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P25809 (KCRU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase U-type, mitochondrial

EC=2.7.3.2
Alternative name(s):
Acidic-type mitochondrial creatine kinase
Short name=Mia-CK
Ubiquitous mitochondrial creatine kinase
Short name=U-MtCK
Gene names
Name:Ckmt1
Synonyms:Ckmt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Ref.2
Chain40 – 418379Creatine kinase U-type, mitochondrial
PRO_0000016592

Regions

Domain46 – 13287Phosphagen kinase N-terminal
Domain159 – 401243Phosphagen kinase C-terminal
Nucleotide binding162 – 1665ATP By similarity
Nucleotide binding354 – 3596ATP By similarity
Region40 – 6425Cardiolipin-binding By similarity

Sites

Binding site2251ATP By similarity
Binding site2701ATP By similarity
Binding site3261ATP By similarity
Binding site3691ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P25809 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 468339C52E4232D5

FASTA41847,029
        10         20         30         40         50         60 
MAGPFSRLLS ARPGLKLLAL AGAGSLAAGI LLRPESVRAA TGERRRLYPP SAEYPDLRKH 

        70         80         90        100        110        120 
NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA 

       130        140        150        160        170        180 
ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC 

       190        200        210        220        230        240 
TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG 

       250        260        270        280        290        300 
MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKKVEKLIQE 

       310        320        330        340        350        360 
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VKLPLLSKDS RFPKILENLR LQKRGTGGVD 

       370        380        390        400        410 
TPATADVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LEKGQDIRIP PPLVHGKH 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59737 mRNA. Translation: CAA42415.1.
PIRS17189.
UniGeneRn.155589.

3D structure databases

ProteinModelPortalP25809.
SMRP25809. Positions 40-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000044253.

PTM databases

PhosphoSiteP25809.

2D gel databases

World-2DPAGE0004:P25809.

Proteomic databases

PaxDbP25809.
PRIDEP25809.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:61976. rat.

Organism-specific databases

RGD61976. Ckmt1.

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP25809.
PhylomeDBP25809.

Gene expression databases

GenevestigatorP25809.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKCRU_RAT
AccessionPrimary (citable) accession number: P25809
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 106 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