[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Intestine; DOI=10.1016/0167-4781(91)90176-M; PubMed=1859839 [NCBI, ExPASy, EBI, Israel, Japan] Payne R.M., Haas R.C., Strauss A.W.; "Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes."; Biochim. Biophys. Acta 1089:352-361(1991).
[2]	PROTEIN SEQUENCE OF 40-56, AND TISSUE SPECIFICITY. PubMed=1939264 [NCBI, ExPASy, EBI, Israel, Japan] Friedman D.L., Perryman M.B.; "Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney."; J. Biol. Chem. 266:22404-22410(1991).
[3]	PROTEIN SEQUENCE OF 152-158; 191-200; 258-270 AND 311-326, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.

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: 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.
MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X59737; CAA42415.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17189; S17189.

UniGene

Rn.155589

3D structure databases

HSSP

P12532; 1QK1. [HSSP ENTRY / PDB]

P25809; 47-413.

PTM databases

P25809; -.

Organism-specific databases

RGD

61976; Ckmt1.

Gene expression databases

ArrayExpress

P25809; -.

GermOnline

ENSRNOG00000014573; Rattus norvegicus.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004111;	Molecular function: creatine kinase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.

PANTHER

PTHR11547; ATP-gua_Ptrans; 1.

Pfam

PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.

PROSITE

PS00112; GUANIDO_KINASE; 1.

BLOCKS

P25809.

Genome annotation databases

Ensembl

ENSRNOG00000014573; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P25809; -.

Other

ProtoNet

P25809.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion.`
`CHAIN`	`40 418`	`379`	`Creatine kinase, ubiquitous mitochondrial.`	`PRO_0000016592`
`NP_BIND`	`162 166`	`5`	`ATP (By similarity).`
`NP_BIND`	`354 359`	`6`	`ATP (By similarity).`
`REGION`	`40 64`	`25`	`Cardiolipin-binding (By similarity).`
`ACT_SITE`	`317 317`		`By similarity.`
`BINDING`	`225 225`		`ATP (By similarity).`
`BINDING`	`326 326`		`ATP (By similarity).`
`BINDING`	`369 369`		`ATP (By similarity).`
`MOD_RES`	`154 154`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47029 Da [This is the MW of the unprocessed precursor]

CRC64: 468339C52E4232D5 [This is a checksum on the sequence]

        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

P25809 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools