Q9VR59 (VIP1_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase EC=2.7.4.21 EC=2.7.4.24 Alternative name(s): InsP6 and PP-IP5 kinase | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Reference proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › ![]() |
Protein attributes
| Sequence length | 1696 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Bifunctional inositol kinase that acts in concert with the IP6K kinases 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, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. 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 | |
| Sequence similarities | Belongs to the histidine acid phosphatase family. VIP1 subfamily. |
| Caution | Although related to histidine acid phosphatases, it lacks the conserved active sites, suggesting that it has no phosphatase activity. |
| RNA editing | Edited at positions 1093, 1117 and 1121. |
| Sequence caution | The sequence ABN49448.1 differs from that shown. Reason: Frameshift at position 735. |
Ontologies
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform I (identifier: Q9VR59-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform G (identifier: Q9VR59-3) The sequence of this isoform differs from the canonical sequence as follows: 1293-1300: LWPQDIVK → QYPTEPSI 1301-1696: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform H (identifier: Q9VR59-6) The sequence of this isoform differs from the canonical sequence as follows: 2-40: SYTELESGYQ...VGFYLGLQDG → EWTWFKDWWR...DDFCYCEVCM 266-266: D → DVYFS 1293-1305: LWPQDIVKAAEDE → RKCRKKSVVEWQC 1306-1696: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform J (identifier: Q9VR59-5) The sequence of this isoform differs from the canonical sequence as follows: 1090-1090: P → PATETAEDTS...PSCCTKTIAT 1293-1300: LWPQDIVK → QYPTEPSI 1301-1696: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform K (identifier: Q9VR59-7) The sequence of this isoform differs from the canonical sequence as follows: 1090-1090: P → PVSSPDFGDN...PSCCTKTIAT 1293-1300: LWPQDIVK → QYPTEPSI 1301-1696: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1696 | 1696 | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase | PRO_0000315697 | |||||
Regions | |||||||||
| Nucleotide binding | 260 – 263 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 269 – 271 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 344 – 346 | 3 | ATP By similarity | ||||||
| Region | 76 – 77 | 2 | Substrate binding By similarity | ||||||
| Region | 236 – 237 | 2 | Substrate binding By similarity | ||||||
| Region | 349 – 352 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 157 | 1 | ATP By similarity | ||||||
| Binding site | 210 | 1 | ATP By similarity | ||||||
| Binding site | 217 | 1 | ATP By similarity | ||||||
| Binding site | 236 | 1 | ATP By similarity | ||||||
| Binding site | 271 | 1 | Substrate By similarity | ||||||
| Binding site | 285 | 1 | Substrate By similarity | ||||||
| Binding site | 287 | 1 | ATP By similarity | ||||||
| Binding site | 332 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 974 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 1001 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 1060 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1255 | 1 | Phosphoserine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 2 – 40 | 39 | SYTEL…GLQDG → EWTWFKDWWRLKKLRSRHQR HKKKLQATAASAEAAVTASA FLAGSGCAESGGSQDPQTNR LHSLDAVPSDGTLARRRHGS RDSLRRNRLLQRQRRSQSAA VRSHRSHDDDDDGEYGPFNV SDYEDYGPNHGSDEESDDFC YCEVCM in isoform H. | VSP_030640 | |||||
| Alternative sequence | 266 | 1 | D → DVYFS in isoform H. | VSP_030641 | |||||
| Alternative sequence | 1090 | 1 | P → PATETAEDTSMDIQPKICIG KCAPGLLTPTVTTTDILKGI RDIAPTATQTSPPTFTPSTT TTTGAAAALFDNTATMSSNR PFTNQFQSIDPTSNDAPHQH HVHQHQYQHHRKTTTTIINN TLNENHTTATITNNTTTTPS CCTKTIAT in isoform J. | VSP_030643 | |||||
