Reviewed,
UniProtKB/Swiss-Prot Q5XLD3 (KCRM_PIG)
Last modified
November 4, 2008.
Version 24.
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 M-type EC=2.7.3.2 Alternative name(s): Creatine kinase M chain M-CK | ||
| Gene names |
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| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 381 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript 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 By similarity. |
| Catalytic activity | ATP + creatine = ADP + phosphocreatine. |
| Subunit structure | Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain By similarity. |
| Sequence similarities | Belongs to the ATP:guanido phosphotransferase family. |
Ontologies
Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
Gene Ontology (GO) | |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine 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 – 381 | 381 | Creatine kinase M-type | PRO_0000211977 | |||||
Regions | |||||||||
| Nucleotide binding | 128 – 132 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 320 – 325 | 6 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 191 | 1 | ATP By similarity | ||||||
| Binding site | 236 | 1 | ATP By similarity | ||||||
| Binding site | 292 | 1 | ATP By similarity | ||||||
| Binding site | 335 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Molecular cloning and characterization of porcine CKM." Xu D.Q., Xiong Y.Z., Ling X.F., Lang J. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle. |
| [2] | "Cloning and sequence analysis of genomic structure and the proximal promoter region of porcine CKM gene." Ling X.F., Xiong Y.Z., Xu D.Q. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AY754869 mRNA. Translation: AAV28621.1. DQ153192 Genomic DNA. Translation: AAZ66747.1. | |
| RefSeq | NP_001123421.1. |
3D structure databases | |
| SMR | Q5XLD3. Positions 2-381. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 397264. |
Phylogenomic databases | |
| HOVERGEN | Q5XLD3. |
Family and domain databases | |
| InterPro | IPR000749. ATP-gua_Ptrans. 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 | KCRM_PIG | ||||||||
| Accession | Primary (citable) accession number: Q5XLD3 Secondary accession number(s): Q45EW9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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