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A7Z050 (VIP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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
Gene names
Name:PPIP5K1
Synonyms:HISPPD2A, VIP1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1477 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 – 14771477Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
PRO_0000315687

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 residue11481Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z050 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: DF692A0B30BB1EB4

FASTA1,477163,665
        10         20         30         40         50         60 
MWSLPASEGE SATAHFFLGA GDEGLGTRGL 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 SVYSPESSVR 

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

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

       370        380        390        400        410        420 
LAPQFQIPWS IPMEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFS 

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

       490        500        510        520        530        540 
GHFSGINRKV QLTYYPHGVK ASNEGQDTQR EALAPSLLLV 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 NQLAPTGSTS 

       670        680        690        700        710        720 
LLSSMAVIQN PVKVCDQVFD LIENLTHQIR ERMQDPKSVD LQLYHSETLE LMLQRWSKLE 

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

       790        800        810        820        830        840 
EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH 

       850        860        870        880        890        900 
VHSLLSVFRY GGLLDETKDT QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH 

       910        920        930        940        950        960 
VELHFSPGVK GVEEEGSAPT GCGFRPASSE NEERKADQGS VEDLCPGKAS DEPDRALQTS 

       970        980        990       1000       1010       1020 
PLPSEGPGLP KRSPLIRNRK AGSMEVLSET SSSRPGGHRL FSSSRPPTEM KQSGLGSQCT 

      1030       1040       1050       1060       1070       1080 
GLFSTTVLGG SSSAPNLQDY ARSQGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGF 

      1090       1100       1110       1120       1130       1140 
EGCSMVPTIY PLETLHNALS LRQVSEFLSR VCQRHTEAQA QASAALFDSM HSNQASDSPF 

      1150       1160       1170       1180       1190       1200 
SPPRTLHSPT LQLQQRSEKP PWYSSGPSST VSSAGPSSPT AVDGNCPFGF SDQPSVSSHV 

      1210       1220       1230       1240       1250       1260 
TEEYQGLGLL QEAPGSGAQE PPLEGQQEPF EQNQSPQEPP VETKKPCQEV AEEVSQPCQD 

      1270       1280       1290       1300       1310       1320 
IPEEVNQPCQ QVSDICQPCE ENHDDVDQTC QEVPQISQPC EDASQLYQKV SKEVCELCQN 

      1330       1340       1350       1360       1370       1380 
SEEVNQPCQG VPVEIGRLVH GFPVGVGGLA QEVLGEVGRP TQEIPEELSQ SCQEFSVDIG 

      1390       1400       1410       1420       1430       1440 
RLAQEASAIN LLSPDTPEVD NPPLEFPGEG ALQAQEVSEW VKQQQSYVVP ELIDQLSREE 

      1450       1460       1470 
VPQVQCPPSN ANPQSQSLAP DQNAPLPPAT CDSSFSH 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC153248 mRNA. Translation: AAI53249.1.
RefSeqNP_001098824.1. NM_001105354.1.
XP_005222243.1. XM_005222186.1.
UniGeneBt.27184.

3D structure databases

ProteinModelPortalA7Z050.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000018635.

Proteomic databases

PRIDEA7Z050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000018635; ENSBTAP00000018635; ENSBTAG00000014005.
GeneID510684.
KEGGbta:510684.

Organism-specific databases

CTD9677.

Phylogenomic databases

eggNOGNOG245915.
GeneTreeENSGT00390000009048.
HOGENOMHOG000177917.
HOVERGENHBG108657.
InParanoidA7Z050.
KOK13024.
OMAEEVSQPC.
OrthoDBEOG77M8MT.
TreeFamTF313594.

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...

Other

NextBio20869569.

Entry information

Entry nameVIP1_BOVIN
AccessionPrimary (citable) accession number: A7Z050
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: June 11, 2014
This is version 55 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