| Alternative sequence | 1090 | 1 | P → PVSSPDFGDNSRTRSSEFGE TCHARVGTASNSDGGGSHPR ADHRTAFQIRVTNSLSFFKI DSSTNELPLSDIDFSLHPPT PQCGPLSHKRFHILTMRRME SCDDGAELEQVRHLPQISPM ATNERPLSSCNCSSSAAQAH SHSKSLMDLAQAVVMTSPQE TGPNSEQGCDPTTAADVSVS SFDDDFQLSSSAPAILMSAH FGNRPVVASLSSMVHVTTSP SASTLQLCRDKDKALASGTS SAHSKATSNSCGQLSMAGSA PVVTENPFRFTVSSLGSAAT NTACFVGSFEPIEEQITSIV EVDSKPLQPEPQVVYNLPTV LITGTASSSELSTKLNSNIL PTVTNAFSAIDTEINDEIGI SKEVGIGTIRITNTHTPCNK ATVTRPDTKIAITTDPQTVT ATETAEDTSMDIQPKICIGK CAPGLLTPTVTTTDILKGIR DIAPTATQTSPPTFTPSTTT TTGAAAALFDNTATMSSNRP FTNQFQSIDPTSNDAPHQHH VHQHQYQHHRKTTTTIINNT LNENHTTATITNNTTTTPSC CTKTIAT in isoform K. | VSP_033593 | |||||
| Alternative sequence | 1293 – 1305 | 13 | LWPQD…AAEDE → RKCRKKSVVEWQC in isoform H. | VSP_030648 | |||||
| Alternative sequence | 1293 – 1300 | 8 | LWPQDIVK → QYPTEPSI in isoform G, isoform J and isoform K. | VSP_030649 | |||||
| Alternative sequence | 1301 – 1696 | 396 | Missing in isoform G, isoform J and isoform K. | VSP_030650 | |||||
| Alternative sequence | 1306 – 1696 | 391 | Missing in isoform H. | VSP_030651 | |||||
| Natural variant | 1093 | 1 | Q → R in RNA edited version. | ||||||
| Natural variant | 1117 | 1 | S → G in RNA edited version. | ||||||
| Natural variant | 1121 | 1 | Q → R in RNA edited version. | ||||||
Experimental info | |||||||||
| Sequence conflict | 329 | 1 | C → F in ABN49448. Ref.3 | ||||||
| Sequence conflict | 734 | 1 | K → KN in ABN49448. Ref.3 | ||||||
| Sequence conflict | 906 | 1 | Y → H in ABN49448. Ref.3 | ||||||
| Sequence conflict | 1092 | 1 | S → G in AAT94524. Ref.3 | ||||||
| Sequence conflict | 1116 | 1 | H → R in AAT94524. Ref.3 | ||||||
| Sequence conflict | 1124 | 1 | Y → C in AAT94524. Ref.3 | ||||||
| Sequence conflict | 1124 | 1 | Y → C in ABN49448. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. Venter J.C.Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley. |
| [2] | "Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley. |
| [3] | Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND H), RNA EDITING OF POSITIONS 1117 AND 1121. Strain: Berkeley. Tissue: Embryo and Head. |
| [4] | "RNA editing in Drosophila melanogaster: new targets and functional consequences." Stapleton M., Carlson J.W., Celniker S.E. RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract] Cited for: RNA EDITING OF POSITION 1093; 1117 AND 1121. |
| [5] | "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1060, MASS SPECTROMETRY. |
| [6] | "Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1001 AND SER-1255, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014298 Genomic DNA. Translation: AAN09569.2. AE014298 Genomic DNA. Translation: AAN09570.3. AE014298 Genomic DNA. Translation: AAN09571.2. AE014298 Genomic DNA. Translation: AAN09573.2. AE014298 Genomic DNA. Translation: ABW09458.2. BT015295 mRNA. Translation: AAT94524.1. BT030309 mRNA. Translation: ABN49448.1. Frameshift. |
| RefSeq | NP_001097041.2. NM_001103571.2. NP_788950.2. NM_176777.2. NP_788951.2. NM_176778.2. NP_788952.2. NM_176779.2. NP_788953.2. NM_176780.2. |
| UniGene | Dm.237. |
3D structure databases | |
| ProteinModelPortal | Q9VR59. |
| SMR | Q9VR59. Positions 66-383. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-21851N. |
| MINT | MINT-1002676. |
| STRING | 7227.FBpp0288801. |
Proteomic databases | |
| PaxDb | Q9VR59. |
| PRIDE | Q9VR59. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0299524; FBpp0288799; FBgn0027279. |
| GeneID | 33137. |
| KEGG | dme:Dmel_CG14616. |
Organism-specific databases | |
| FlyBase | FBgn0027279. l(1)G0196. |
Phylogenomic databases | |
| eggNOG | NOG245915. |
| GeneTree | ENSGT00390000009048. |
| InParanoid | Q9VR59. |
| KO | K13024. |
| OMA | DGFPLEK. |
| OrthoDB | EOG473N63. |
Gene expression databases | |
| Bgee | Q9VR59. |
Family and domain databases | |
| InterPro | IPR000560. His_Pase_superF_clade-2. [Graphical view] |
| Pfam | PF00328. His_Phos_2. 1 hit. [Graphical view] |
| PROSITE | PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 33137. |
| NextBio | 782108. |
Entry information
| Entry name | VIP1_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9VR59 Secondary accession number(s): A2VEZ0 Q8IQ24 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
