Reviewed,
UniProtKB/Swiss-Prot P25809 (KCRU_RAT)
Last modified
June 16, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Creatine kinase, ubiquitous mitochondrial EC=2.7.3.2 Alternative name(s): U-MtCK Acidic-type mitochondrial creatine kinase Short name=Mia-CK | ||||
| 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 | 418 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. |
| Catalytic activity | ATP + creatine = ADP + phosphocreatine. |
| Subunit structure | Exists as an octamer composed of four MTCK homodimers. |
| Subcellular location | Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. |
| Tissue specificity | In many tissues, with highest levels in brain gut and kidney. In the kidney localized primarily in the outer medulla in the thick ascending limb and distal convoluted tubule. Ref.2 |
| Miscellaneous | Mitochondrial creatine kinase binds cardiolipin. |
| Sequence similarities | Belongs to the ATP:guanido phosphotransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | phosphocreatine biosynthetic process Ref.1 Traceable author statement. Source: RGD |
| Cellular component | mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Ref.1Traceable author statement. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 39 | 39 | Mitochondrion Ref.2 | ||||||
| Chain | 40 – 418 | 379 | Creatine kinase, ubiquitous mitochondrial | PRO_0000016592 | |||||
Regions | |||||||||
| Nucleotide binding | 162 – 166 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 354 – 359 | 6 | ATP By similarity | ||||||
| Region | 40 – 64 | 25 | Cardiolipin-binding By similarity | ||||||
Sites | |||||||||
| Binding site | 225 | 1 | ATP By similarity | ||||||
| Binding site | 270 | 1 | ATP By similarity | ||||||
| Binding site | 326 | 1 | ATP By similarity | ||||||
| Binding site | 369 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 154 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | "Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes." Payne R.M., Haas R.C., Strauss A.W. Biochim. Biophys. Acta 1089:352-361(1991) [PubMed: 1859839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Intestine. |
| [2] | "Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney." Friedman D.L., Perryman M.B. J. Biol. Chem. 266:22404-22410(1991) [PubMed: 1939264] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-56, TISSUE SPECIFICITY. |
| [3] | Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 152-158; 191-200; 258-270 AND 311-326, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| X59737 mRNA. Translation: CAA42415.1. | |
| IPI | IPI00193445. |
| PIR | S17189. |
| UniGene | Rn.155589 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QK1 based on UniProtKB P12532. |
| SMR | P25809. Positions 47-413. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P25809. |
Proteomic databases | |
| PRIDE | P25809. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000014573. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 61976. Ckmt1. |
Phylogenomic databases | |
| HOVERGEN | P25809. |
Enzyme and pathway databases | |
| BRENDA | 2.7.3.2. 248. |
Gene expression databases | |
| ArrayExpress | P25809. |
| GermOnline | ENSRNOG00000014573. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000749. ATP-guanido_PTrfase. IPR014746. Gln_synth/guanido_kin_cat. [Graphical view] |
| Gene3D | G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit. G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit. |
| PANTHER | PTHR11547. ATP-gua_Ptrans. 1 hit. |
| Pfam | PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view] |
| PROSITE | PS00112. GUANIDO_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KCRU_RAT | ||||||||
| Accession | Primary (citable) accession number: P25809 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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