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Q5XHF8 (VIP2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. 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 2
EC=2.7.4.21
EC=2.7.4.24
Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 2
Histidine acid phosphatase domain-containing protein 1
InsP6 and PP-IP5 kinase 2
VIP1 homolog 2
Gene names
Name:ppip5k2
Synonyms:hisppd1, vip2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length1131 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 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 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown).

ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown).

Subcellular location

Cytoplasm › cytosol 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 – 11311131Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
PRO_0000315695

Regions

Nucleotide binding251 – 2544ATP By similarity
Nucleotide binding260 – 2623ATP By similarity
Nucleotide binding335 – 3373ATP By similarity
Region67 – 682Substrate binding By similarity
Region227 – 2282Substrate binding By similarity
Region340 – 3434Substrate binding By similarity
Region385 – 45672Polyphosphoinositide-binding domain By similarity

Sites

Binding site1481ATP By similarity
Binding site2011ATP By similarity
Binding site2081ATP By similarity
Binding site2271ATP By similarity
Binding site2621Substrate By similarity
Binding site2761Substrate By similarity
Binding site2781ATP By similarity
Binding site3231ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XHF8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 4ADD5D46EC308E46

FASTA1,131128,720
        10         20         30         40         50         60 
MSVSATENDV PRFFVGCEES DELLDQSKPE NLDNLYEHTE DEEDEEDDEY DSPPERQIVV 

        70         80         90        100        110        120 
GICAMAKKSK SKPMKEILER LSLFKYITVV IFEEEVILNE TVENWPLCDC LISFHSKGFL 

       130        140        150        160        170        180 
LDKAVAYAKL RNPFVINDLN LQYQIQDRRE VYRILTNEGI MLPRYAVLNR DPNKPEECNL 

       190        200        210        220        230        240 
IEGEDHVEVN GEIFQKPFVE KPVSAEDHNV YIYYPTSAGG GSQRLFRKIG SRSSVYSPES 

       250        260        270        280        290        300 
SVRKTGSYIY EEFMPTDGTD VKVYTVGPDY AHAEARKSPA LDGKVERDSE GKEVRYPVIL 

       310        320        330        340        350        360 
NAREKLIAWK VCLAFKQTVC GFDLLRASGQ SYVCDVNGFS FVKNSMKYYD DCAKILGNII 

       370        380        390        400        410        420 
MRELAPVFHI PWSIPLEAED IPIVPTTSGT KMELRCVIAV IRHGDRTPKQ KMKMEVRHQR 

       430        440        450        460        470        480 
FFDLFEKYHG YKTGKIKLKK PKQLQEVLDI ARQLLVELGQ NNDSEIEESK AKLEQLKTVL 

       490        500        510        520        530        540 
EMYGHFSGIN RKVQLTYLPH GCPKTSSEEE DCRREEPSLL LVLKWGGELT PAGRVQAEEL 

       550        560        570        580        590        600 
GRAFRCMYPG GQGDYAGFPG CGLLRLHSTY RHDLKIYASD EGRVQMTAAA FAKGLLALEG 

       610        620        630        640        650        660 
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHEI LQRDRDFSSE DFEKLSPTGS 

       670        680        690        700        710        720 
VSQIKSMHFI KNPVKTCDKV YSLIQSLTSQ IRQRMEDPKF ADIQLYHSET LELMLRRWSK 

       730        740        750        760        770        780 
LEKDFKTKNG RYDISKIPDI YDCIKYDVQH NCSLKLENTM ELYRLSKALA DIVIPQEYGI 

       790        800        810        820        830        840 
SRPEKLEIAK GYCTPLVRKI RSDLQRTQDD DTVNKLHPLY SRGVMSPERH VRTRLYFTSE 

       850        860        870        880        890        900 
SHVHSLLSIL RFGALCDETK DEQWKRAMDY LNVVSELNYM TQIVIMLYED PNKDVSSEER 

       910        920        930        940        950        960 
FHVELHFSPG AKGCEEDKNL PSGFGYRPAS QENESSKKHT HANDSDEDLG VCRRDEPDRA 

       970        980        990       1000       1010       1020 
LVMFKPMVSD PIHIHRKSPL PRSRKIGSVE VLSDNNSHLR TARLLEQKHI GLGFELYSMV 

      1030       1040       1050       1060       1070       1080 
PSICPLETLH NSLSLKQVDE FLSAVAAPSS DYQMDTPTAS PSTPGFYTYV GGRKISLNTY 

      1090       1100       1110       1120       1130 
TPTKILPPLF PVSTDVEMSD SVFQSCSSTS MVPGLAGSAD NTERNHQAQD D

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC084099 mRNA. Translation: AAH84099.1.
RefSeqNP_001088187.1. NM_001094718.1.
UniGeneXl.18971.

3D structure databases

ProteinModelPortalQ5XHF8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID495012.
KEGGxla:495012.

Organism-specific databases

CTD23262.
XenbaseXB-GENE-1000382. ppip5k2.

Phylogenomic databases

HOVERGENHBG108657.
KOK13024.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIP2_XENLA
AccessionPrimary (citable) accession number: Q5XHF8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: May 1, 2013
This is version 50 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

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