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P0C644 (VIP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.2

Catalytic activity

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

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. Ref.2

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. Ref.2

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 – 14341434Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
PRO_0000315691

Regions

Nucleotide binding250 – 2534ATP By similarity
Nucleotide binding259 – 2613ATP By similarity
Nucleotide binding334 – 3363ATP By similarity
Region66 – 672Substrate binding By similarity
Region226 – 2272Substrate binding By similarity
Region339 – 3424Substrate binding By similarity
Region384 – 45572Polyphosphoinositide-binding domain By similarity

Sites

Binding site1471ATP By similarity
Binding site2001ATP By similarity
Binding site2071ATP By similarity
Binding site2261ATP By similarity
Binding site2611Substrate By similarity
Binding site2751Substrate By similarity
Binding site2771ATP By similarity
Binding site3221ATP By similarity

Amino acid modifications

Modified residue11491Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C644 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A3C2C9C28B4EAB47

FASTA1,434159,619
        10         20         30         40         50         60 
MWSLTANEDE DESATAHFFL GAGDEGLGTC GIGMRTGESD SELLEDEEDE VPPEPQIIVG 

        70         80         90        100        110        120 
ICAMTKKSKS KPMTQILERL CRFDYLTVVI LGEDVILNEP VENWPPCHCL ISFHSKGFPL 

       130        140        150        160        170        180 
DKAVAYSKLR NPFLINDLTM QYYIQDRREV YRILQEEGID LPRYAVLNRD PACPEECNLI 

       190        200        210        220        230        240 
EGEDQVEVNG AVFPKPFVEK PVSAEDHNVY IYYPSSAGGG SQRLFRKIGS RSSVYSPESS 

       250        260        270        280        290        300 
VRKTGSYIYE EFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG KEVRYPVMLT 

       310        320        330        340        350        360 
AMEKLVARKV CVAFKQTVCG FDLLRANGHS FVCDVNGFSF VKNSMKYYDD CAKILGNTIM 

       370        380        390        400        410        420 
RELAPQFQIP WSIPTEAEDI PIVPTTSGTM MELRCVIAII RHGDRTPKQK MKMEVTHPRF 

       430        440        450        460        470        480 
FALFEKHGGY KTGKLKLKRP EQLQEVLDIT RLLLAELEKE PGAEIEEKTG KLEQLKSVLE 

       490        500        510        520        530        540 
MYGHFSGINR KVQLTYYPHG VKASSEGQDL QREPPAPSLL LVLKWGGELT PDGRVQAEEL 

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

       610        620        630        640        650        660 
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHHI LQQDAPFGPE DYDQLAPTGS 

       670        680        690        700        710        720 
TSLLNSMSVI QNPVKVCDQV FALIENLTHQ IRERMQDPSS VDLQLYHSET LELMLQRWSK 

       730        740        750        760        770        780 
LERDFRQKSG RYDISKIPDI YDCVKYDVQH NGSLGLQGTA ELLRLSKALA DVVIPQEYGI 

       790        800        810        820        830        840 
SREEKVEIAV GFCLPLLRKI LLDLQRTHED ESVNKLHPLY SRGVLSPGRH VRTRLYFTSE 

       850        860        870        880        890        900 
SHVHSLLSVF RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER 

       910        920        930        940        950        960 
FHVELHFSPG VKGVEEGSAP AGCGFRPASS ENEEMKTDPG SIENLCPAKP SDEPDRALQT 

       970        980        990       1000       1010       1020 
SPQPVEGTGL PRRSPLIRNR KAGSMEVLSE TSSSRPGGYR LFSSSRPPTE MKQSGLGSQC 

      1030       1040       1050       1060       1070       1080 
TGLFSTTVLG GSSSAPNLQD YARTHGKKLP PAGLKHRDEL LFVPAVKRFS VSFAKHPTNG 

      1090       1100       1110       1120       1130       1140 
FEGCSMVPTI YPLETLHNAL SLRQVSEFLT KVCQRHTDAH AQASAALFDS MHNHQASDNP 

      1150       1160       1170       1180       1190       1200 
FSPPRTLHSP PLQLRHRSEK PPWYSSGPSS TVSSAGPSSP TTVDGNSHFG FSDQSSVNTQ 

      1210       1220       1230       1240       1250       1260 
MIEEKQGLGL LQETPGDGTP EFHIELAEST QSPQEPPVEI SPPGSQDDTE VNQTCQEVPD 

      1270       1280       1290       1300       1310       1320 
TIQPCHDILE EIGQPNQEVP DISQLLLKNH DTATNTCQPC QASQLSKKVY EEICQLCQDN 

      1330       1340       1350       1360       1370       1380 
PEESNQLCQE VSVELGRMVH RFPVSIGSTT QETLMEIGRP TQEIPEEPCQ EFSEKVGMLT 

      1390       1400       1410       1420       1430 
QKASAISELS QDILETDNPS QELSEETDLQ AQEVSEEIDQ EPEVVDELSN EDIS 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress."
Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.
J. Biol. Chem. 282:30763-30775(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC116071 Genomic DNA. No translation available.
UniGeneRn.46305.

3D structure databases

ProteinModelPortalP0C644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000059430.

Proteomic databases

PaxDbP0C644.
PRIDEP0C644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1311552. rat.

Organism-specific databases

RGD1311552. Ppip5k1.

Phylogenomic databases

eggNOGNOG245915.
HOGENOMHOG000177917.
HOVERGENHBG108657.
InParanoidP0C644.
PhylomeDBP0C644.

Gene expression databases

GenevestigatorP0C644.

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.
[Graphical view]
ProtoNetSearch...

Other

PROP0C644.

Entry information

Entry nameVIP1_RAT
AccessionPrimary (citable) accession number: P0C644
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 49 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