Q80ZG2 (IP3KC_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Inositol-trisphosphate 3-kinase C EC=2.7.1.127 Alternative name(s): Inositol 1,4,5-trisphosphate 3-kinase C Short name=IP3 3-kinase C Short name=IP3K C Short name=InsP 3-kinase C | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 678 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate. Ref.1 |
| Catalytic activity | ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate. |
| Enzyme regulation | Activated by Ca2+/calmodulin. Inhibited by high concentrations of the substrate Ins(1,2,4)P3, and allosterically activated by the product Ins(1,3,4,5)P4. |
| Subcellular location | Nucleus. Cytoplasm. Note: Shuttles actively between nucleus and cytoplasm with both nuclear import and nuclear export activity. Ref.1 |
| Tissue specificity | Highly expressed in tongue epithelium, taste papilla, heart, brain and testis. Weakly expressed in lung, liver and kidney. Ref.1 |
| Sequence similarities | Belongs to the inositol phosphokinase (IPK) family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.2 µM for Ins(1,4,5)P3 Ref.1 KM=1.5 µM for Ins(2,4,5)P3 KM=33 µM for ATP |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Ligand | ATP-binding Calmodulin-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin bindingInferred from electronic annotation. Source: UniProtKB-KW inositol-1,4,5-trisphosphate 3-kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 678 | 678 | Inositol-trisphosphate 3-kinase C | PRO_0000234072 | |||||
Regions | |||||||||
| Nucleotide binding | 466 – 468 | 3 | ATP By similarity | ||||||
| Region | 318 – 326 | 9 | Nuclear export signal | ||||||
| Region | 502 – 508 | 7 | Substrate binding By similarity | ||||||
| Region | 504 – 512 | 9 | Calmodulin-binding By similarity | ||||||
| Region | 529 – 536 | 8 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 426 | 1 | ATP By similarity | ||||||
| Binding site | 479 | 1 | ATP By similarity | ||||||
| Binding site | 481 | 1 | Substrate By similarity | ||||||
| Binding site | 553 | 1 | ATP By similarity | ||||||
| Binding site | 633 | 1 | ATP By similarity | ||||||
| Binding site | 636 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 318 – 326 | 9 | Missing: No export in the cytoplasm. Ref.1 | ||||||
| Mutagenesis | 318 – 321 | 4 | LCPV → ACPA: No export in the cytoplasm. Ref.1 | ||||||
Sequences
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References
| [1] | "Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm." Nalaskowski M.M., Bertsch U., Fanick W., Stockebrand M.C., Schmale H., Mayr G.W. J. Biol. Chem. 278:19765-19776(2003) [PubMed: 12649294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF 318-LEU--VAL-321 AND 318-LEU--ILE-326. Strain: Wistar. Tissue: Circumvallate papilla. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY160770 mRNA. Translation: AAO20335.1. AJ440782 mRNA. Translation: CAD29464.1. |
| IPI | IPI00331949. |
| RefSeq | NP_835195.1. NM_178094.3. |
| UniGene | Rn.85907. |
3D structure databases | |
| ProteinModelPortal | Q80ZG2. |
| SMR | Q80ZG2. Positions 389-678. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000018696; ENSRNOP00000018696; ENSRNOG00000013945. |
| GeneID | 308451. |
| KEGG | rno:308451. |
| UCSC | NM_178094. rat. |
Organism-specific databases | |
| CTD | 80271. |
| RGD | 631336. Itpkc. |
Phylogenomic databases | |
| eggNOG | roNOG12623. |
| GeneTree | ENSGT00390000017438. |
| HOVERGEN | HBG081804. |
| InParanoid | Q80ZG2. |
| OMA | DNLWTHQ. |
| OrthoDB | EOG476JZS. |
| PhylomeDB | Q80ZG2. |
Gene expression databases | |
| ArrayExpress | Q80ZG2. |
| Genevestigator | Q80ZG2. |
| GermOnline | ENSRNOG00000013945. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR005522. IPK. [Graphical view] |
| PANTHER | PTHR12400. IPK. 1 hit. |
| Pfam | PF03770. IPK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 658916. |
Entry information
| Entry name | IP3KC_RAT | ||||||||
| Accession | Primary (citable) accession number: Q80ZG2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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