway By similarity.

Domain

The polyphosphoinositide-binding domain mediates binding of PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity By similarity.

Sequence similarities

Belongs to the histidine acid phosphatase family. VIP1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14091409Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
PRO_0000315690

Regions

Nucleotide binding248 – 2514ATP By similarity
Nucleotide binding257 – 2593ATP By similarity
Nucleotide binding332 – 3343ATP By similarity
Region64 – 652Substrate binding By similarity
Region224 – 2252Substrate binding By similarity
Region337 – 3404Substrate binding By similarity
Region382 – 45372Polyphosphoinositide-binding domain By similarity

Sites

Binding site1451ATP By similarity
Binding site1981ATP By similarity
Binding site2051ATP By similarity
Binding site2241ATP By similarity
Binding site2591Substrate By similarity
Binding site2731Substrate By similarity
Binding site2751ATP By similarity
Binding site3201ATP By similarity

Amino acid modifications

Modified residue11281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RDF1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: EDFDB8AF4D0BED96

FASTA1,409156,514
        10         20         30         40         50         60 
MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC 

        70         80         90        100        110        120 
AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK 

       130        140        150        160        170        180 
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG 

       190        200        210        220        230        240 
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESIVR 

       250        260        270        280        290        300 
KTGSYIYEEF MPTDGTDVKV YAVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 

       310        320        330        340        350        360 
EKLVARKVCV AFRQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE 

       370        380        390        400        410        420 
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA 

       430        440        450        460        470        480 
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY 

       490        500        510        520        530        540 
GHFSGINRKV QSTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR 

       550        560        570        580        590        600 
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 

       610        620        630        640        650        660 
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DELAPTRSTS 

       670        680        690        700        710        720 
LLNSMTVIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE 

       730        740        750        760        770        780 
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGAAEL LRLSKALADV VIPQEYGISR 

       790        800        810        820        830        840 
EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLESH VHSLLSVFRY GGLLDETQDA 

       850        860        870        880        890        900 
QWQRALDYLS AISELNYMTQ IVIMLYEDNT QDPLSEERFH VELHFSPGVK GVEEEGSAPA 

       910        920        930        940        950        960 
GCGFRPASSE NEEMKTNEGS MENLCPGKAS DEPDRALQTS PQPPEGPGLP RRSPLIRNRK 

       970        980        990       1000       1010       1020 
AGSMEVLSET SSSRPGGYRL FSSSRPPTEM KQSGLGSQCT GLFSTTVLGG SFSAPNLQDY 

      1030       1040       1050       1060       1070       1080 
ARSHGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGF EGCSMVPTIY PLETLHNALS 

      1090       1100       1110       1120       1130       1140 
LHQVSEFLSR VCQRHTDAQA QASAALFDSM HSSQASDNPF SPPRTLHSPP LQLQQRSEKP 

      1150       1160       1170       1180       1190       1200 
PWYSSGPSST VSSAGPSSPT TVDGNSQFGF SDQPSLNSHV AEEHQGLGLL LETPGSGAQE 

      1210       1220       1230       1240       1250       1260 
LSIEGEQELF EPNQSPQVPP VETSQPYEEV SQPCQEVPDI SQPCQDISEA LSQPCQEVPD 

      1270       1280       1290       1300       1310       1320 
ISQQCQENHD NGNHTCQEVP HISQPCQKSS QLCQKVSEEV CQLCLENSEE VSQPCQGVSV 

      1330       1340       1350       1360       1370       1380 
EVGKLVHKFH VGVGSLVQET LVEVGSPAEE IPEEVIQPYQ GFSVEVGRLA QEASAINLLS 

      1390       1400 
QGIPEIDKPS QEFPEEIDLQ AQEVPEEIN 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857961 mRNA. Translation: CAH90206.1.
UniGenePab.17834.

3D structure databases

ProteinModelPortalQ5RDF1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000177917.
HOVERGENHBG108657.
InParanoidQ5RDF1.

Family and domain databases

Gene3D3.40.50.1240. 4 hits.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 3 hits.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIP1_PONAB
AccessionPrimary (citable) accession number: Q5RDF1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families